AU2007342275B2 - Polypeptides and biosynthetic pathways for the production of stereoisomers of monatin and their precursors - Google Patents
Polypeptides and biosynthetic pathways for the production of stereoisomers of monatin and their precursors Download PDFInfo
- Publication number
- AU2007342275B2 AU2007342275B2 AU2007342275A AU2007342275A AU2007342275B2 AU 2007342275 B2 AU2007342275 B2 AU 2007342275B2 AU 2007342275 A AU2007342275 A AU 2007342275A AU 2007342275 A AU2007342275 A AU 2007342275A AU 2007342275 B2 AU2007342275 B2 AU 2007342275B2
- Authority
- AU
- Australia
- Prior art keywords
- monatin
- tryptophan
- racemase
- seq
- amino acid
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Ceased
Links
- RMLYXMMBIZLGAQ-HZMBPMFUSA-N (2s,4s)-4-amino-2-hydroxy-2-(1h-indol-3-ylmethyl)pentanedioic acid Chemical compound C1=CC=C2C(C[C@](O)(C[C@H](N)C(O)=O)C(O)=O)=CNC2=C1 RMLYXMMBIZLGAQ-HZMBPMFUSA-N 0.000 title claims abstract description 518
- RMLYXMMBIZLGAQ-UHFFFAOYSA-N (-)-monatin Natural products C1=CC=C2C(CC(O)(CC(N)C(O)=O)C(O)=O)=CNC2=C1 RMLYXMMBIZLGAQ-UHFFFAOYSA-N 0.000 title claims abstract description 513
- 238000004519 manufacturing process Methods 0.000 title claims abstract description 89
- 108090000765 processed proteins & peptides Proteins 0.000 title abstract description 38
- 102000004196 processed proteins & peptides Human genes 0.000 title abstract description 37
- 229920001184 polypeptide Polymers 0.000 title abstract description 34
- 230000006696 biosynthetic metabolic pathway Effects 0.000 title abstract description 23
- 239000002243 precursor Substances 0.000 title description 25
- 150000003839 salts Chemical class 0.000 claims abstract description 9
- 238000006243 chemical reaction Methods 0.000 claims description 274
- 102000004190 Enzymes Human genes 0.000 claims description 265
- 108090000790 Enzymes Proteins 0.000 claims description 264
- 230000000694 effects Effects 0.000 claims description 190
- 108010068561 Fructose-Bisphosphate Aldolase Proteins 0.000 claims description 132
- 102000001390 Fructose-Bisphosphate Aldolase Human genes 0.000 claims description 127
- QIVBCDIJIAJPQS-SECBINFHSA-N D-tryptophane Chemical compound C1=CC=C2C(C[C@@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-SECBINFHSA-N 0.000 claims description 125
- 229930182827 D-tryptophan Natural products 0.000 claims description 119
- 108090001066 Racemases and epimerases Proteins 0.000 claims description 105
- 102000004879 Racemases and epimerases Human genes 0.000 claims description 103
- 238000000034 method Methods 0.000 claims description 99
- 108090000340 Transaminases Proteins 0.000 claims description 80
- 230000035772 mutation Effects 0.000 claims description 68
- 102000014898 transaminase activity proteins Human genes 0.000 claims description 61
- 150000001413 amino acids Chemical group 0.000 claims description 60
- 150000007523 nucleic acids Chemical group 0.000 claims description 56
- 108091028043 Nucleic acid sequence Proteins 0.000 claims description 40
- 238000006467 substitution reaction Methods 0.000 claims description 24
- 239000012634 fragment Substances 0.000 claims description 19
- 241000589196 Sinorhizobium meliloti Species 0.000 claims description 16
- 241000193385 Geobacillus stearothermophilus Species 0.000 claims description 14
- 241000193830 Bacillus <bacterium> Species 0.000 claims description 12
- 241000193386 Lysinibacillus sphaericus Species 0.000 claims description 11
- 108010017192 4-hydroxy-4-methyl-2-oxoglutarate aldolase Proteins 0.000 claims description 10
- 241000006382 Bacillus halodurans Species 0.000 claims description 6
- 241000194108 Bacillus licheniformis Species 0.000 claims description 2
- 108050009223 Branched-chain aminotransferases Proteins 0.000 claims description 2
- 102000001967 Branched-chain aminotransferases Human genes 0.000 claims description 2
- 230000037361 pathway Effects 0.000 abstract description 56
- 230000015572 biosynthetic process Effects 0.000 abstract description 3
- 238000003786 synthesis reaction Methods 0.000 abstract description 3
- QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 description 327
- 229940088598 enzyme Drugs 0.000 description 263
- 229960004799 tryptophan Drugs 0.000 description 232
- 101710190868 Broad specificity amino acid racemase Proteins 0.000 description 165
- RSTKLPZEZYGQPY-UHFFFAOYSA-N 3-(indol-3-yl)pyruvic acid Chemical compound C1=CC=C2C(CC(=O)C(=O)O)=CNC2=C1 RSTKLPZEZYGQPY-UHFFFAOYSA-N 0.000 description 143
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 128
- 108090000623 proteins and genes Proteins 0.000 description 109
- 244000005700 microbiome Species 0.000 description 89
- 239000000758 substrate Substances 0.000 description 75
- 102000004169 proteins and genes Human genes 0.000 description 69
- 210000004027 cell Anatomy 0.000 description 67
- 235000018102 proteins Nutrition 0.000 description 67
- 235000001014 amino acid Nutrition 0.000 description 63
- 101710102786 ATP-dependent leucine adenylase Proteins 0.000 description 62
- 238000003556 assay Methods 0.000 description 60
- 229940024606 amino acid Drugs 0.000 description 59
- 229910052717 sulfur Inorganic materials 0.000 description 57
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 55
- 229960003767 alanine Drugs 0.000 description 54
- 108010073079 tryptophan racemase Proteins 0.000 description 53
- LWIHDJKSTIGBAC-UHFFFAOYSA-K tripotassium phosphate Chemical compound [K+].[K+].[K+].[O-]P([O-])([O-])=O LWIHDJKSTIGBAC-UHFFFAOYSA-K 0.000 description 50
- 241000589518 Comamonas testosteroni Species 0.000 description 49
- 239000000203 mixture Substances 0.000 description 45
- 229940076788 pyruvate Drugs 0.000 description 44
- 108010041525 Alanine racemase Proteins 0.000 description 43
- QNAYBMKLOCPYGJ-UWTATZPHSA-N L-Alanine Natural products C[C@@H](N)C(O)=O QNAYBMKLOCPYGJ-UWTATZPHSA-N 0.000 description 43
- LCTONWCANYUPML-UHFFFAOYSA-M Pyruvate Chemical compound CC(=O)C([O-])=O LCTONWCANYUPML-UHFFFAOYSA-M 0.000 description 43
- 230000001965 increasing effect Effects 0.000 description 42
- QNAYBMKLOCPYGJ-UHFFFAOYSA-N D-alpha-Ala Natural products CC([NH3+])C([O-])=O QNAYBMKLOCPYGJ-UHFFFAOYSA-N 0.000 description 41
- WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 0.000 description 39
- NGVDGCNFYWLIFO-UHFFFAOYSA-N pyridoxal 5'-phosphate Chemical compound CC1=NC=C(COP(O)(O)=O)C(C=O)=C1O NGVDGCNFYWLIFO-UHFFFAOYSA-N 0.000 description 36
- KPGXRSRHYNQIFN-UHFFFAOYSA-L 2-oxoglutarate(2-) Chemical compound [O-]C(=O)CCC(=O)C([O-])=O KPGXRSRHYNQIFN-UHFFFAOYSA-L 0.000 description 35
- 239000000047 product Substances 0.000 description 35
- 235000007682 pyridoxal 5'-phosphate Nutrition 0.000 description 35
- 239000011589 pyridoxal 5'-phosphate Substances 0.000 description 35
- 239000002609 medium Substances 0.000 description 33
- 239000013615 primer Substances 0.000 description 33
- 150000008574 D-amino acids Chemical class 0.000 description 32
- 239000000284 extract Substances 0.000 description 31
- 235000004279 alanine Nutrition 0.000 description 30
- 238000003752 polymerase chain reaction Methods 0.000 description 30
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 29
- 241000589776 Pseudomonas putida Species 0.000 description 29
- 230000002441 reversible effect Effects 0.000 description 29
- 230000008569 process Effects 0.000 description 28
- 230000014509 gene expression Effects 0.000 description 27
- 238000004458 analytical method Methods 0.000 description 26
- 102000039446 nucleic acids Human genes 0.000 description 26
- 108020004707 nucleic acids Proteins 0.000 description 26
- 150000008575 L-amino acids Chemical class 0.000 description 25
- 229910000160 potassium phosphate Inorganic materials 0.000 description 25
- 235000011009 potassium phosphates Nutrition 0.000 description 25
- 230000036961 partial effect Effects 0.000 description 24
- 238000002474 experimental method Methods 0.000 description 23
- 239000013612 plasmid Substances 0.000 description 23
- BDAGIHXWWSANSR-UHFFFAOYSA-N methanoic acid Natural products OC=O BDAGIHXWWSANSR-UHFFFAOYSA-N 0.000 description 22
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical group OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 description 21
- 241000588724 Escherichia coli Species 0.000 description 20
- 230000002210 biocatalytic effect Effects 0.000 description 20
- 238000002703 mutagenesis Methods 0.000 description 20
- 231100000350 mutagenesis Toxicity 0.000 description 20
- DAEPDZWVDSPTHF-UHFFFAOYSA-M sodium pyruvate Chemical compound [Na+].CC(=O)C([O-])=O DAEPDZWVDSPTHF-UHFFFAOYSA-M 0.000 description 20
- 241000320117 Pseudomonas putida KT2440 Species 0.000 description 19
- 239000000499 gel Substances 0.000 description 19
- 238000001727 in vivo Methods 0.000 description 19
- KHPXUQMNIQBQEV-UHFFFAOYSA-N oxaloacetic acid Chemical compound OC(=O)CC(=O)C(O)=O KHPXUQMNIQBQEV-UHFFFAOYSA-N 0.000 description 19
- 239000012071 phase Substances 0.000 description 19
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 19
- 102000003677 Aldehyde-Lyases Human genes 0.000 description 18
- 108090000072 Aldehyde-Lyases Proteins 0.000 description 18
- 229930195714 L-glutamate Natural products 0.000 description 18
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical group OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 17
- 229930195712 glutamate Natural products 0.000 description 17
- 229940049906 glutamate Drugs 0.000 description 17
- IFGCUJZIWBUILZ-UHFFFAOYSA-N sodium 2-[[2-[[hydroxy-(3,4,5-trihydroxy-6-methyloxan-2-yl)oxyphosphoryl]amino]-4-methylpentanoyl]amino]-3-(1H-indol-3-yl)propanoic acid Chemical compound [Na+].C=1NC2=CC=CC=C2C=1CC(C(O)=O)NC(=O)C(CC(C)C)NP(O)(=O)OC1OC(C)C(O)C(O)C1O IFGCUJZIWBUILZ-UHFFFAOYSA-N 0.000 description 17
- 230000007704 transition Effects 0.000 description 17
- 102000003929 Transaminases Human genes 0.000 description 16
- WHOOUMGHGSPMGR-UHFFFAOYSA-N indol-3-ylacetaldehyde Chemical compound C1=CC=C2C(CC=O)=CNC2=C1 WHOOUMGHGSPMGR-UHFFFAOYSA-N 0.000 description 16
- 238000001294 liquid chromatography-tandem mass spectrometry Methods 0.000 description 16
- 229960005190 phenylalanine Drugs 0.000 description 16
- 239000000126 substance Substances 0.000 description 16
- 108010003989 D-amino-acid oxidase Proteins 0.000 description 15
- 102000004674 D-amino-acid oxidase Human genes 0.000 description 15
- 239000000872 buffer Substances 0.000 description 15
- 238000000338 in vitro Methods 0.000 description 15
- 238000002552 multiple reaction monitoring Methods 0.000 description 15
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 description 15
- NEPLBHLFDJOJGP-BYPYZUCNSA-N (2s)-2-(5-fluoro-2,4-dinitroanilino)propanamide Chemical compound NC(=O)[C@H](C)NC1=CC(F)=C([N+]([O-])=O)C=C1[N+]([O-])=O NEPLBHLFDJOJGP-BYPYZUCNSA-N 0.000 description 14
- 230000000707 stereoselective effect Effects 0.000 description 14
- 108010008830 Amino Acid Isomerases Proteins 0.000 description 13
- 102000006534 Amino Acid Isomerases Human genes 0.000 description 13
- 229910052799 carbon Inorganic materials 0.000 description 13
- 238000005119 centrifugation Methods 0.000 description 13
- 230000000670 limiting effect Effects 0.000 description 13
- 239000008188 pellet Substances 0.000 description 13
- 238000002360 preparation method Methods 0.000 description 13
- 238000002741 site-directed mutagenesis Methods 0.000 description 13
- 229960004441 tyrosine Drugs 0.000 description 13
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 12
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 12
- 241000218903 Pseudomonas taetrolens Species 0.000 description 12
- -1 and in particular Proteins 0.000 description 12
- 238000011534 incubation Methods 0.000 description 12
- 238000000746 purification Methods 0.000 description 12
- 239000000523 sample Substances 0.000 description 12
- 231100000419 toxicity Toxicity 0.000 description 12
- 230000001988 toxicity Effects 0.000 description 12
- 238000005891 transamination reaction Methods 0.000 description 12
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 12
- OSWFIVFLDKOXQC-UHFFFAOYSA-N 4-(3-methoxyphenyl)aniline Chemical compound COC1=CC=CC(C=2C=CC(N)=CC=2)=C1 OSWFIVFLDKOXQC-UHFFFAOYSA-N 0.000 description 11
- 108010015382 Tryptophan transaminase Proteins 0.000 description 11
- 238000005273 aeration Methods 0.000 description 11
- 239000006227 byproduct Substances 0.000 description 11
- 238000010367 cloning Methods 0.000 description 11
- 238000001514 detection method Methods 0.000 description 11
- 235000019253 formic acid Nutrition 0.000 description 11
- 230000012010 growth Effects 0.000 description 11
- BPHPUYQFMNQIOC-NXRLNHOXSA-N isopropyl beta-D-thiogalactopyranoside Chemical compound CC(C)S[C@@H]1O[C@H](CO)[C@H](O)[C@H](O)[C@H]1O BPHPUYQFMNQIOC-NXRLNHOXSA-N 0.000 description 11
- 239000008057 potassium phosphate buffer Substances 0.000 description 11
- 241000607516 Aeromonas caviae Species 0.000 description 10
- 235000014469 Bacillus subtilis Nutrition 0.000 description 10
- 108010078791 Carrier Proteins Proteins 0.000 description 10
- 229930195713 D-glutamate Natural products 0.000 description 10
- WHUUTDBJXJRKMK-GSVOUGTGSA-N D-glutamic acid Chemical compound OC(=O)[C@H](N)CCC(O)=O WHUUTDBJXJRKMK-GSVOUGTGSA-N 0.000 description 10
- 241000589516 Pseudomonas Species 0.000 description 10
- 230000001413 cellular effect Effects 0.000 description 10
- 150000001875 compounds Chemical class 0.000 description 10
- 239000000543 intermediate Substances 0.000 description 10
- 150000002500 ions Chemical class 0.000 description 10
- 229940054269 sodium pyruvate Drugs 0.000 description 10
- 239000007858 starting material Substances 0.000 description 10
- 239000013598 vector Substances 0.000 description 10
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 10
- 108050004635 D-amino acid aminotransferases Proteins 0.000 description 9
- 108700016167 Glutamate racemases Proteins 0.000 description 9
- 102000003939 Membrane transport proteins Human genes 0.000 description 9
- 108090000301 Membrane transport proteins Proteins 0.000 description 9
- 239000000370 acceptor Substances 0.000 description 9
- 125000003275 alpha amino acid group Chemical group 0.000 description 9
- 229940009098 aspartate Drugs 0.000 description 9
- RAXXELZNTBOGNW-UHFFFAOYSA-N imidazole Natural products C1=CNC=N1 RAXXELZNTBOGNW-UHFFFAOYSA-N 0.000 description 9
- CURLTUGMZLYLDI-UHFFFAOYSA-N Carbon dioxide Chemical compound O=C=O CURLTUGMZLYLDI-UHFFFAOYSA-N 0.000 description 8
- MHAJPDPJQMAIIY-UHFFFAOYSA-N Hydrogen peroxide Chemical compound OO MHAJPDPJQMAIIY-UHFFFAOYSA-N 0.000 description 8
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 8
- 102220618242 Putative uncharacterized protein UNQ9370/PRO34162_Y354T_mutation Human genes 0.000 description 8
- DTQVDTLACAAQTR-UHFFFAOYSA-N Trifluoroacetic acid Chemical compound OC(=O)C(F)(F)F DTQVDTLACAAQTR-UHFFFAOYSA-N 0.000 description 8
- 238000001212 derivatisation Methods 0.000 description 8
- 239000003643 water by type Substances 0.000 description 8
- 101710201421 Aromatic amino acid transport protein AroP Proteins 0.000 description 7
- 108010005694 Aspartate 4-decarboxylase Proteins 0.000 description 7
- 244000063299 Bacillus subtilis Species 0.000 description 7
- 108010078895 D-Alanine Transaminase Proteins 0.000 description 7
- 108010019475 D-phenylglycine aminotransferase Proteins 0.000 description 7
- KDXKERNSBIXSRK-YFKPBYRVSA-N L-lysine Chemical group NCCCC[C@H](N)C(O)=O KDXKERNSBIXSRK-YFKPBYRVSA-N 0.000 description 7
- 108010034546 Serratia marcescens nuclease Proteins 0.000 description 7
- 239000002299 complementary DNA Substances 0.000 description 7
- 230000007423 decrease Effects 0.000 description 7
- 239000002773 nucleotide Substances 0.000 description 7
- 125000003729 nucleotide group Chemical group 0.000 description 7
- 230000006340 racemization Effects 0.000 description 7
- 239000011541 reaction mixture Substances 0.000 description 7
- DVLFYONBTKHTER-UHFFFAOYSA-N 3-(N-morpholino)propanesulfonic acid Chemical compound OS(=O)(=O)CCCN1CCOCC1 DVLFYONBTKHTER-UHFFFAOYSA-N 0.000 description 6
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 6
- 241000894006 Bacteria Species 0.000 description 6
- CKLJMWTZIZZHCS-UWTATZPHSA-N D-aspartic acid Chemical compound OC(=O)[C@H](N)CC(O)=O CKLJMWTZIZZHCS-UWTATZPHSA-N 0.000 description 6
- 241000196324 Embryophyta Species 0.000 description 6
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 6
- 108010008292 L-Amino Acid Oxidase Proteins 0.000 description 6
- 102000007070 L-amino-acid oxidase Human genes 0.000 description 6
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical group CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 6
- 235000002637 Nicotiana tabacum Nutrition 0.000 description 6
- 244000061176 Nicotiana tabacum Species 0.000 description 6
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 6
- 150000004716 alpha keto acids Chemical class 0.000 description 6
- AVKUERGKIZMTKX-NJBDSQKTSA-N ampicillin Chemical compound C1([C@@H](N)C(=O)N[C@H]2[C@H]3SC([C@@H](N3C2=O)C(O)=O)(C)C)=CC=CC=C1 AVKUERGKIZMTKX-NJBDSQKTSA-N 0.000 description 6
- 229960000723 ampicillin Drugs 0.000 description 6
- 101150010999 aroP gene Proteins 0.000 description 6
- 230000003247 decreasing effect Effects 0.000 description 6
- 238000004807 desolvation Methods 0.000 description 6
- 238000009826 distribution Methods 0.000 description 6
- 238000010828 elution Methods 0.000 description 6
- 238000000605 extraction Methods 0.000 description 6
- 239000007789 gas Substances 0.000 description 6
- 229930027917 kanamycin Natural products 0.000 description 6
- 229960000318 kanamycin Drugs 0.000 description 6
- SBUJHOSQTJFQJX-NOAMYHISSA-N kanamycin Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CN)O[C@@H]1O[C@H]1[C@H](O)[C@@H](O[C@@H]2[C@@H]([C@@H](N)[C@H](O)[C@@H](CO)O2)O)[C@H](N)C[C@@H]1N SBUJHOSQTJFQJX-NOAMYHISSA-N 0.000 description 6
- 229930182823 kanamycin A Natural products 0.000 description 6
- 238000005259 measurement Methods 0.000 description 6
- 230000007246 mechanism Effects 0.000 description 6
- 125000001360 methionine group Chemical group N[C@@H](CCSC)C(=O)* 0.000 description 6
- 230000004048 modification Effects 0.000 description 6
- 238000012986 modification Methods 0.000 description 6
- 231100000219 mutagenic Toxicity 0.000 description 6
- 230000003505 mutagenic effect Effects 0.000 description 6
- 102200125675 rs137852783 Human genes 0.000 description 6
- 230000032258 transport Effects 0.000 description 6
- 108700024136 Aspartate racemases Proteins 0.000 description 5
- 239000002028 Biomass Substances 0.000 description 5
- 235000019750 Crude protein Nutrition 0.000 description 5
- 101710180978 D-alanine aminotransferase Proteins 0.000 description 5
- FFEARJCKVFRZRR-SCSAIBSYSA-N D-methionine Chemical compound CSCC[C@@H](N)C(O)=O FFEARJCKVFRZRR-SCSAIBSYSA-N 0.000 description 5
- 229930182818 D-methionine Natural products 0.000 description 5
- ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical group OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 0.000 description 5
- AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical group CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 description 5
- 125000002707 L-tryptophyl group Chemical group [H]C1=C([H])C([H])=C2C(C([C@](N([H])[H])(C(=O)[*])[H])([H])[H])=C([H])N([H])C2=C1[H] 0.000 description 5
- 239000007993 MOPS buffer Substances 0.000 description 5
- 108020004511 Recombinant DNA Proteins 0.000 description 5
- 241000207197 Symbiobacterium thermophilum Species 0.000 description 5
- 238000005576 amination reaction Methods 0.000 description 5
- 125000003277 amino group Chemical group 0.000 description 5
- 239000012491 analyte Substances 0.000 description 5
- 238000005859 coupling reaction Methods 0.000 description 5
- 108020001507 fusion proteins Proteins 0.000 description 5
- 102000037865 fusion proteins Human genes 0.000 description 5
- 230000006698 induction Effects 0.000 description 5
- 238000011002 quantification Methods 0.000 description 5
- 239000011535 reaction buffer Substances 0.000 description 5
- 238000004064 recycling Methods 0.000 description 5
- 238000004366 reverse phase liquid chromatography Methods 0.000 description 5
- 229910052702 rhenium Inorganic materials 0.000 description 5
- 238000012216 screening Methods 0.000 description 5
- 238000000926 separation method Methods 0.000 description 5
- 230000009466 transformation Effects 0.000 description 5
- PKYCWFICOKSIHZ-UHFFFAOYSA-N 1-(3,7-dihydroxyphenoxazin-10-yl)ethanone Chemical compound OC1=CC=C2N(C(=O)C)C3=CC=C(O)C=C3OC2=C1 PKYCWFICOKSIHZ-UHFFFAOYSA-N 0.000 description 4
- SLWQCDYJBNGHQV-UHFFFAOYSA-N 2-hydroxy-2-(1h-indol-3-ylmethyl)-4-oxopentanedioic acid Chemical compound C1=CC=C2C(CC(O)(CC(=O)C(=O)O)C(O)=O)=CNC2=C1 SLWQCDYJBNGHQV-UHFFFAOYSA-N 0.000 description 4
- 241000607534 Aeromonas Species 0.000 description 4
- 101000798396 Bacillus licheniformis Phenylalanine racemase [ATP hydrolyzing] Proteins 0.000 description 4
- 101000742094 Bacillus subtilis (strain 168) ATP-dependent tyrosine adenylase 2 Proteins 0.000 description 4
- LJCWONGJFPCTTL-SSDOTTSWSA-N D-4-hydroxyphenylglycine Chemical compound [O-]C(=O)[C@H]([NH3+])C1=CC=C(O)C=C1 LJCWONGJFPCTTL-SSDOTTSWSA-N 0.000 description 4
- 108030001020 D-methionine-pyruvate transaminases Proteins 0.000 description 4
- 101000776102 Geobacillus stearothermophilus Alanine racemase Proteins 0.000 description 4
- 240000001929 Lactobacillus brevis Species 0.000 description 4
- 235000013957 Lactobacillus brevis Nutrition 0.000 description 4
- 101710163270 Nuclease Proteins 0.000 description 4
- 102000004316 Oxidoreductases Human genes 0.000 description 4
- 108090000854 Oxidoreductases Proteins 0.000 description 4
- 238000012300 Sequence Analysis Methods 0.000 description 4
- 241000209140 Triticum Species 0.000 description 4
- 241000607626 Vibrio cholerae Species 0.000 description 4
- 238000002835 absorbance Methods 0.000 description 4
- VZTDIZULWFCMLS-UHFFFAOYSA-N ammonium formate Chemical compound [NH4+].[O-]C=O VZTDIZULWFCMLS-UHFFFAOYSA-N 0.000 description 4
- 230000008901 benefit Effects 0.000 description 4
- 210000004556 brain Anatomy 0.000 description 4
- 238000011088 calibration curve Methods 0.000 description 4
- 239000001569 carbon dioxide Substances 0.000 description 4
- 229910002092 carbon dioxide Inorganic materials 0.000 description 4
- 230000006037 cell lysis Effects 0.000 description 4
- 239000003153 chemical reaction reagent Substances 0.000 description 4
- 230000001419 dependent effect Effects 0.000 description 4
- 238000011067 equilibration Methods 0.000 description 4
- 239000012737 fresh medium Substances 0.000 description 4
- 239000001963 growth medium Substances 0.000 description 4
- 230000014759 maintenance of location Effects 0.000 description 4
- 229930182817 methionine Natural products 0.000 description 4
- 229960004452 methionine Drugs 0.000 description 4
- 239000013642 negative control Substances 0.000 description 4
- 239000013641 positive control Substances 0.000 description 4
- 238000002731 protein assay Methods 0.000 description 4
- 239000000376 reactant Substances 0.000 description 4
- 230000004044 response Effects 0.000 description 4
- 239000007787 solid Substances 0.000 description 4
- 230000002269 spontaneous effect Effects 0.000 description 4
- 229940118696 vibrio cholerae Drugs 0.000 description 4
- 108010043797 4-alpha-glucanotransferase Proteins 0.000 description 3
- CSCPPACGZOOCGX-UHFFFAOYSA-N Acetone Chemical compound CC(C)=O CSCPPACGZOOCGX-UHFFFAOYSA-N 0.000 description 3
- WEVYAHXRMPXWCK-UHFFFAOYSA-N Acetonitrile Chemical compound CC#N WEVYAHXRMPXWCK-UHFFFAOYSA-N 0.000 description 3
- 241000607528 Aeromonas hydrophila Species 0.000 description 3
- 241000607522 Aeromonas sobria Species 0.000 description 3
- 241000607620 Aliivibrio fischeri Species 0.000 description 3
- 240000000662 Anethum graveolens Species 0.000 description 3
- 241000207207 Aquifex pyrophilus Species 0.000 description 3
- 241000203069 Archaea Species 0.000 description 3
- 108010003415 Aspartate Aminotransferases Proteins 0.000 description 3
- 241000193755 Bacillus cereus Species 0.000 description 3
- 241000194103 Bacillus pumilus Species 0.000 description 3
- 241001453380 Burkholderia Species 0.000 description 3
- 108030001081 D-amino-acid transaminases Proteins 0.000 description 3
- 102000053602 DNA Human genes 0.000 description 3
- 101710088194 Dehydrogenase Proteins 0.000 description 3
- 241001198387 Escherichia coli BL21(DE3) Species 0.000 description 3
- 241000206602 Eukaryota Species 0.000 description 3
- 102000008214 Glutamate decarboxylase Human genes 0.000 description 3
- 108091022930 Glutamate decarboxylase Proteins 0.000 description 3
- 101150026303 HEX1 gene Proteins 0.000 description 3
- 108050004645 Indole-3-pyruvate decarboxylases Proteins 0.000 description 3
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 3
- 241000186660 Lactobacillus Species 0.000 description 3
- 241000186840 Lactobacillus fermentum Species 0.000 description 3
- 240000000599 Lentinula edodes Species 0.000 description 3
- 235000001715 Lentinula edodes Nutrition 0.000 description 3
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 3
- 102000004317 Lyases Human genes 0.000 description 3
- 108090000856 Lyases Proteins 0.000 description 3
- 239000004472 Lysine Substances 0.000 description 3
- 241000191996 Pediococcus pentosaceus Species 0.000 description 3
- 241000589517 Pseudomonas aeruginosa Species 0.000 description 3
- 241001645955 Pseudomonas chlororaphis subsp. aureofaciens Species 0.000 description 3
- 241000589540 Pseudomonas fluorescens Species 0.000 description 3
- 241000589781 Pseudomonas oleovorans Species 0.000 description 3
- 241000293869 Salmonella enterica subsp. enterica serovar Typhimurium Species 0.000 description 3
- 241000237506 Scapharca Species 0.000 description 3
- 108010006152 Serine racemase Proteins 0.000 description 3
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 3
- 241000194017 Streptococcus Species 0.000 description 3
- 108020004566 Transfer RNA Proteins 0.000 description 3
- 235000021307 Triticum Nutrition 0.000 description 3
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Chemical group CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 description 3
- 108010047495 alanylglycine Proteins 0.000 description 3
- 238000013459 approach Methods 0.000 description 3
- 125000003118 aryl group Chemical group 0.000 description 3
- 210000004899 c-terminal region Anatomy 0.000 description 3
- 239000011203 carbon fibre reinforced carbon Substances 0.000 description 3
- 230000008859 change Effects 0.000 description 3
- 150000001793 charged compounds Chemical class 0.000 description 3
- 125000001309 chloro group Chemical group Cl* 0.000 description 3
- 230000000295 complement effect Effects 0.000 description 3
- 238000001962 electrophoresis Methods 0.000 description 3
- 238000002330 electrospray ionisation mass spectrometry Methods 0.000 description 3
- 238000000855 fermentation Methods 0.000 description 3
- 230000004151 fermentation Effects 0.000 description 3
- 230000002068 genetic effect Effects 0.000 description 3
- 108010037850 glycylvaline Proteins 0.000 description 3
- 239000001257 hydrogen Substances 0.000 description 3
- 229910052739 hydrogen Inorganic materials 0.000 description 3
- 230000005764 inhibitory process Effects 0.000 description 3
- 101150032117 ipdC gene Proteins 0.000 description 3
- 229960000310 isoleucine Drugs 0.000 description 3
- AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 description 3
- 229960003136 leucine Drugs 0.000 description 3
- 239000007788 liquid Substances 0.000 description 3
- 238000005457 optimization Methods 0.000 description 3
- 230000002018 overexpression Effects 0.000 description 3
- 150000003141 primary amines Chemical group 0.000 description 3
- 239000012508 resin bead Substances 0.000 description 3
- 108091008146 restriction endonucleases Proteins 0.000 description 3
- 230000028327 secretion Effects 0.000 description 3
- 238000012163 sequencing technique Methods 0.000 description 3
- 239000011780 sodium chloride Substances 0.000 description 3
- 239000000243 solution Substances 0.000 description 3
- 238000010561 standard procedure Methods 0.000 description 3
- 125000001424 substituent group Chemical group 0.000 description 3
- 239000006228 supernatant Substances 0.000 description 3
- 238000012360 testing method Methods 0.000 description 3
- 210000001519 tissue Anatomy 0.000 description 3
- MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical compound OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 description 2
- SLWQCDYJBNGHQV-CQSZACIVSA-N (2r)-2-hydroxy-2-(1h-indol-3-ylmethyl)-4-oxopentanedioic acid Chemical compound C1=CC=C2C(C[C@@](O)(CC(=O)C(=O)O)C(O)=O)=CNC2=C1 SLWQCDYJBNGHQV-CQSZACIVSA-N 0.000 description 2
- QGZKDVFQNNGYKY-UHFFFAOYSA-N Ammonia Chemical compound N QGZKDVFQNNGYKY-UHFFFAOYSA-N 0.000 description 2
- 241000192531 Anabaena sp. Species 0.000 description 2
- 102000004625 Aspartate Aminotransferases Human genes 0.000 description 2
- 229930192334 Auxin Natural products 0.000 description 2
- 235000016068 Berberis vulgaris Nutrition 0.000 description 2
- 241000335053 Beta vulgaris Species 0.000 description 2
- 241000255789 Bombyx mori Species 0.000 description 2
- 108090000489 Carboxy-Lyases Proteins 0.000 description 2
- 102000004031 Carboxy-Lyases Human genes 0.000 description 2
- 108091026890 Coding region Proteins 0.000 description 2
- 102000012410 DNA Ligases Human genes 0.000 description 2
- 108010061982 DNA Ligases Proteins 0.000 description 2
- 241000205236 Desulfurococcus Species 0.000 description 2
- 241000194030 Enterococcus gallinarum Species 0.000 description 2
- 241000626621 Geobacillus Species 0.000 description 2
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 2
- FZQLXNIMCPJVJE-YUMQZZPRSA-N Gly-Asp-Leu Chemical compound [H]NCC(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC(C)C)C(O)=O FZQLXNIMCPJVJE-YUMQZZPRSA-N 0.000 description 2
- UFHFLCQGNIYNRP-UHFFFAOYSA-N Hydrogen Chemical compound [H][H] UFHFLCQGNIYNRP-UHFFFAOYSA-N 0.000 description 2
- SIKJAQJRHWYJAI-UHFFFAOYSA-N Indole Chemical compound C1=CC=C2NC=CC2=C1 SIKJAQJRHWYJAI-UHFFFAOYSA-N 0.000 description 2
- 125000000241 L-isoleucino group Chemical group [H]OC(=O)[C@@]([H])(N([H])[*])[C@@](C([H])([H])[H])(C(C([H])([H])[H])([H])[H])[H] 0.000 description 2
- 239000006137 Luria-Bertani broth Substances 0.000 description 2
- 235000007688 Lycopersicon esculentum Nutrition 0.000 description 2
- 241000193459 Moorella thermoacetica Species 0.000 description 2
- 241000699666 Mus <mouse, genus> Species 0.000 description 2
- 229910019142 PO4 Inorganic materials 0.000 description 2
- 241000192001 Pediococcus Species 0.000 description 2
- 241001208362 Photobacterium profundum SS9 Species 0.000 description 2
- 241001646398 Pseudomonas chlororaphis Species 0.000 description 2
- 241000700159 Rattus Species 0.000 description 2
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 2
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 2
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 2
- 235000014680 Saccharomyces cerevisiae Nutrition 0.000 description 2
- 241000235347 Schizosaccharomyces pombe Species 0.000 description 2
- 241000299590 Sclerochiton ilicifolius Species 0.000 description 2
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 2
- 102100035717 Serine racemase Human genes 0.000 description 2
- UIIMBOGNXHQVGW-UHFFFAOYSA-M Sodium bicarbonate Chemical compound [Na+].OC([O-])=O UIIMBOGNXHQVGW-UHFFFAOYSA-M 0.000 description 2
- 240000003768 Solanum lycopersicum Species 0.000 description 2
- 241000205188 Thermococcus Species 0.000 description 2
- 244000098338 Triticum aestivum Species 0.000 description 2
- 108030006554 Tryptophan dehydrogenases Proteins 0.000 description 2
- 108030001089 Tryptophan-phenylpyruvate transaminases Proteins 0.000 description 2
- 241000607598 Vibrio Species 0.000 description 2
- 241000700605 Viruses Species 0.000 description 2
- 241000607734 Yersinia <bacteria> Species 0.000 description 2
- 238000007792 addition Methods 0.000 description 2
- 125000003158 alcohol group Chemical group 0.000 description 2
- 150000001299 aldehydes Chemical class 0.000 description 2
- 238000005882 aldol condensation reaction Methods 0.000 description 2
- 230000003321 amplification Effects 0.000 description 2
- 239000003242 anti bacterial agent Substances 0.000 description 2
- 229940088710 antibiotic agent Drugs 0.000 description 2
- 238000007845 assembly PCR Methods 0.000 description 2
- 239000002363 auxin Substances 0.000 description 2
- 101150103518 bar gene Proteins 0.000 description 2
- HUMNYLRZRPPJDN-UHFFFAOYSA-N benzaldehyde Chemical compound O=CC1=CC=CC=C1 HUMNYLRZRPPJDN-UHFFFAOYSA-N 0.000 description 2
- 239000012148 binding buffer Substances 0.000 description 2
- 238000005842 biochemical reaction Methods 0.000 description 2
- 230000003115 biocidal effect Effects 0.000 description 2
- 230000001851 biosynthetic effect Effects 0.000 description 2
- 230000003197 catalytic effect Effects 0.000 description 2
- 238000004587 chromatography analysis Methods 0.000 description 2
- 238000004440 column chromatography Methods 0.000 description 2
- 238000009833 condensation Methods 0.000 description 2
- 230000005494 condensation Effects 0.000 description 2
- 235000009508 confectionery Nutrition 0.000 description 2
- 239000013256 coordination polymer Substances 0.000 description 2
- 239000013078 crystal Substances 0.000 description 2
- 230000002950 deficient Effects 0.000 description 2
- 238000006731 degradation reaction Methods 0.000 description 2
- 238000011033 desalting Methods 0.000 description 2
- 239000012039 electrophile Substances 0.000 description 2
- 239000003480 eluent Substances 0.000 description 2
- 239000012149 elution buffer Substances 0.000 description 2
- 238000001952 enzyme assay Methods 0.000 description 2
- 239000013604 expression vector Substances 0.000 description 2
- 239000012467 final product Substances 0.000 description 2
- 238000001917 fluorescence detection Methods 0.000 description 2
- 230000006870 function Effects 0.000 description 2
- 230000004927 fusion Effects 0.000 description 2
- BTCSSZJGUNDROE-UHFFFAOYSA-N gamma-aminobutyric acid Chemical compound NCCCC(O)=O BTCSSZJGUNDROE-UHFFFAOYSA-N 0.000 description 2
- 239000008103 glucose Substances 0.000 description 2
- 235000001727 glucose Nutrition 0.000 description 2
- 125000000291 glutamic acid group Chemical group N[C@@H](CCC(O)=O)C(=O)* 0.000 description 2
- 229910052736 halogen Inorganic materials 0.000 description 2
- 150000002367 halogens Chemical class 0.000 description 2
- 125000002887 hydroxy group Chemical group [H]O* 0.000 description 2
- 230000000415 inactivating effect Effects 0.000 description 2
- 125000001041 indolyl group Chemical group 0.000 description 2
- 230000002401 inhibitory effect Effects 0.000 description 2
- 230000002427 irreversible effect Effects 0.000 description 2
- 238000002955 isolation Methods 0.000 description 2
- 150000004715 keto acids Chemical class 0.000 description 2
- 150000002596 lactones Chemical class 0.000 description 2
- 238000004811 liquid chromatography Methods 0.000 description 2
- 238000004895 liquid chromatography mass spectrometry Methods 0.000 description 2
- 239000011777 magnesium Substances 0.000 description 2
- 235000013615 non-nutritive sweetener Nutrition 0.000 description 2
- 238000003199 nucleic acid amplification method Methods 0.000 description 2
- 150000002894 organic compounds Chemical class 0.000 description 2
- 150000002994 phenylalanines Chemical class 0.000 description 2
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 2
- 239000010452 phosphate Substances 0.000 description 2
- 239000008363 phosphate buffer Substances 0.000 description 2
- 238000001742 protein purification Methods 0.000 description 2
- 238000002708 random mutagenesis Methods 0.000 description 2
- 230000003362 replicative effect Effects 0.000 description 2
- 238000011160 research Methods 0.000 description 2
- 102220094405 rs876659691 Human genes 0.000 description 2
- 238000002864 sequence alignment Methods 0.000 description 2
- 235000004400 serine Nutrition 0.000 description 2
- 239000011734 sodium Substances 0.000 description 2
- 229910052708 sodium Inorganic materials 0.000 description 2
- 238000004885 tandem mass spectrometry Methods 0.000 description 2
- 239000011573 trace mineral Substances 0.000 description 2
- 235000013619 trace mineral Nutrition 0.000 description 2
- 241000701161 unidentified adenovirus Species 0.000 description 2
- 241001529453 unidentified herpesvirus Species 0.000 description 2
- 241001430294 unidentified retrovirus Species 0.000 description 2
- 229940088594 vitamin Drugs 0.000 description 2
- 229930003231 vitamin Natural products 0.000 description 2
- 235000013343 vitamin Nutrition 0.000 description 2
- 239000011782 vitamin Substances 0.000 description 2
- ONDYIUYXOSMHPE-PGMHMLKASA-N (2R)-2-amino-4-methylsulfanylbutanoic acid 2-oxopropanoic acid Chemical compound CC(=O)C(O)=O.CSCC[C@@H](N)C(O)=O ONDYIUYXOSMHPE-PGMHMLKASA-N 0.000 description 1
- BROUQASVDJNLCW-MYIOLCAUSA-N (2s)-2-(hydroxyamino)-4-(1h-indol-3-ylmethyl)pentanedioic acid Chemical compound C1=CC=C2C(CC(C[C@H](NO)C(O)=O)C(O)=O)=CNC2=C1 BROUQASVDJNLCW-MYIOLCAUSA-N 0.000 description 1
- RBCOYOYDYNXAFA-UHFFFAOYSA-L (5-hydroxy-4,6-dimethylpyridin-3-yl)methyl phosphate Chemical compound CC1=NC=C(COP([O-])([O-])=O)C(C)=C1O RBCOYOYDYNXAFA-UHFFFAOYSA-L 0.000 description 1
- QCHPKSFMDHPSNR-GSVOUGTGSA-N (R)-3-aminoisobutyric acid Chemical compound [NH3+]C[C@@H](C)C([O-])=O QCHPKSFMDHPSNR-GSVOUGTGSA-N 0.000 description 1
- 108030001082 (S)-3-amino-2-methylpropionate transaminases Proteins 0.000 description 1
- QCHPKSFMDHPSNR-VKHMYHEASA-N (S)-3-aminoisobutyric acid Chemical compound [NH3+]C[C@H](C)C([O-])=O QCHPKSFMDHPSNR-VKHMYHEASA-N 0.000 description 1
- PPINMSZPTPRQQB-NHCYSSNCSA-N 2-[[(2s)-1-[(2s)-2-[[(2s)-2-amino-3-methylbutanoyl]amino]propanoyl]pyrrolidine-2-carbonyl]amino]acetic acid Chemical compound CC(C)[C@H](N)C(=O)N[C@@H](C)C(=O)N1CCC[C@H]1C(=O)NCC(O)=O PPINMSZPTPRQQB-NHCYSSNCSA-N 0.000 description 1
- KPGXRSRHYNQIFN-UHFFFAOYSA-N 2-oxoglutaric acid Chemical compound OC(=O)CCC(=O)C(O)=O KPGXRSRHYNQIFN-UHFFFAOYSA-N 0.000 description 1
- FWMNVWWHGCHHJJ-SKKKGAJSSA-N 4-amino-1-[(2r)-6-amino-2-[[(2r)-2-[[(2r)-2-[[(2r)-2-amino-3-phenylpropanoyl]amino]-3-phenylpropanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]piperidine-4-carboxylic acid Chemical compound C([C@H](C(=O)N[C@H](CC(C)C)C(=O)N[C@H](CCCCN)C(=O)N1CCC(N)(CC1)C(O)=O)NC(=O)[C@H](N)CC=1C=CC=CC=1)C1=CC=CC=C1 FWMNVWWHGCHHJJ-SKKKGAJSSA-N 0.000 description 1
- LDCYZAJDBXYCGN-VIFPVBQESA-N 5-hydroxy-L-tryptophan Chemical compound C1=C(O)C=C2C(C[C@H](N)C(O)=O)=CNC2=C1 LDCYZAJDBXYCGN-VIFPVBQESA-N 0.000 description 1
- 229940000681 5-hydroxytryptophan Drugs 0.000 description 1
- FICLVQOYKYBXFN-SECBINFHSA-N 6-chloro-D-tryptophan zwitterion Chemical compound ClC1=CC=C2C(C[C@@H](N)C(O)=O)=CNC2=C1 FICLVQOYKYBXFN-SECBINFHSA-N 0.000 description 1
- ZCYVEMRRCGMTRW-UHFFFAOYSA-N 7553-56-2 Chemical group [I] ZCYVEMRRCGMTRW-UHFFFAOYSA-N 0.000 description 1
- QTBSBXVTEAMEQO-UHFFFAOYSA-M Acetate Chemical compound CC([O-])=O QTBSBXVTEAMEQO-UHFFFAOYSA-M 0.000 description 1
- 241000589291 Acinetobacter Species 0.000 description 1
- 229920001817 Agar Polymers 0.000 description 1
- 235000001674 Agaricus brunnescens Nutrition 0.000 description 1
- 241000589158 Agrobacterium Species 0.000 description 1
- DKJPOZOEBONHFS-ZLUOBGJFSA-N Ala-Ala-Asp Chemical compound C[C@H](N)C(=O)N[C@@H](C)C(=O)N[C@H](C(O)=O)CC(O)=O DKJPOZOEBONHFS-ZLUOBGJFSA-N 0.000 description 1
- RLMISHABBKUNFO-WHFBIAKZSA-N Ala-Ala-Gly Chemical compound C[C@H](N)C(=O)N[C@@H](C)C(=O)NCC(O)=O RLMISHABBKUNFO-WHFBIAKZSA-N 0.000 description 1
- DVWVZSJAYIJZFI-FXQIFTODSA-N Ala-Arg-Asn Chemical compound [H]N[C@@H](C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(N)=O)C(O)=O DVWVZSJAYIJZFI-FXQIFTODSA-N 0.000 description 1
- SVBXIUDNTRTKHE-CIUDSAMLSA-N Ala-Arg-Glu Chemical compound [H]N[C@@H](C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCC(O)=O)C(O)=O SVBXIUDNTRTKHE-CIUDSAMLSA-N 0.000 description 1
- LSLIRHLIUDVNBN-CIUDSAMLSA-N Ala-Asp-Lys Chemical compound C[C@H](N)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@H](C(O)=O)CCCCN LSLIRHLIUDVNBN-CIUDSAMLSA-N 0.000 description 1
- IOFVWPYSRSCWHI-JXUBOQSCSA-N Ala-Thr-Leu Chemical compound CC(C)C[C@@H](C(O)=O)NC(=O)[C@H]([C@@H](C)O)NC(=O)[C@H](C)N IOFVWPYSRSCWHI-JXUBOQSCSA-N 0.000 description 1
- 108010011170 Ala-Trp-Arg-His-Pro-Gln-Phe-Gly-Gly Proteins 0.000 description 1
- YJHKTAMKPGFJCT-NRPADANISA-N Ala-Val-Glu Chemical compound [H]N[C@@H](C)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CCC(O)=O)C(O)=O YJHKTAMKPGFJCT-NRPADANISA-N 0.000 description 1
- 102100036475 Alanine aminotransferase 1 Human genes 0.000 description 1
- 108010082126 Alanine transaminase Proteins 0.000 description 1
- 108030006859 Amino-acid racemases Proteins 0.000 description 1
- QGZKDVFQNNGYKY-UHFFFAOYSA-O Ammonium Chemical compound [NH4+] QGZKDVFQNNGYKY-UHFFFAOYSA-O 0.000 description 1
- USFZMSVCRYTOJT-UHFFFAOYSA-N Ammonium acetate Chemical compound N.CC(O)=O USFZMSVCRYTOJT-UHFFFAOYSA-N 0.000 description 1
- 239000005695 Ammonium acetate Substances 0.000 description 1
- 235000017060 Arachis glabrata Nutrition 0.000 description 1
- 244000105624 Arachis hypogaea Species 0.000 description 1
- 235000010777 Arachis hypogaea Nutrition 0.000 description 1
- 235000018262 Arachis monticola Nutrition 0.000 description 1
- 241000205046 Archaeoglobus Species 0.000 description 1
- SGYSTDWPNPKJPP-GUBZILKMSA-N Arg-Ala-Arg Chemical compound NC(=N)NCCC[C@H](N)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCNC(N)=N)C(O)=O SGYSTDWPNPKJPP-GUBZILKMSA-N 0.000 description 1
- UISQLSIBJKEJSS-GUBZILKMSA-N Arg-Arg-Ser Chemical compound NC(N)=NCCC[C@H](N)C(=O)N[C@@H](CCCN=C(N)N)C(=O)N[C@@H](CO)C(O)=O UISQLSIBJKEJSS-GUBZILKMSA-N 0.000 description 1
- NMRHDSAOIURTNT-RWMBFGLXSA-N Arg-Leu-Pro Chemical compound CC(C)C[C@@H](C(=O)N1CCC[C@@H]1C(=O)O)NC(=O)[C@H](CCCN=C(N)N)N NMRHDSAOIURTNT-RWMBFGLXSA-N 0.000 description 1
- BSYKSCBTTQKOJG-GUBZILKMSA-N Arg-Pro-Ala Chemical compound [H]N[C@@H](CCCNC(N)=N)C(=O)N1CCC[C@H]1C(=O)N[C@@H](C)C(O)=O BSYKSCBTTQKOJG-GUBZILKMSA-N 0.000 description 1
- ATABBWFGOHKROJ-GUBZILKMSA-N Arg-Pro-Ser Chemical compound [H]N[C@@H](CCCNC(N)=N)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CO)C(O)=O ATABBWFGOHKROJ-GUBZILKMSA-N 0.000 description 1
- UVTGNSWSRSCPLP-UHFFFAOYSA-N Arg-Tyr Natural products NC(CCNC(=N)N)C(=O)NC(Cc1ccc(O)cc1)C(=O)O UVTGNSWSRSCPLP-UHFFFAOYSA-N 0.000 description 1
- ICDDSTLEMLGSTB-GUBZILKMSA-N Asn-Met-Arg Chemical compound [H]N[C@@H](CC(N)=O)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCCNC(N)=N)C(O)=O ICDDSTLEMLGSTB-GUBZILKMSA-N 0.000 description 1
- ICTXFVKYAGQURS-UBHSHLNASA-N Asp-Asn-Trp Chemical compound [H]N[C@@H](CC(O)=O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC1=CNC2=C1C=CC=C2)C(O)=O ICTXFVKYAGQURS-UBHSHLNASA-N 0.000 description 1
- FANQWNCPNFEPGZ-WHFBIAKZSA-N Asp-Asp-Gly Chemical compound [H]N[C@@H](CC(O)=O)C(=O)N[C@@H](CC(O)=O)C(=O)NCC(O)=O FANQWNCPNFEPGZ-WHFBIAKZSA-N 0.000 description 1
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 description 1
- 108030003579 Aspartate 1-decarboxylases Proteins 0.000 description 1
- 102100034193 Aspartate aminotransferase, mitochondrial Human genes 0.000 description 1
- 108030002081 Aspartate transaminases Proteins 0.000 description 1
- 241000588807 Bordetella Species 0.000 description 1
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 1
- 238000009010 Bradford assay Methods 0.000 description 1
- 241000589173 Bradyrhizobium Species 0.000 description 1
- 235000011299 Brassica oleracea var botrytis Nutrition 0.000 description 1
- 240000003259 Brassica oleracea var. botrytis Species 0.000 description 1
- 241000186146 Brevibacterium Species 0.000 description 1
- WKBOTKDWSSQWDR-UHFFFAOYSA-N Bromine atom Chemical group [Br] WKBOTKDWSSQWDR-UHFFFAOYSA-N 0.000 description 1
- 241000589567 Brucella abortus Species 0.000 description 1
- 241000589876 Campylobacter Species 0.000 description 1
- 241000222120 Candida <Saccharomycetales> Species 0.000 description 1
- 241000863012 Caulobacter Species 0.000 description 1
- 240000001817 Cereus hexagonus Species 0.000 description 1
- 241000193403 Clostridium Species 0.000 description 1
- 241000193468 Clostridium perfringens Species 0.000 description 1
- 108020004705 Codon Proteins 0.000 description 1
- 108091035707 Consensus sequence Proteins 0.000 description 1
- VBPGTULCFGKGTF-ACZMJKKPSA-N Cys-Glu-Asp Chemical compound [H]N[C@@H](CS)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(O)=O)C(O)=O VBPGTULCFGKGTF-ACZMJKKPSA-N 0.000 description 1
- 108030001137 D-4-hydroxyphenylglycine transaminases Proteins 0.000 description 1
- 125000003941 D-tryptophan group Chemical group [H]C1=C([H])C([H])=C2C(C([C@@](N([H])[H])(C(=O)[*])[H])([H])[H])=C([H])N([H])C2=C1[H] 0.000 description 1
- 230000007023 DNA restriction-modification system Effects 0.000 description 1
- 238000001712 DNA sequencing Methods 0.000 description 1
- 241001509319 Desulfitobacterium Species 0.000 description 1
- 241001560102 Desulfotalea Species 0.000 description 1
- 241001228605 Desulfovibrio alaskensis G20 Species 0.000 description 1
- 241000500377 Desulfurococcus sp. Species 0.000 description 1
- 108700033083 EC 2.6.1.61 Proteins 0.000 description 1
- 108700034774 EC 4.99.-.- Proteins 0.000 description 1
- 241000194033 Enterococcus Species 0.000 description 1
- 241000194032 Enterococcus faecalis Species 0.000 description 1
- 239000004593 Epoxy Substances 0.000 description 1
- 241000588698 Erwinia Species 0.000 description 1
- 241000588722 Escherichia Species 0.000 description 1
- YPZRHBJKEMOYQH-UYBVJOGSSA-N FADH2 Chemical compound C1=NC2=C(N)N=CN=C2N1[C@@H]([C@H](O)[C@@H]1O)O[C@@H]1COP(O)(=O)OP(O)(=O)OC[C@@H](O)[C@@H](O)[C@@H](O)CN1C(NC(=O)NC2=O)=C2NC2=C1C=C(C)C(C)=C2 YPZRHBJKEMOYQH-UYBVJOGSSA-N 0.000 description 1
- 241001280345 Ferroplasma Species 0.000 description 1
- 241000233866 Fungi Species 0.000 description 1
- CXFUMJQFZVCETK-FXQIFTODSA-N Gln-Cys-Gln Chemical compound NC(=O)CC[C@H](N)C(=O)N[C@@H](CS)C(=O)N[C@@H](CCC(N)=O)C(O)=O CXFUMJQFZVCETK-FXQIFTODSA-N 0.000 description 1
- IKFZXRLDMYWNBU-YUMQZZPRSA-N Gln-Gly-Arg Chemical compound NC(=O)CC[C@H](N)C(=O)NCC(=O)N[C@H](C(O)=O)CCCN=C(N)N IKFZXRLDMYWNBU-YUMQZZPRSA-N 0.000 description 1
- JXFLPKSDLDEOQK-JHEQGTHGSA-N Gln-Gly-Thr Chemical compound C[C@@H](O)[C@@H](C(O)=O)NC(=O)CNC(=O)[C@@H](N)CCC(N)=O JXFLPKSDLDEOQK-JHEQGTHGSA-N 0.000 description 1
- CLSDNFWKGFJIBZ-YUMQZZPRSA-N Gln-Lys Chemical group NCCCC[C@@H](C(O)=O)NC(=O)[C@@H](N)CCC(N)=O CLSDNFWKGFJIBZ-YUMQZZPRSA-N 0.000 description 1
- UTKUTMJSWKKHEM-WDSKDSINSA-N Glu-Ala-Gly Chemical compound OC(=O)CNC(=O)[C@H](C)NC(=O)[C@@H](N)CCC(O)=O UTKUTMJSWKKHEM-WDSKDSINSA-N 0.000 description 1
- BCYGDJXHAGZNPQ-DCAQKATOSA-N Glu-Lys-Glu Chemical compound OC(=O)CC[C@H](N)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCC(O)=O)C(O)=O BCYGDJXHAGZNPQ-DCAQKATOSA-N 0.000 description 1
- 102000016901 Glutamate dehydrogenase Human genes 0.000 description 1
- 108700023156 Glutamate dehydrogenases Proteins 0.000 description 1
- PUUYVMYCMIWHFE-BQBZGAKWSA-N Gly-Ala-Arg Chemical compound NCC(=O)N[C@@H](C)C(=O)N[C@H](C(O)=O)CCCN=C(N)N PUUYVMYCMIWHFE-BQBZGAKWSA-N 0.000 description 1
- YYPFZVIXAVDHIK-IUCAKERBSA-N Gly-Glu-Leu Chemical compound CC(C)C[C@@H](C(O)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)CN YYPFZVIXAVDHIK-IUCAKERBSA-N 0.000 description 1
- NSTUFLGQJCOCDL-UWVGGRQHSA-N Gly-Leu-Arg Chemical compound NCC(=O)N[C@@H](CC(C)C)C(=O)N[C@H](C(O)=O)CCCN=C(N)N NSTUFLGQJCOCDL-UWVGGRQHSA-N 0.000 description 1
- YTSVAIMKVLZUDU-YUMQZZPRSA-N Gly-Leu-Asp Chemical compound [H]NCC(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(O)=O)C(O)=O YTSVAIMKVLZUDU-YUMQZZPRSA-N 0.000 description 1
- GGLIDLCEPDHEJO-BQBZGAKWSA-N Gly-Pro-Ala Chemical compound OC(=O)[C@H](C)NC(=O)[C@@H]1CCCN1C(=O)CN GGLIDLCEPDHEJO-BQBZGAKWSA-N 0.000 description 1
- OCRQUYDOYKCOQG-IRXDYDNUSA-N Gly-Tyr-Phe Chemical compound C([C@H](NC(=O)CN)C(=O)N[C@@H](CC=1C=CC=CC=1)C(O)=O)C1=CC=C(O)C=C1 OCRQUYDOYKCOQG-IRXDYDNUSA-N 0.000 description 1
- 241000589989 Helicobacter Species 0.000 description 1
- 241000647964 Helicobacter hepaticus ATCC 51449 Species 0.000 description 1
- HIAHVKLTHNOENC-HGNGGELXSA-N His-Glu-Ala Chemical compound [H]N[C@@H](CC1=CNC=N1)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](C)C(O)=O HIAHVKLTHNOENC-HGNGGELXSA-N 0.000 description 1
- FSOXZQBMPBQKGJ-QSFUFRPTSA-N His-Ile-Ala Chemical compound [O-]C(=O)[C@H](C)NC(=O)[C@H]([C@@H](C)CC)NC(=O)[C@@H]([NH3+])CC1=CN=CN1 FSOXZQBMPBQKGJ-QSFUFRPTSA-N 0.000 description 1
- 108091006054 His-tagged proteins Proteins 0.000 description 1
- NKVZTQVGUNLLQW-JBDRJPRFSA-N Ile-Ala-Ala Chemical compound CC[C@H](C)[C@@H](C(=O)N[C@@H](C)C(=O)N[C@@H](C)C(=O)O)N NKVZTQVGUNLLQW-JBDRJPRFSA-N 0.000 description 1
- CYHYBSGMHMHKOA-CIQUZCHMSA-N Ile-Ala-Thr Chemical compound CC[C@H](C)[C@@H](C(=O)N[C@@H](C)C(=O)N[C@@H]([C@@H](C)O)C(=O)O)N CYHYBSGMHMHKOA-CIQUZCHMSA-N 0.000 description 1
- RQZFWBLDTBDEOF-RNJOBUHISA-N Ile-Val-Pro Chemical compound CC[C@H](C)[C@@H](C(=O)N[C@@H](C(C)C)C(=O)N1CCC[C@@H]1C(=O)O)N RQZFWBLDTBDEOF-RNJOBUHISA-N 0.000 description 1
- DGAQECJNVWCQMB-PUAWFVPOSA-M Ilexoside XXIX Chemical compound C[C@@H]1CC[C@@]2(CC[C@@]3(C(=CC[C@H]4[C@]3(CC[C@@H]5[C@@]4(CC[C@@H](C5(C)C)OS(=O)(=O)[O-])C)C)[C@@H]2[C@]1(C)O)C)C(=O)O[C@H]6[C@@H]([C@H]([C@@H]([C@H](O6)CO)O)O)O.[Na+] DGAQECJNVWCQMB-PUAWFVPOSA-M 0.000 description 1
- 108010093096 Immobilized Enzymes Proteins 0.000 description 1
- 241000588748 Klebsiella Species 0.000 description 1
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 1
- DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 description 1
- 125000000010 L-asparaginyl group Chemical group O=C([*])[C@](N([H])[H])([H])C([H])([H])C(=O)N([H])[H] 0.000 description 1
- 125000003290 L-leucino group Chemical group [H]OC(=O)[C@@]([H])(N([H])[*])C([H])([H])C(C([H])([H])[H])([H])C([H])([H])[H] 0.000 description 1
- LRQKBLKVPFOOQJ-YFKPBYRVSA-N L-norleucine Chemical compound CCCC[C@H]([NH3+])C([O-])=O LRQKBLKVPFOOQJ-YFKPBYRVSA-N 0.000 description 1
- 241000222732 Leishmania major Species 0.000 description 1
- 241000880493 Leptailurus serval Species 0.000 description 1
- XBBKIIGCUMBKCO-JXUBOQSCSA-N Leu-Ala-Thr Chemical compound [H]N[C@@H](CC(C)C)C(=O)N[C@@H](C)C(=O)N[C@@H]([C@@H](C)O)C(O)=O XBBKIIGCUMBKCO-JXUBOQSCSA-N 0.000 description 1
- SEMUSFOBZGKBGW-YTFOTSKYSA-N Leu-Ile-Ile Chemical compound [H]N[C@@H](CC(C)C)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H]([C@@H](C)CC)C(O)=O SEMUSFOBZGKBGW-YTFOTSKYSA-N 0.000 description 1
- LFSQWRSVPNKJGP-WDCWCFNPSA-N Leu-Thr-Glu Chemical compound CC(C)C[C@H](N)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@H](C(O)=O)CCC(O)=O LFSQWRSVPNKJGP-WDCWCFNPSA-N 0.000 description 1
- PNPYKQFJGRFYJE-GUBZILKMSA-N Lys-Ala-Glu Chemical compound [H]N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)N[C@@H](CCC(O)=O)C(O)=O PNPYKQFJGRFYJE-GUBZILKMSA-N 0.000 description 1
- IUWMQCZOTYRXPL-ZPFDUUQYSA-N Lys-Ile-Asp Chemical compound [H]N[C@@H](CCCCN)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CC(O)=O)C(O)=O IUWMQCZOTYRXPL-ZPFDUUQYSA-N 0.000 description 1
- FYYHWMGAXLPEAU-UHFFFAOYSA-N Magnesium Chemical compound [Mg] FYYHWMGAXLPEAU-UHFFFAOYSA-N 0.000 description 1
- 241001293415 Mannheimia Species 0.000 description 1
- 241000219823 Medicago Species 0.000 description 1
- 241000970829 Mesorhizobium Species 0.000 description 1
- WXHHTBVYQOSYSL-FXQIFTODSA-N Met-Ala-Ser Chemical compound CSCC[C@H](N)C(=O)N[C@@H](C)C(=O)N[C@@H](CO)C(O)=O WXHHTBVYQOSYSL-FXQIFTODSA-N 0.000 description 1
- IIPHCNKHEZYSNE-DCAQKATOSA-N Met-Arg-Gln Chemical compound CSCC[C@H](N)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCC(N)=O)C(O)=O IIPHCNKHEZYSNE-DCAQKATOSA-N 0.000 description 1
- NLHSFJQUHGCWSD-PYJNHQTQSA-N Met-Ile-His Chemical compound N[C@@H](CCSC)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CC1=CNC=N1)C(O)=O NLHSFJQUHGCWSD-PYJNHQTQSA-N 0.000 description 1
- ZRACLHJYVRBJFC-ULQDDVLXSA-N Met-Lys-Phe Chemical compound CSCC[C@H](N)C(=O)N[C@@H](CCCCN)C(=O)N[C@H](C(O)=O)CC1=CC=CC=C1 ZRACLHJYVRBJFC-ULQDDVLXSA-N 0.000 description 1
- QLESZRANMSYLCZ-CYDGBPFRSA-N Met-Pro-Ile Chemical compound [H]N[C@@H](CCSC)C(=O)N1CCC[C@H]1C(=O)N[C@@H]([C@@H](C)CC)C(O)=O QLESZRANMSYLCZ-CYDGBPFRSA-N 0.000 description 1
- FZDOBWIKRQORAC-ULQDDVLXSA-N Met-Tyr-Leu Chemical compound CC(C)C[C@@H](C(=O)O)NC(=O)[C@H](CC1=CC=C(C=C1)O)NC(=O)[C@H](CCSC)N FZDOBWIKRQORAC-ULQDDVLXSA-N 0.000 description 1
- 241000203353 Methanococcus Species 0.000 description 1
- 241000205276 Methanosarcina Species 0.000 description 1
- BQVUABVGYYSDCJ-UHFFFAOYSA-N Nalpha-L-Leucyl-L-tryptophan Natural products C1=CC=C2C(CC(NC(=O)C(N)CC(C)C)C(O)=O)=CNC2=C1 BQVUABVGYYSDCJ-UHFFFAOYSA-N 0.000 description 1
- 108010084810 Neurotransmitter Transport Proteins Proteins 0.000 description 1
- 102000005665 Neurotransmitter Transport Proteins Human genes 0.000 description 1
- 239000004677 Nylon Substances 0.000 description 1
- 241001072230 Oceanobacillus Species 0.000 description 1
- 241000202223 Oenococcus Species 0.000 description 1
- 108700026244 Open Reading Frames Proteins 0.000 description 1
- 108091005804 Peptidases Proteins 0.000 description 1
- MGBRZXXGQBAULP-DRZSPHRISA-N Phe-Glu-Ala Chemical compound OC(=O)[C@H](C)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@@H](N)CC1=CC=CC=C1 MGBRZXXGQBAULP-DRZSPHRISA-N 0.000 description 1
- 241000607568 Photobacterium Species 0.000 description 1
- 241000512254 Polaribacter Species 0.000 description 1
- ULIWFCCJIOEHMU-BQBZGAKWSA-N Pro-Gly-Asp Chemical compound OC(=O)C[C@@H](C(O)=O)NC(=O)CNC(=O)[C@@H]1CCCN1 ULIWFCCJIOEHMU-BQBZGAKWSA-N 0.000 description 1
- RYJRPPUATSKNAY-STECZYCISA-N Pro-Ile-Tyr Chemical compound CC[C@H](C)[C@@H](C(=O)N[C@@H](CC1=CC=C(C=C1)O)C(=O)O)NC(=O)[C@@H]2CCCN2 RYJRPPUATSKNAY-STECZYCISA-N 0.000 description 1
- MTMJNKFZDQEVSY-BZSNNMDCSA-N Pro-Val-Trp Chemical compound [H]N1CCC[C@H]1C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CC1=CNC2=C1C=CC=C2)C(O)=O MTMJNKFZDQEVSY-BZSNNMDCSA-N 0.000 description 1
- 108010064465 Proline racemase Proteins 0.000 description 1
- 102000015220 Proline racemase Human genes 0.000 description 1
- 229940124158 Protease/peptidase inhibitor Drugs 0.000 description 1
- 241000589614 Pseudomonas stutzeri Species 0.000 description 1
- 241000205160 Pyrococcus Species 0.000 description 1
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 1
- 241000191043 Rhodobacter sphaeroides Species 0.000 description 1
- 241000607142 Salmonella Species 0.000 description 1
- 229920005654 Sephadex Polymers 0.000 description 1
- 239000012507 Sephadex™ Substances 0.000 description 1
- SRTCFKGBYBZRHA-ACZMJKKPSA-N Ser-Ala-Glu Chemical compound [H]N[C@@H](CO)C(=O)N[C@@H](C)C(=O)N[C@@H](CCC(O)=O)C(O)=O SRTCFKGBYBZRHA-ACZMJKKPSA-N 0.000 description 1
- HQTKVSCNCDLXSX-BQBZGAKWSA-N Ser-Arg-Gly Chemical compound [H]N[C@@H](CO)C(=O)N[C@@H](CCCNC(N)=N)C(=O)NCC(O)=O HQTKVSCNCDLXSX-BQBZGAKWSA-N 0.000 description 1
- QYSFWUIXDFJUDW-DCAQKATOSA-N Ser-Leu-Arg Chemical compound [H]N[C@@H](CO)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(O)=O QYSFWUIXDFJUDW-DCAQKATOSA-N 0.000 description 1
- GZSZPKSBVAOGIE-CIUDSAMLSA-N Ser-Lys-Ala Chemical compound [H]N[C@@H](CO)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(O)=O GZSZPKSBVAOGIE-CIUDSAMLSA-N 0.000 description 1
- PCMZJFMUYWIERL-ZKWXMUAHSA-N Ser-Val-Asn Chemical compound [H]N[C@@H](CO)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CC(N)=O)C(O)=O PCMZJFMUYWIERL-ZKWXMUAHSA-N 0.000 description 1
- 241000607768 Shigella Species 0.000 description 1
- 241001135312 Sinorhizobium Species 0.000 description 1
- VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 description 1
- 241000736131 Sphingomonas Species 0.000 description 1
- 108091006014 Strep-tagged proteins Proteins 0.000 description 1
- 101100370749 Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) trpC1 gene Proteins 0.000 description 1
- 101100046504 Symbiobacterium thermophilum (strain T / IAM 14863) tnaA2 gene Proteins 0.000 description 1
- 241000230504 Syntrophus sp. (in: Bacteria) Species 0.000 description 1
- 241000186339 Thermoanaerobacter Species 0.000 description 1
- 241001495444 Thermococcus sp. Species 0.000 description 1
- QQWNRERCGGZOKG-WEDXCCLWSA-N Thr-Gly-Leu Chemical compound [H]N[C@@H]([C@@H](C)O)C(=O)NCC(=O)N[C@@H](CC(C)C)C(O)=O QQWNRERCGGZOKG-WEDXCCLWSA-N 0.000 description 1
- XOWKUMFHEZLKLT-CIQUZCHMSA-N Thr-Ile-Ala Chemical compound [H]N[C@@H]([C@@H](C)O)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](C)C(O)=O XOWKUMFHEZLKLT-CIQUZCHMSA-N 0.000 description 1
- VUXIQSUQQYNLJP-XAVMHZPKSA-N Thr-Ser-Pro Chemical compound C[C@H]([C@@H](C(=O)N[C@@H](CO)C(=O)N1CCC[C@@H]1C(=O)O)N)O VUXIQSUQQYNLJP-XAVMHZPKSA-N 0.000 description 1
- 241000970911 Trichormus variabilis ATCC 29413 Species 0.000 description 1
- 239000007983 Tris buffer Substances 0.000 description 1
- 108010075344 Tryptophan synthase Proteins 0.000 description 1
- CTDPLKMBVALCGN-JSGCOSHPSA-N Tyr-Gly-Val Chemical compound [H]N[C@@H](CC1=CC=C(O)C=C1)C(=O)NCC(=O)N[C@@H](C(C)C)C(O)=O CTDPLKMBVALCGN-JSGCOSHPSA-N 0.000 description 1
- PQPWEALFTLKSEB-DZKIICNBSA-N Tyr-Val-Glu Chemical compound [H]N[C@@H](CC1=CC=C(O)C=C1)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CCC(O)=O)C(O)=O PQPWEALFTLKSEB-DZKIICNBSA-N 0.000 description 1
- 102100021869 Tyrosine aminotransferase Human genes 0.000 description 1
- 108010042606 Tyrosine transaminase Proteins 0.000 description 1
- 244000077923 Vaccinium vitis idaea Species 0.000 description 1
- 235000017606 Vaccinium vitis idaea Nutrition 0.000 description 1
- FZSPNKUFROZBSG-ZKWXMUAHSA-N Val-Ala-Asp Chemical compound CC(C)[C@H](N)C(=O)N[C@@H](C)C(=O)N[C@H](C(O)=O)CC(O)=O FZSPNKUFROZBSG-ZKWXMUAHSA-N 0.000 description 1
- NMANTMWGQZASQN-QXEWZRGKSA-N Val-Arg-Asp Chemical compound CC(C)[C@@H](C(=O)N[C@@H](CCCN=C(N)N)C(=O)N[C@@H](CC(=O)O)C(=O)O)N NMANTMWGQZASQN-QXEWZRGKSA-N 0.000 description 1
- CWSIBTLMMQLPPZ-FXQIFTODSA-N Val-Cys-Ala Chemical compound C[C@@H](C(=O)O)NC(=O)[C@H](CS)NC(=O)[C@H](C(C)C)N CWSIBTLMMQLPPZ-FXQIFTODSA-N 0.000 description 1
- BRPKEERLGYNCNC-NHCYSSNCSA-N Val-Glu-Arg Chemical compound CC(C)[C@H](N)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@H](C(O)=O)CCCN=C(N)N BRPKEERLGYNCNC-NHCYSSNCSA-N 0.000 description 1
- JZWZACGUZVCQPS-RNJOBUHISA-N Val-Ile-Pro Chemical compound CC[C@H](C)[C@@H](C(=O)N1CCC[C@@H]1C(=O)O)NC(=O)[C@H](C(C)C)N JZWZACGUZVCQPS-RNJOBUHISA-N 0.000 description 1
- BTWMICVCQLKKNR-DCAQKATOSA-N Val-Leu-Ser Chemical compound CC(C)[C@H]([NH3+])C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C([O-])=O BTWMICVCQLKKNR-DCAQKATOSA-N 0.000 description 1
- IJGPOONOTBNTFS-GVXVVHGQSA-N Val-Lys-Glu Chemical compound [H]N[C@@H](C(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCC(O)=O)C(O)=O IJGPOONOTBNTFS-GVXVVHGQSA-N 0.000 description 1
- DIOSYUIWOQCXNR-ONGXEEELSA-N Val-Lys-Gly Chemical compound CC(C)[C@H](N)C(=O)N[C@@H](CCCCN)C(=O)NCC(O)=O DIOSYUIWOQCXNR-ONGXEEELSA-N 0.000 description 1
- LJSZPMSUYKKKCP-UBHSHLNASA-N Val-Phe-Ala Chemical compound CC(C)[C@H](N)C(=O)N[C@H](C(=O)N[C@@H](C)C(O)=O)CC1=CC=CC=C1 LJSZPMSUYKKKCP-UBHSHLNASA-N 0.000 description 1
- XBJKAZATRJBDCU-GUBZILKMSA-N Val-Pro-Ala Chemical compound CC(C)[C@H](N)C(=O)N1CCC[C@H]1C(=O)N[C@@H](C)C(O)=O XBJKAZATRJBDCU-GUBZILKMSA-N 0.000 description 1
- NHXZRXLFOBFMDM-AVGNSLFASA-N Val-Pro-Leu Chemical compound CC(C)C[C@@H](C(O)=O)NC(=O)[C@@H]1CCCN1C(=O)[C@@H](N)C(C)C NHXZRXLFOBFMDM-AVGNSLFASA-N 0.000 description 1
- BZDGLJPROOOUOZ-XGEHTFHBSA-N Val-Thr-Cys Chemical compound C[C@H]([C@@H](C(=O)N[C@@H](CS)C(=O)O)NC(=O)[C@H](C(C)C)N)O BZDGLJPROOOUOZ-XGEHTFHBSA-N 0.000 description 1
- MIAZWUMFUURQNP-YDHLFZDLSA-N Val-Tyr-Asn Chemical compound CC(C)[C@@H](C(=O)N[C@@H](CC1=CC=C(C=C1)O)C(=O)N[C@@H](CC(=O)N)C(=O)O)N MIAZWUMFUURQNP-YDHLFZDLSA-N 0.000 description 1
- JSOXWWFKRJKTMT-WOPDTQHZSA-N Val-Val-Pro Chemical compound CC(C)[C@@H](C(=O)N[C@@H](C(C)C)C(=O)N1CCC[C@@H]1C(=O)O)N JSOXWWFKRJKTMT-WOPDTQHZSA-N 0.000 description 1
- JVGDAEKKZKKZFO-RCWTZXSCSA-N Val-Val-Thr Chemical compound C[C@H]([C@@H](C(=O)O)NC(=O)[C@H](C(C)C)NC(=O)[C@H](C(C)C)N)O JVGDAEKKZKKZFO-RCWTZXSCSA-N 0.000 description 1
- 241000999854 Vibrio cholerae O1 biovar El Tor str. N16961 Species 0.000 description 1
- 241001253549 Vibrio fischeri ES114 Species 0.000 description 1
- 241000272506 Vibrio parahaemolyticus RIMD 2210633 Species 0.000 description 1
- 241000607265 Vibrio vulnificus Species 0.000 description 1
- 241000605941 Wolinella Species 0.000 description 1
- 241000589506 Xanthobacter Species 0.000 description 1
- 241000589634 Xanthomonas Species 0.000 description 1
- 241001117074 Yersinia pestis KIM10+ Species 0.000 description 1
- 241000607477 Yersinia pseudotuberculosis Species 0.000 description 1
- 241000588901 Zymomonas Species 0.000 description 1
- 238000001042 affinity chromatography Methods 0.000 description 1
- 239000008272 agar Substances 0.000 description 1
- 239000011543 agarose gel Substances 0.000 description 1
- 238000000246 agarose gel electrophoresis Methods 0.000 description 1
- 230000002776 aggregation Effects 0.000 description 1
- 238000004220 aggregation Methods 0.000 description 1
- 108010044940 alanylglutamine Proteins 0.000 description 1
- 108010070944 alanylhistidine Proteins 0.000 description 1
- KOSRFJWDECSPRO-UHFFFAOYSA-N alpha-L-glutamyl-L-glutamic acid Natural products OC(=O)CCC(N)C(=O)NC(CCC(O)=O)C(O)=O KOSRFJWDECSPRO-UHFFFAOYSA-N 0.000 description 1
- 125000000539 amino acid group Chemical group 0.000 description 1
- 229910021529 ammonia Inorganic materials 0.000 description 1
- 229940043376 ammonium acetate Drugs 0.000 description 1
- 235000019257 ammonium acetate Nutrition 0.000 description 1
- BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 description 1
- 229910052921 ammonium sulfate Inorganic materials 0.000 description 1
- 235000011130 ammonium sulphate Nutrition 0.000 description 1
- 238000000137 annealing Methods 0.000 description 1
- 239000012431 aqueous reaction media Substances 0.000 description 1
- 239000007864 aqueous solution Substances 0.000 description 1
- 108010052670 arginyl-glutamyl-glutamic acid Proteins 0.000 description 1
- 108010060035 arginylproline Proteins 0.000 description 1
- 235000009582 asparagine Nutrition 0.000 description 1
- 229960001230 asparagine Drugs 0.000 description 1
- 235000003704 aspartic acid Nutrition 0.000 description 1
- 150000001510 aspartic acids Chemical class 0.000 description 1
- 239000012131 assay buffer Substances 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- 238000004166 bioassay Methods 0.000 description 1
- 238000005422 blasting Methods 0.000 description 1
- 229940098773 bovine serum albumin Drugs 0.000 description 1
- 229940056450 brucella abortus Drugs 0.000 description 1
- 125000004432 carbon atom Chemical group C* 0.000 description 1
- CREMABGTGYGIQB-UHFFFAOYSA-N carbon carbon Chemical compound C.C CREMABGTGYGIQB-UHFFFAOYSA-N 0.000 description 1
- 125000002915 carbonyl group Chemical group [*:2]C([*:1])=O 0.000 description 1
- 150000001732 carboxylic acid derivatives Chemical class 0.000 description 1
- 230000006652 catabolic pathway Effects 0.000 description 1
- 230000015556 catabolic process Effects 0.000 description 1
- 238000006555 catalytic reaction Methods 0.000 description 1
- 238000004113 cell culture Methods 0.000 description 1
- 239000002738 chelating agent Substances 0.000 description 1
- 239000007795 chemical reaction product Substances 0.000 description 1
- 229960005091 chloramphenicol Drugs 0.000 description 1
- WIIZWVCIJKGZOK-RKDXNWHRSA-N chloramphenicol Chemical compound ClC(Cl)C(=O)N[C@H](CO)[C@H](O)C1=CC=C([N+]([O-])=O)C=C1 WIIZWVCIJKGZOK-RKDXNWHRSA-N 0.000 description 1
- 229910052801 chlorine Inorganic materials 0.000 description 1
- 238000013375 chromatographic separation Methods 0.000 description 1
- 238000003776 cleavage reaction Methods 0.000 description 1
- 238000004891 communication Methods 0.000 description 1
- 230000000052 comparative effect Effects 0.000 description 1
- 239000007859 condensation product Substances 0.000 description 1
- 238000012790 confirmation Methods 0.000 description 1
- 239000000470 constituent Substances 0.000 description 1
- 238000010276 construction Methods 0.000 description 1
- 239000000356 contaminant Substances 0.000 description 1
- 230000001276 controlling effect Effects 0.000 description 1
- 230000008878 coupling Effects 0.000 description 1
- 238000010168 coupling process Methods 0.000 description 1
- 239000000287 crude extract Substances 0.000 description 1
- 235000018417 cysteine Nutrition 0.000 description 1
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 1
- 101150111280 dadB gene Proteins 0.000 description 1
- 101150012893 dat gene Proteins 0.000 description 1
- 238000007872 degassing Methods 0.000 description 1
- 239000012483 derivatization solution Substances 0.000 description 1
- 108010054813 diprotin B Proteins 0.000 description 1
- 238000000132 electrospray ionisation Methods 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 230000002708 enhancing effect Effects 0.000 description 1
- 230000007613 environmental effect Effects 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 238000006911 enzymatic reaction Methods 0.000 description 1
- 238000006345 epimerization reaction Methods 0.000 description 1
- 229910052731 fluorine Inorganic materials 0.000 description 1
- 125000001153 fluoro group Chemical group F* 0.000 description 1
- 238000005194 fractionation Methods 0.000 description 1
- 238000010353 genetic engineering Methods 0.000 description 1
- 230000035784 germination Effects 0.000 description 1
- 235000013922 glutamic acid Nutrition 0.000 description 1
- 239000004220 glutamic acid Substances 0.000 description 1
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 1
- 229960002743 glutamine Drugs 0.000 description 1
- 108010042598 glutamyl-aspartyl-glycine Proteins 0.000 description 1
- 108010055341 glutamyl-glutamic acid Proteins 0.000 description 1
- 108010079547 glutamylmethionine Proteins 0.000 description 1
- 108010050848 glycylleucine Proteins 0.000 description 1
- PCHJSUWPFVWCPO-UHFFFAOYSA-N gold Chemical compound [Au] PCHJSUWPFVWCPO-UHFFFAOYSA-N 0.000 description 1
- 229910052737 gold Inorganic materials 0.000 description 1
- 239000010931 gold Substances 0.000 description 1
- 239000011544 gradient gel Substances 0.000 description 1
- 125000005843 halogen group Chemical group 0.000 description 1
- 238000004128 high performance liquid chromatography Methods 0.000 description 1
- 239000008123 high-intensity sweetener Substances 0.000 description 1
- 150000002431 hydrogen Chemical class 0.000 description 1
- 125000004435 hydrogen atom Chemical group [H]* 0.000 description 1
- 230000007062 hydrolysis Effects 0.000 description 1
- 238000006460 hydrolysis reaction Methods 0.000 description 1
- 230000002209 hydrophobic effect Effects 0.000 description 1
- 230000006872 improvement Effects 0.000 description 1
- PZOUSPYUWWUPPK-UHFFFAOYSA-N indole Natural products CC1=CC=CC2=C1C=CN2 PZOUSPYUWWUPPK-UHFFFAOYSA-N 0.000 description 1
- SEOVTRFCIGRIMH-UHFFFAOYSA-N indole-3-acetic acid Chemical compound C1=CC=C2C(CC(=O)O)=CNC2=C1 SEOVTRFCIGRIMH-UHFFFAOYSA-N 0.000 description 1
- RKJUIXBNRJVNHR-UHFFFAOYSA-N indolenine Natural products C1=CC=C2CC=NC2=C1 RKJUIXBNRJVNHR-UHFFFAOYSA-N 0.000 description 1
- 150000002475 indoles Chemical class 0.000 description 1
- 230000001939 inductive effect Effects 0.000 description 1
- 239000004615 ingredient Substances 0.000 description 1
- 230000002452 interceptive effect Effects 0.000 description 1
- 229910052740 iodine Inorganic materials 0.000 description 1
- 238000005342 ion exchange Methods 0.000 description 1
- 238000010829 isocratic elution Methods 0.000 description 1
- 125000001449 isopropyl group Chemical group [H]C([H])([H])C([H])(*)C([H])([H])[H] 0.000 description 1
- BTNMPGBKDVTSJY-UHFFFAOYSA-N keto-phenylpyruvic acid Chemical compound OC(=O)C(=O)CC1=CC=CC=C1 BTNMPGBKDVTSJY-UHFFFAOYSA-N 0.000 description 1
- 125000000468 ketone group Chemical group 0.000 description 1
- 229940039696 lactobacillus Drugs 0.000 description 1
- 108010083708 leucyl-aspartyl-valine Proteins 0.000 description 1
- 108010091871 leucylmethionine Proteins 0.000 description 1
- 229960003646 lysine Drugs 0.000 description 1
- 229910052749 magnesium Inorganic materials 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 239000011159 matrix material Substances 0.000 description 1
- IBIKHMZPHNKTHM-RDTXWAMCSA-N merck compound 25 Chemical compound C1C[C@@H](C(O)=O)[C@H](O)CN1C(C1=C(F)C=CC=C11)=NN1C(=O)C1=C(Cl)C=CC=C1C1CC1 IBIKHMZPHNKTHM-RDTXWAMCSA-N 0.000 description 1
- 108020004999 messenger RNA Proteins 0.000 description 1
- SYHGEUNFJIGTRX-UHFFFAOYSA-N methylenedioxypyrovalerone Chemical compound C=1C=C2OCOC2=CC=1C(=O)C(CCC)N1CCCC1 SYHGEUNFJIGTRX-UHFFFAOYSA-N 0.000 description 1
- 230000000813 microbial effect Effects 0.000 description 1
- 238000002156 mixing Methods 0.000 description 1
- 238000010369 molecular cloning Methods 0.000 description 1
- 239000003068 molecular probe Substances 0.000 description 1
- 101150047269 murI gene Proteins 0.000 description 1
- 238000006386 neutralization reaction Methods 0.000 description 1
- 238000001668 nucleic acid synthesis Methods 0.000 description 1
- 229920001778 nylon Polymers 0.000 description 1
- 230000003287 optical effect Effects 0.000 description 1
- 230000008723 osmotic stress Effects 0.000 description 1
- LDCYZAJDBXYCGN-UHFFFAOYSA-N oxitriptan Natural products C1=C(O)C=C2C(CC(N)C(O)=O)=CNC2=C1 LDCYZAJDBXYCGN-UHFFFAOYSA-N 0.000 description 1
- 238000010979 pH adjustment Methods 0.000 description 1
- QNGNSVIICDLXHT-UHFFFAOYSA-N para-ethylbenzaldehyde Natural products CCC1=CC=C(C=O)C=C1 QNGNSVIICDLXHT-UHFFFAOYSA-N 0.000 description 1
- 235000020232 peanut Nutrition 0.000 description 1
- 239000000137 peptide hydrolase inhibitor Substances 0.000 description 1
- 125000001997 phenyl group Chemical group [H]C1=C([H])C([H])=C(*)C([H])=C1[H] 0.000 description 1
- 108010078226 phenylalanine oxidase Proteins 0.000 description 1
- 108090000554 phenylalanine racemase (ATP-hydrolyzing) Proteins 0.000 description 1
- 230000035790 physiological processes and functions Effects 0.000 description 1
- 239000013600 plasmid vector Substances 0.000 description 1
- 238000001121 post-column derivatisation Methods 0.000 description 1
- 238000001556 precipitation Methods 0.000 description 1
- 108010004914 prolylarginine Proteins 0.000 description 1
- 108010029020 prolylglycine Proteins 0.000 description 1
- 239000012521 purified sample Substances 0.000 description 1
- 229960001327 pyridoxal phosphate Drugs 0.000 description 1
- 238000006268 reductive amination reaction Methods 0.000 description 1
- 239000011347 resin Substances 0.000 description 1
- 229920005989 resin Polymers 0.000 description 1
- 238000012552 review Methods 0.000 description 1
- 102200159068 rs201738967 Human genes 0.000 description 1
- 229920006395 saturated elastomer Polymers 0.000 description 1
- 230000007017 scission Effects 0.000 description 1
- 238000012764 semi-quantitative analysis Methods 0.000 description 1
- 239000001632 sodium acetate Substances 0.000 description 1
- 235000017281 sodium acetate Nutrition 0.000 description 1
- 239000007974 sodium acetate buffer Substances 0.000 description 1
- 235000017557 sodium bicarbonate Nutrition 0.000 description 1
- 229910000030 sodium bicarbonate Inorganic materials 0.000 description 1
- BEOOHQFXGBMRKU-UHFFFAOYSA-N sodium cyanoborohydride Chemical compound [Na+].[B-]C#N BEOOHQFXGBMRKU-UHFFFAOYSA-N 0.000 description 1
- 238000000527 sonication Methods 0.000 description 1
- 241000894007 species Species 0.000 description 1
- 230000003595 spectral effect Effects 0.000 description 1
- 239000011550 stock solution Substances 0.000 description 1
- 238000003860 storage Methods 0.000 description 1
- 230000001502 supplementing effect Effects 0.000 description 1
- 230000008685 targeting Effects 0.000 description 1
- 229930101283 tetracycline Natural products 0.000 description 1
- OFVLGDICTFRJMM-WESIUVDSSA-N tetracycline Chemical compound C1=CC=C2[C@](O)(C)[C@H]3C[C@H]4[C@H](N(C)C)C(O)=C(C(N)=O)C(=O)[C@@]4(O)C(O)=C3C(=O)C2=C1O OFVLGDICTFRJMM-WESIUVDSSA-N 0.000 description 1
- 238000010257 thawing Methods 0.000 description 1
- 231100000331 toxic Toxicity 0.000 description 1
- 230000002588 toxic effect Effects 0.000 description 1
- 108700012359 toxins Proteins 0.000 description 1
- 238000012546 transfer Methods 0.000 description 1
- 238000011282 treatment Methods 0.000 description 1
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 1
- 101150016309 trpC gene Proteins 0.000 description 1
- 125000000430 tryptophan group Chemical group [H]N([H])C(C(=O)O*)C([H])([H])C1=C([H])N([H])C2=C([H])C([H])=C([H])C([H])=C12 0.000 description 1
- 125000002987 valine group Chemical group [H]N([H])C([H])(C(*)=O)C([H])(C([H])([H])[H])C([H])([H])[H] 0.000 description 1
- 108010072644 valyl-alanyl-prolyl-glycine Proteins 0.000 description 1
- 239000011534 wash buffer Substances 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/10—Transferases (2.)
- C12N9/1096—Transferases (2.) transferring nitrogenous groups (2.6)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/90—Isomerases (5.)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P17/00—Preparation of heterocyclic carbon compounds with only O, N, S, Se or Te as ring hetero atoms
- C12P17/10—Nitrogen as only ring hetero atom
Landscapes
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Health & Medical Sciences (AREA)
- Organic Chemistry (AREA)
- Zoology (AREA)
- Engineering & Computer Science (AREA)
- Wood Science & Technology (AREA)
- Genetics & Genomics (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Microbiology (AREA)
- General Health & Medical Sciences (AREA)
- Biochemistry (AREA)
- Biotechnology (AREA)
- General Engineering & Computer Science (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- Biomedical Technology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Enzymes And Modification Thereof (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Indole Compounds (AREA)
- Seasonings (AREA)
Applications Claiming Priority (5)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US58401606A | 2006-10-20 | 2006-10-20 | |
| US11/584,016 | 2006-10-20 | ||
| US11/714,279 US8076108B2 (en) | 2005-04-26 | 2007-03-06 | Polypeptides and biosynthetic pathways for the production of stereoisomers of monatin and their precursors |
| US11/714,279 | 2007-03-06 | ||
| PCT/US2007/081932 WO2008085575A2 (en) | 2006-10-20 | 2007-10-19 | Polypeptides and biosynthetic pathways for the production of stereoisomers of monatin and their precursors |
Publications (3)
| Publication Number | Publication Date |
|---|---|
| AU2007342275A1 AU2007342275A1 (en) | 2008-07-17 |
| AU2007342275A2 AU2007342275A2 (en) | 2009-07-09 |
| AU2007342275B2 true AU2007342275B2 (en) | 2013-06-20 |
Family
ID=39615760
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| AU2007342275A Ceased AU2007342275B2 (en) | 2006-10-20 | 2007-10-19 | Polypeptides and biosynthetic pathways for the production of stereoisomers of monatin and their precursors |
Country Status (7)
| Country | Link |
|---|---|
| US (2) | US8076108B2 (enExample) |
| EP (1) | EP2089529B1 (enExample) |
| JP (2) | JP2010507367A (enExample) |
| AR (1) | AR063348A1 (enExample) |
| AU (1) | AU2007342275B2 (enExample) |
| CA (1) | CA2666348A1 (enExample) |
| WO (1) | WO2008085575A2 (enExample) |
Families Citing this family (30)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US7297800B2 (en) | 2001-12-27 | 2007-11-20 | Ajinomoto Co., Inc. | Process of producing glutamate derivatives |
| US8372989B2 (en) * | 2002-04-23 | 2013-02-12 | Cargill, Incorporated | Polypeptides and biosynthetic pathways for the production of monatin and its precursors |
| US7572607B2 (en) * | 2002-04-23 | 2009-08-11 | Cargill, Incorporated | Polypeptides and biosynthetic pathways for the production of monatin and its precursors |
| RU2307871C2 (ru) | 2002-08-26 | 2007-10-10 | Адзиномото Ко., Инк. | НОВАЯ АЛЬДОЛАЗА И СПОСОБ ПОЛУЧЕНИЯ ЗАМЕЩЕННЫХ α-КЕТОКИСЛОТ |
| EP2050821A3 (en) * | 2002-12-09 | 2009-05-13 | Ajinomoto Co., Inc. | Mutated D-aminotransferase and method for producing optically active glutamic acid derivatives using the same |
| KR20060061811A (ko) * | 2003-08-01 | 2006-06-08 | 카아길, 인코포레이팃드 | 모나틴 식탁용 감미제 조성물 및 이의 제조 방법 |
| EP1653810B1 (en) * | 2003-08-14 | 2007-04-25 | Cargill, Incorporated | Chewing gum compositions comprising monatin and methods of making same |
| EP1657985A1 (en) * | 2003-08-25 | 2006-05-24 | Cargill Inc. | Beverage compositions comprising monatin and methods of making same |
| ATE498691T1 (de) * | 2003-10-21 | 2011-03-15 | Cargill Inc | Herstellung von monatin und monatinvorstufen |
| JP5059746B2 (ja) * | 2005-04-20 | 2012-10-31 | カーギル,インコーポレイティド | モナチンの生体内分泌のための生成物及び方法 |
| US8158389B2 (en) * | 2005-04-20 | 2012-04-17 | Cargill, Incorporated | Products and methods for in vivo secretion of monatin |
| US7582455B2 (en) * | 2005-04-26 | 2009-09-01 | Cargill, Incorporated | Polypeptides and biosynthetic pathways for the production of stereoisomers of monatin and their precursors |
| US8076108B2 (en) * | 2005-04-26 | 2011-12-13 | Cargill, Incorporated | Polypeptides and biosynthetic pathways for the production of stereoisomers of monatin and their precursors |
| CN102690833B (zh) * | 2006-03-07 | 2015-09-09 | 巴斯夫酶有限责任公司 | 醛缩酶、编码它们的核酸及制备和使用它们的方法 |
| ES2416104T3 (es) * | 2006-03-07 | 2013-07-30 | Cargill, Incorporated | Aldolasas, ácidos nucleicos que las codifican y métodos para producir y usar las mismas |
| US20090198072A1 (en) * | 2006-05-24 | 2009-08-06 | Cargill, Incorporated | Methods and systems for increasing production of equilibrium reactions |
| AU2007267618B2 (en) * | 2006-05-24 | 2013-07-18 | Cargill, Incorporated | Methods and systems for increasing production of equilibrium reactions |
| CN101239941B (zh) * | 2007-02-08 | 2012-02-29 | 味之素株式会社 | 光学活性化合物的制造方法 |
| US8003361B2 (en) * | 2007-10-01 | 2011-08-23 | Cargill Incorporated | Production of monatin enantiomers |
| US8076107B2 (en) * | 2007-10-01 | 2011-12-13 | Cargill, Incorporated | Production of monatin stereoisomers |
| US8367847B2 (en) * | 2007-10-01 | 2013-02-05 | Cargill, Incorporated | Production of monatin enantiomers |
| WO2009088442A2 (en) * | 2008-01-03 | 2009-07-16 | Cargill, Incorporated | Isomerases and epimerases and methods of using |
| JP5683962B2 (ja) * | 2008-01-03 | 2015-03-11 | カーギル・インコーポレイテッド | アミノトランスフェラーゼおよびオキシドレダクターゼの核酸およびポリペプチドおよび使用方法 |
| WO2012050125A1 (ja) | 2010-10-14 | 2012-04-19 | 味の素株式会社 | モナティンの製造方法 |
| US8771997B2 (en) | 2011-04-20 | 2014-07-08 | Ajinomoto Co., Inc. | Method for producing monatin using an L-amino acid aminotransferase |
| WO2012147674A1 (ja) * | 2011-04-25 | 2012-11-01 | 味の素株式会社 | モナティンの製造方法 |
| ES2538720B1 (es) * | 2013-12-20 | 2016-05-12 | Universidad Autónoma de Madrid | Racemasa BsrAh para la racemización de aminoácidos |
| US11685942B2 (en) | 2016-03-04 | 2023-06-27 | President And Fellows Of Harvard College | Methods for making polypeptides including d-amino acids |
| CN106636227B (zh) * | 2016-09-22 | 2020-11-06 | 精晶药业股份有限公司 | 一种酶法转化l-丙氨酸制备丙酮酸的方法 |
| CN113025602A (zh) * | 2021-03-18 | 2021-06-25 | 绵阳晟氏健康科技有限公司 | 固定化精氨酸消旋酶及其制备方法、应用 |
Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US20050221455A1 (en) * | 2003-10-21 | 2005-10-06 | Cargill, Inc. | Production of monatin and monatin precursors |
| US20050282260A1 (en) * | 2002-04-23 | 2005-12-22 | Cargill, Incorporated | Polypeptides and biosynthetic pathways for the production of monatin and its precursors |
| WO2007133183A2 (en) * | 2006-04-26 | 2007-11-22 | Cargill, Incorporated | Polypeptides and biosynthetic pathways for the production of stereoisomers of monatin and their precursors |
Family Cites Families (75)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US3002889A (en) | 1960-06-20 | 1961-10-03 | Kyowa Hakko Kogyo Kk | Method of producing l-glutamic acid |
| US3128237A (en) | 1961-02-24 | 1964-04-07 | Ajinomoto Kk | Process for producing l-glutamic acid by bacterial fermentation |
| US3399114A (en) | 1964-08-22 | 1968-08-27 | Asahi Chemical Ind | Process for producing l-glutamic acid by using bacteria |
| US4371614A (en) | 1980-08-22 | 1983-02-01 | Ajinomoto Co., Inc. | E.Coli bacteria carrying recombinant plasmids and their use in the fermentative production of L-tryptophan |
| EP0232262A4 (en) | 1985-08-15 | 1989-09-19 | Stauffer Chemical Co | TRYPTOPHANE GENERATING MICROORGANISM. |
| GB2205834B (en) | 1987-06-15 | 1990-10-31 | South African Inventions | 3-(1-amino-1,3-dicarboxy-3-hydroxy-but-4-yl)-indole compounds |
| US5300437A (en) | 1989-06-22 | 1994-04-05 | Celgene Corporation | Enantiomeric enrichment and stereoselective synthesis of chiral amines |
| WO1989011212A2 (en) | 1989-08-30 | 1989-11-30 | Wm. Wrigley Jr. Company | Method of controlling release of cyclamate in chewing gum and gum produced thereby |
| ES2063443T3 (es) | 1990-01-19 | 1995-01-01 | Technology Finance Corp | Procedimiento para la produccion de 3-(1-amino-1,3-dicarboxi-3-hidroxi-but-4-il) indol. |
| US5360724A (en) | 1992-12-18 | 1994-11-01 | Celgene Corporation | Process for the preparation of chiral 1-aryl-2-aminopropanes |
| US6264999B1 (en) | 1993-09-30 | 2001-07-24 | Wm. Wrigley Jr. Company | Chewing gum containing erythritol and method of making |
| US6117679A (en) * | 1994-02-17 | 2000-09-12 | Maxygen, Inc. | Methods for generating polynucleotides having desired characteristics by iterative selection and recombination |
| JP3698742B2 (ja) | 1994-03-01 | 2005-09-21 | 協和醗酵工業株式会社 | 光学活性4−ヒドロキシ−2−ケトグルタル酸の製造法 |
| US5985617A (en) | 1997-02-18 | 1999-11-16 | Liao; James C. | Microorganisms and methods for overproduction of DAHP by cloned PPS gene |
| GB9701425D0 (en) * | 1997-01-24 | 1997-03-12 | Bioinvent Int Ab | A method for in vitro molecular evolution of protein function |
| CA2234412C (en) | 1997-06-09 | 2008-09-02 | Kyowa Hakko Kogyo Co., Ltd. | Method for producing optically active compound |
| US6099848A (en) * | 1997-11-18 | 2000-08-08 | The Trustees Of The University Of Pennsylvania | Immunogenic compositions comprising DAL/DAT double-mutant, auxotrophic, attenuated strains of Listeria and their methods of use |
| DE19818541C2 (de) | 1998-04-24 | 2003-04-10 | Forschungszentrum Juelich Gmbh | Mikrobielle Herstellung von Substanzen aus dem aromatischen Stoffwechsel / III |
| US5994559A (en) | 1998-08-06 | 1999-11-30 | The Board Of Governors For Higher Education, State Of Rhode Island And Providence Plantations | Synthesis of monatin-A high intensity natural sweetener |
| JP2002060382A (ja) | 2000-08-22 | 2002-02-26 | Ajinomoto Co Inc | モナティンの立体異性体及びその使用、並びにモナティン類の製造方法及びそのための中間体 |
| DE10129711B4 (de) | 2001-06-22 | 2007-08-23 | Forschungszentrum Jülich GmbH | Verfahren zur fermentativen Herstellung von Pyruvat |
| JP2003171365A (ja) | 2001-11-30 | 2003-06-20 | Ajinomoto Co Inc | モナティン類及びその製造中間体の製造方法並びに新規中間体 |
| EP2409968A1 (en) | 2001-11-30 | 2012-01-25 | Ajinomoto Co., Inc. | Crystals of non-natural-type stereoisomer salt of monatin and use thereof |
| DE60239072D1 (de) | 2001-12-27 | 2011-03-10 | Ajinomoto Kk | Verfahren zur herstellung von glutaminsäurederivaten |
| US7297800B2 (en) * | 2001-12-27 | 2007-11-20 | Ajinomoto Co., Inc. | Process of producing glutamate derivatives |
| CN100465156C (zh) | 2001-12-27 | 2009-03-04 | 味之素株式会社 | 谷氨酸化合物及其制备中间体的制造方法与为此所用的新型中间体 |
| US7247466B2 (en) | 2002-03-01 | 2007-07-24 | Kyowa Hakko Kogyo Co., Ltd. | Amino acid racemase having low substrate specificity and process for producing racemic amino acid |
| JP2003292484A (ja) | 2002-04-01 | 2003-10-15 | Ajinomoto Co Inc | γ−ヒドロキシアミノ酸誘導体及びモナティン類の製造方法 |
| KR100902813B1 (ko) | 2002-04-23 | 2009-06-12 | 카길 인코포레이티드 | 폴리펩티드 및 생합성 경로 |
| US8372989B2 (en) | 2002-04-23 | 2013-02-12 | Cargill, Incorporated | Polypeptides and biosynthetic pathways for the production of monatin and its precursors |
| RU2307871C2 (ru) | 2002-08-26 | 2007-10-10 | Адзиномото Ко., Инк. | НОВАЯ АЛЬДОЛАЗА И СПОСОБ ПОЛУЧЕНИЯ ЗАМЕЩЕННЫХ α-КЕТОКИСЛОТ |
| EP2050821A3 (en) | 2002-12-09 | 2009-05-13 | Ajinomoto Co., Inc. | Mutated D-aminotransferase and method for producing optically active glutamic acid derivatives using the same |
| CA2512752C (en) | 2003-01-09 | 2012-05-29 | Ajinomoto Co., Inc. | Process for manufacturing a glutamic acid derivative and a pyroglutamic acid derivative and a novel intermediate in the manufacture thereof |
| JP4239600B2 (ja) | 2003-01-24 | 2009-03-18 | 味の素株式会社 | 2r−モナティンの製造方法 |
| WO2004085624A2 (en) | 2003-03-24 | 2004-10-07 | Diversa Corporation | Transaminases, deaminases and aminomutases and compositions and methods for enzymatic detoxification |
| JP2004331650A (ja) | 2003-04-14 | 2004-11-25 | Kanazawa Univ Tlo Inc | モナチン類の製造法 |
| JP2004331644A (ja) | 2003-04-14 | 2004-11-25 | Kanazawa Univ Tlo Inc | モナチン類の製造法 |
| WO2005001105A1 (ja) | 2003-06-26 | 2005-01-06 | Ajinomoto Co., Inc. | モナティンの製造方法 |
| KR20060061811A (ko) | 2003-08-01 | 2006-06-08 | 카아길, 인코포레이팃드 | 모나틴 식탁용 감미제 조성물 및 이의 제조 방법 |
| EP1653810B1 (en) | 2003-08-14 | 2007-04-25 | Cargill, Incorporated | Chewing gum compositions comprising monatin and methods of making same |
| EP1657985A1 (en) | 2003-08-25 | 2006-05-24 | Cargill Inc. | Beverage compositions comprising monatin and methods of making same |
| JP4500977B2 (ja) | 2003-11-05 | 2010-07-14 | 味の素株式会社 | 新規アミノ酸誘導体及び甘味剤 |
| JP5113978B2 (ja) | 2003-11-21 | 2013-01-09 | 味の素株式会社 | グルタミン酸誘導体の有機アミン塩及びその利用 |
| EP1719758B1 (en) | 2004-02-27 | 2012-02-22 | Ajinomoto Co., Inc. | Process for producing monatin |
| JP4604524B2 (ja) | 2004-03-16 | 2011-01-05 | 味の素株式会社 | 変異型アルドラーゼ、並びにこれを用いた光学活性ihog及び光学活性モナティンの製造方法 |
| JP4604537B2 (ja) | 2004-03-31 | 2011-01-05 | 味の素株式会社 | L−システイン生産菌及びl−システインの製造法 |
| US7935377B2 (en) | 2004-06-04 | 2011-05-03 | Ajinomoto Co., Inc. | Crystals of free (2R, 4R)-monatin and use thereof |
| CA2506247C (en) | 2004-06-07 | 2012-02-21 | Ajinomoto Co., Inc. | Novel aldolase, and method for producing optically active ihog and monatin |
| KR101216575B1 (ko) | 2004-07-14 | 2012-12-31 | 아지노모토 가부시키가이샤 | (2r,4r)-모나틴 칼륨 염 결정 및 이를 함유하는 감미료조성물 |
| JP2007284349A (ja) | 2004-07-27 | 2007-11-01 | Ajinomoto Co Inc | モナティンまたはその塩の製造方法 |
| ATE554178T1 (de) | 2004-10-05 | 2012-05-15 | Ajinomoto Kk | Verfahren zur herstellung von aminosäurederivaten aus hydroxyiminosäuren |
| BRPI0517419A (pt) | 2004-10-15 | 2008-10-07 | Ajinomoto Kk | composição adoçante, bebida, alimento, composição para cavidade bucal ou produto farmacêutico, estabilizador de conservação para monatina ou um sal da mesma, métodos de conservação de monatina ou de um sal da mesma e de composição adoçante, bebida, alimento, composição para cavidade bucal ou produto farmacêutico compreendendo monatina ou um sal da mesma, e, monatina ou um sal da mesma |
| JP2008530978A (ja) | 2005-03-03 | 2008-08-14 | 味の素株式会社 | 4−ハイドロキシ−l−イソロイシン又はその塩の製造法 |
| US8158389B2 (en) | 2005-04-20 | 2012-04-17 | Cargill, Incorporated | Products and methods for in vivo secretion of monatin |
| JP5059746B2 (ja) | 2005-04-20 | 2012-10-31 | カーギル,インコーポレイティド | モナチンの生体内分泌のための生成物及び方法 |
| US8076108B2 (en) | 2005-04-26 | 2011-12-13 | Cargill, Incorporated | Polypeptides and biosynthetic pathways for the production of stereoisomers of monatin and their precursors |
| US7524660B2 (en) | 2005-05-05 | 2009-04-28 | E.I. Du Pont De Nemours And Company | Utilization of fructose in microbial production strains |
| CN102690833B (zh) | 2006-03-07 | 2015-09-09 | 巴斯夫酶有限责任公司 | 醛缩酶、编码它们的核酸及制备和使用它们的方法 |
| ES2416104T3 (es) | 2006-03-07 | 2013-07-30 | Cargill, Incorporated | Aldolasas, ácidos nucleicos que las codifican y métodos para producir y usar las mismas |
| RU2338784C2 (ru) | 2006-03-24 | 2008-11-20 | Закрытое акционерное общество "Научно-исследовательский институт Аджиномото-Генетика" (ЗАО АГРИ) | Новая альдолаза, днк, кодирующая альдолазу, клетки, трансформированные днк, способ получения альдолазы и способ получения 4-гидрокси-l-изолейцина (варианты) |
| AU2007267618B2 (en) | 2006-05-24 | 2013-07-18 | Cargill, Incorporated | Methods and systems for increasing production of equilibrium reactions |
| US20090198072A1 (en) | 2006-05-24 | 2009-08-06 | Cargill, Incorporated | Methods and systems for increasing production of equilibrium reactions |
| US7354746B1 (en) | 2006-12-11 | 2008-04-08 | Ajinomoto Co., Inc. | Method for producing optically active IHOG and monatin |
| CN101239941B (zh) | 2007-02-08 | 2012-02-29 | 味之素株式会社 | 光学活性化合物的制造方法 |
| US8003361B2 (en) | 2007-10-01 | 2011-08-23 | Cargill Incorporated | Production of monatin enantiomers |
| US8076107B2 (en) | 2007-10-01 | 2011-12-13 | Cargill, Incorporated | Production of monatin stereoisomers |
| US8367847B2 (en) | 2007-10-01 | 2013-02-05 | Cargill, Incorporated | Production of monatin enantiomers |
| WO2011002469A1 (en) | 2009-07-02 | 2011-01-06 | Cargill, Incorporated | Isomerases and epimerases and methods of using |
| JP5683962B2 (ja) | 2008-01-03 | 2015-03-11 | カーギル・インコーポレイテッド | アミノトランスフェラーゼおよびオキシドレダクターゼの核酸およびポリペプチドおよび使用方法 |
| JP2012520079A (ja) | 2009-03-12 | 2012-09-06 | カーギル・インコーポレイテッド | モナチンおよびカルシウムを含む組成物 |
| CN102481007A (zh) | 2009-05-28 | 2012-05-30 | 嘉吉公司 | 储存稳定的莫纳汀增甜饮料 |
| WO2011082365A2 (en) | 2009-12-30 | 2011-07-07 | Cargill, Incorporated | Improved bioreactor performance in the production of monatin |
| WO2011082353A1 (en) | 2009-12-30 | 2011-07-07 | Cargill, Incorporated | Separation and purification of monatin |
| EP2519406A4 (en) | 2009-12-30 | 2014-03-26 | Cargill Inc | POLYMER AND METHODS FOR PREPARING AND USING POLYMER |
| US20120264948A1 (en) | 2009-12-30 | 2012-10-18 | Cargill, Incorporated | Membrane separation and purification of monatin |
-
2007
- 2007-03-06 US US11/714,279 patent/US8076108B2/en not_active Expired - Fee Related
- 2007-10-19 CA CA002666348A patent/CA2666348A1/en not_active Abandoned
- 2007-10-19 AU AU2007342275A patent/AU2007342275B2/en not_active Ceased
- 2007-10-19 EP EP07872326.9A patent/EP2089529B1/en not_active Not-in-force
- 2007-10-19 JP JP2009533566A patent/JP2010507367A/ja active Pending
- 2007-10-19 WO PCT/US2007/081932 patent/WO2008085575A2/en not_active Ceased
- 2007-10-19 AR ARP070104644A patent/AR063348A1/es not_active Application Discontinuation
-
2011
- 2011-11-02 US US13/287,900 patent/US8975046B2/en not_active Expired - Fee Related
-
2015
- 2015-06-17 JP JP2015122370A patent/JP2015211679A/ja active Pending
Patent Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US20050282260A1 (en) * | 2002-04-23 | 2005-12-22 | Cargill, Incorporated | Polypeptides and biosynthetic pathways for the production of monatin and its precursors |
| US20050221455A1 (en) * | 2003-10-21 | 2005-10-06 | Cargill, Inc. | Production of monatin and monatin precursors |
| WO2007133183A2 (en) * | 2006-04-26 | 2007-11-22 | Cargill, Incorporated | Polypeptides and biosynthetic pathways for the production of stereoisomers of monatin and their precursors |
Also Published As
| Publication number | Publication date |
|---|---|
| AU2007342275A1 (en) | 2008-07-17 |
| US8076108B2 (en) | 2011-12-13 |
| EP2089529A2 (en) | 2009-08-19 |
| EP2089529A4 (en) | 2012-04-11 |
| WO2008085575A2 (en) | 2008-07-17 |
| WO2008085575A3 (en) | 2009-03-19 |
| EP2089529B1 (en) | 2019-03-20 |
| JP2010507367A (ja) | 2010-03-11 |
| JP2015211679A (ja) | 2015-11-26 |
| AR063348A1 (es) | 2009-01-21 |
| AU2007342275A2 (en) | 2009-07-09 |
| US20120164697A1 (en) | 2012-06-28 |
| CA2666348A1 (en) | 2008-07-17 |
| US8975046B2 (en) | 2015-03-10 |
| US20080020434A1 (en) | 2008-01-24 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| AU2007342275B2 (en) | Polypeptides and biosynthetic pathways for the production of stereoisomers of monatin and their precursors | |
| US7582455B2 (en) | Polypeptides and biosynthetic pathways for the production of stereoisomers of monatin and their precursors | |
| AU2004286207B2 (en) | Production of monatin and monatin precursors | |
| CA2606178C (en) | Polypeptides and biosynthetic pathways for the production of monatin and its precursors | |
| EP2361976B1 (en) | Polypeptides and biosynthetic pathways for the production of stereoisomers of monatin and their precursors | |
| AU2012201740B2 (en) | Polypeptides and biosynthetic pathways for the production of stereoisomers of monatin and their precursors |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| DA3 | Amendments made section 104 |
Free format text: THE NATURE OF THE AMENDMENT IS AS SHOWN IN THE STATEMENT(S) FILED 25 MAY 2009 |
|
| FGA | Letters patent sealed or granted (standard patent) | ||
| MK14 | Patent ceased section 143(a) (annual fees not paid) or expired |