ES2285128T3 - Polipeptidos que tienen actividad amida del alfa-h-alfa aminoacido racemasa y los acidos nucleicos que codifican los mismos. - Google Patents
Polipeptidos que tienen actividad amida del alfa-h-alfa aminoacido racemasa y los acidos nucleicos que codifican los mismos. Download PDFInfo
- Publication number
- ES2285128T3 ES2285128T3 ES03733629T ES03733629T ES2285128T3 ES 2285128 T3 ES2285128 T3 ES 2285128T3 ES 03733629 T ES03733629 T ES 03733629T ES 03733629 T ES03733629 T ES 03733629T ES 2285128 T3 ES2285128 T3 ES 2285128T3
- Authority
- ES
- Spain
- Prior art keywords
- amide
- amino acid
- activity
- amino
- racemase
- 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.)
- Expired - Lifetime
Links
- 230000000694 effects Effects 0.000 title claims abstract description 137
- 229920001184 polypeptide Polymers 0.000 title claims abstract description 72
- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 72
- 102000004196 processed proteins & peptides Human genes 0.000 title claims abstract description 72
- 150000007523 nucleic acids Chemical class 0.000 title claims abstract description 59
- 108020004707 nucleic acids Proteins 0.000 title claims abstract description 23
- 102000039446 nucleic acids Human genes 0.000 title claims abstract description 23
- 241000670727 Amida Species 0.000 title claims description 8
- 238000000034 method Methods 0.000 claims abstract description 86
- 244000005700 microbiome Species 0.000 claims abstract description 53
- 239000013598 vector Substances 0.000 claims abstract description 39
- 150000001408 amides Chemical class 0.000 claims description 235
- 108010008830 Amino Acid Isomerases Proteins 0.000 claims description 143
- 102000006534 Amino Acid Isomerases Human genes 0.000 claims description 143
- JBKVHLHDHHXQEQ-UHFFFAOYSA-N epsilon-caprolactam Chemical compound O=C1CCCCCN1 JBKVHLHDHHXQEQ-UHFFFAOYSA-N 0.000 claims description 139
- 150000001413 amino acids Chemical class 0.000 claims description 116
- 235000001014 amino acid Nutrition 0.000 claims description 112
- 235000008206 alpha-amino acids Nutrition 0.000 claims description 98
- 239000000203 mixture Substances 0.000 claims description 47
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 claims description 46
- 241000588814 Ochrobactrum anthropi Species 0.000 claims description 42
- 238000002360 preparation method Methods 0.000 claims description 33
- 108091028043 Nucleic acid sequence Proteins 0.000 claims description 32
- 239000012634 fragment Substances 0.000 claims description 32
- 241001524188 Glutamicibacter nicotianae Species 0.000 claims description 23
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 claims description 23
- 229910052757 nitrogen Inorganic materials 0.000 claims description 23
- 241000589156 Agrobacterium rhizogenes Species 0.000 claims description 19
- 239000002253 acid Substances 0.000 claims description 19
- 230000008569 process Effects 0.000 claims description 19
- 230000006340 racemization Effects 0.000 claims description 17
- 239000001963 growth medium Substances 0.000 claims description 11
- 239000011734 sodium Substances 0.000 claims description 11
- 239000011780 sodium chloride Substances 0.000 claims description 11
- 238000009396 hybridization Methods 0.000 claims description 10
- 102000037865 fusion proteins Human genes 0.000 claims description 9
- 108020001507 fusion proteins Proteins 0.000 claims description 9
- 238000012546 transfer Methods 0.000 claims description 9
- 101000835082 Homo sapiens TCF3 fusion partner Proteins 0.000 claims description 7
- 102100026140 TCF3 fusion partner Human genes 0.000 claims description 7
- 230000000295 complement effect Effects 0.000 claims description 5
- 239000003550 marker Substances 0.000 claims description 5
- 101710151246 Enantioselective amidase Proteins 0.000 claims description 4
- 230000009260 cross reactivity Effects 0.000 claims description 4
- 230000001900 immune effect Effects 0.000 claims description 3
- 239000001509 sodium citrate Substances 0.000 claims description 3
- NLJMYIDDQXHKNR-UHFFFAOYSA-K sodium citrate Chemical compound O.O.[Na+].[Na+].[Na+].[O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O NLJMYIDDQXHKNR-UHFFFAOYSA-K 0.000 claims description 3
- 238000004519 manufacturing process Methods 0.000 claims description 2
- 102000004879 Racemases and epimerases Human genes 0.000 abstract description 30
- 108090001066 Racemases and epimerases Proteins 0.000 abstract description 30
- 210000004027 cell Anatomy 0.000 description 114
- 229940024606 amino acid Drugs 0.000 description 101
- 241000588724 Escherichia coli Species 0.000 description 88
- 238000006243 chemical reaction Methods 0.000 description 62
- 239000000758 substrate Substances 0.000 description 50
- 108020004414 DNA Proteins 0.000 description 43
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 40
- 239000000872 buffer Substances 0.000 description 39
- 108090000623 proteins and genes Proteins 0.000 description 39
- 239000000243 solution Substances 0.000 description 35
- 239000002609 medium Substances 0.000 description 34
- 239000013612 plasmid Substances 0.000 description 31
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 30
- 238000005119 centrifugation Methods 0.000 description 25
- 239000011541 reaction mixture Substances 0.000 description 24
- 238000004458 analytical method Methods 0.000 description 22
- 238000011534 incubation Methods 0.000 description 22
- 229960003136 leucine Drugs 0.000 description 21
- 238000002474 experimental method Methods 0.000 description 19
- 238000009343 monoculture Methods 0.000 description 19
- 238000003752 polymerase chain reaction Methods 0.000 description 19
- 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 19
- 235000007682 pyridoxal 5'-phosphate Nutrition 0.000 description 19
- 239000011589 pyridoxal 5'-phosphate Substances 0.000 description 19
- 229960001327 pyridoxal phosphate Drugs 0.000 description 19
- ZNJHFNUEQDVFCJ-UHFFFAOYSA-M sodium;2-[4-(2-hydroxyethyl)piperazin-1-yl]ethanesulfonic acid;hydroxide Chemical compound [OH-].[Na+].OCCN1CCN(CCS(O)(=O)=O)CC1 ZNJHFNUEQDVFCJ-UHFFFAOYSA-M 0.000 description 19
- 239000004395 L-leucine Substances 0.000 description 18
- 235000019454 L-leucine Nutrition 0.000 description 18
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 18
- 238000000746 purification Methods 0.000 description 18
- 239000000284 extract Substances 0.000 description 16
- 238000004128 high performance liquid chromatography Methods 0.000 description 16
- 229930027917 kanamycin Natural products 0.000 description 16
- 229960000318 kanamycin Drugs 0.000 description 16
- 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 16
- 229930182823 kanamycin A Natural products 0.000 description 16
- 239000008188 pellet Substances 0.000 description 16
- 239000000523 sample Substances 0.000 description 16
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 14
- FORGMRSGVSYZQR-RXMQYKEDSA-N (2r)-2-amino-4-methylpentanamide Chemical compound CC(C)C[C@@H](N)C(N)=O FORGMRSGVSYZQR-RXMQYKEDSA-N 0.000 description 13
- ROHFNLRQFUQHCH-RXMQYKEDSA-N D-leucine Chemical compound CC(C)C[C@@H](N)C(O)=O ROHFNLRQFUQHCH-RXMQYKEDSA-N 0.000 description 13
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 13
- QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 12
- CSCPPACGZOOCGX-UHFFFAOYSA-N Acetone Chemical compound CC(C)=O CSCPPACGZOOCGX-UHFFFAOYSA-N 0.000 description 12
- 229930182819 D-leucine Natural products 0.000 description 12
- 241000589776 Pseudomonas putida Species 0.000 description 12
- QWCKQJZIFLGMSD-UHFFFAOYSA-N alpha-aminobutyric acid Chemical compound CCC(N)C(O)=O QWCKQJZIFLGMSD-UHFFFAOYSA-N 0.000 description 12
- 239000006285 cell suspension Substances 0.000 description 12
- 238000001514 detection method Methods 0.000 description 12
- 239000013615 primer Substances 0.000 description 12
- 102000004190 Enzymes Human genes 0.000 description 11
- 108090000790 Enzymes Proteins 0.000 description 11
- 235000019606 astringent taste Nutrition 0.000 description 11
- 238000002955 isolation Methods 0.000 description 11
- 239000002245 particle Substances 0.000 description 11
- HBAQYPYDRFILMT-UHFFFAOYSA-N 8-[3-(1-cyclopropylpyrazol-4-yl)-1H-pyrazolo[4,3-d]pyrimidin-5-yl]-3-methyl-3,8-diazabicyclo[3.2.1]octan-2-one Chemical class C1(CC1)N1N=CC(=C1)C1=NNC2=C1N=C(N=C2)N1C2C(N(CC1CC2)C)=O HBAQYPYDRFILMT-UHFFFAOYSA-N 0.000 description 10
- 108700023418 Amidases Proteins 0.000 description 10
- 241001302160 Escherichia coli str. K-12 substr. DH10B Species 0.000 description 10
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 10
- 102000005922 amidase Human genes 0.000 description 10
- 239000002773 nucleotide Substances 0.000 description 10
- 239000000126 substance Substances 0.000 description 10
- 230000009466 transformation Effects 0.000 description 10
- YXFVVABEGXRONW-UHFFFAOYSA-N Toluene Chemical compound CC1=CC=CC=C1 YXFVVABEGXRONW-UHFFFAOYSA-N 0.000 description 9
- 239000003153 chemical reaction reagent Substances 0.000 description 9
- 238000010790 dilution Methods 0.000 description 9
- 239000012895 dilution Substances 0.000 description 9
- 229940088598 enzyme Drugs 0.000 description 9
- 125000003729 nucleotide group Chemical group 0.000 description 9
- 102000004400 Aminopeptidases Human genes 0.000 description 8
- 108090000915 Aminopeptidases Proteins 0.000 description 8
- 125000004432 carbon atom Chemical group C* 0.000 description 8
- 238000001816 cooling Methods 0.000 description 8
- VHJLVAABSRFDPM-QWWZWVQMSA-N dithiothreitol Chemical compound SC[C@@H](O)[C@H](O)CS VHJLVAABSRFDPM-QWWZWVQMSA-N 0.000 description 8
- 239000000725 suspension Substances 0.000 description 8
- 239000011543 agarose gel Substances 0.000 description 7
- 238000010367 cloning Methods 0.000 description 7
- 238000010276 construction Methods 0.000 description 7
- 230000029087 digestion Effects 0.000 description 7
- 239000003480 eluent Substances 0.000 description 7
- 238000010369 molecular cloning Methods 0.000 description 7
- 235000018102 proteins Nutrition 0.000 description 7
- 102000004169 proteins and genes Human genes 0.000 description 7
- 108091008146 restriction endonucleases Proteins 0.000 description 7
- 239000007160 ty medium Substances 0.000 description 7
- 108020004465 16S ribosomal RNA Proteins 0.000 description 6
- WEVYAHXRMPXWCK-UHFFFAOYSA-N Acetonitrile Chemical compound CC#N WEVYAHXRMPXWCK-UHFFFAOYSA-N 0.000 description 6
- BTBUEUYNUDRHOZ-UHFFFAOYSA-N Borate Chemical compound [O-]B([O-])[O-] BTBUEUYNUDRHOZ-UHFFFAOYSA-N 0.000 description 6
- 108700026244 Open Reading Frames Proteins 0.000 description 6
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 6
- 125000000217 alkyl group Chemical group 0.000 description 6
- 239000013604 expression vector Substances 0.000 description 6
- 238000003780 insertion Methods 0.000 description 6
- 230000037431 insertion Effects 0.000 description 6
- DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 description 6
- HNNJFUDLLWOVKZ-UHFFFAOYSA-N 2-aminobutanamide Chemical compound CCC(N)C(N)=O HNNJFUDLLWOVKZ-UHFFFAOYSA-N 0.000 description 5
- 102000012410 DNA Ligases Human genes 0.000 description 5
- 108010061982 DNA Ligases Proteins 0.000 description 5
- QWCKQJZIFLGMSD-VKHMYHEASA-N L-alpha-aminobutyric acid Chemical compound CC[C@H](N)C(O)=O QWCKQJZIFLGMSD-VKHMYHEASA-N 0.000 description 5
- FORGMRSGVSYZQR-YFKPBYRVSA-N L-leucinamide Chemical compound CC(C)C[C@H](N)C(N)=O FORGMRSGVSYZQR-YFKPBYRVSA-N 0.000 description 5
- 238000000246 agarose gel electrophoresis Methods 0.000 description 5
- 150000001370 alpha-amino acid derivatives Chemical class 0.000 description 5
- 125000003118 aryl group Chemical group 0.000 description 5
- 235000010633 broth Nutrition 0.000 description 5
- FPPNZSSZRUTDAP-UWFZAAFLSA-N carbenicillin Chemical compound N([C@H]1[C@H]2SC([C@@H](N2C1=O)C(O)=O)(C)C)C(=O)C(C(O)=O)C1=CC=CC=C1 FPPNZSSZRUTDAP-UWFZAAFLSA-N 0.000 description 5
- 229960003669 carbenicillin Drugs 0.000 description 5
- 239000000047 product Substances 0.000 description 5
- 238000005215 recombination Methods 0.000 description 5
- 230000006798 recombination Effects 0.000 description 5
- 230000002441 reversible effect Effects 0.000 description 5
- 239000002689 soil Substances 0.000 description 5
- XDEHMKQLKPZERH-SCSAIBSYSA-N (2r)-2-amino-3-methylbutanamide Chemical compound CC(C)[C@@H](N)C(N)=O XDEHMKQLKPZERH-SCSAIBSYSA-N 0.000 description 4
- FORGMRSGVSYZQR-UHFFFAOYSA-N 2-amino-4-methylpentanamide Chemical compound CC(C)CC(N)C(N)=O FORGMRSGVSYZQR-UHFFFAOYSA-N 0.000 description 4
- 241001504009 Achromobacter obae Species 0.000 description 4
- 102000004092 Amidohydrolases Human genes 0.000 description 4
- 108090000531 Amidohydrolases Proteins 0.000 description 4
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 4
- 108020004705 Codon Proteins 0.000 description 4
- QWCKQJZIFLGMSD-GSVOUGTGSA-N D-alpha-aminobutyric acid Chemical compound CC[C@@H](N)C(O)=O QWCKQJZIFLGMSD-GSVOUGTGSA-N 0.000 description 4
- KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 description 4
- 238000012181 QIAquick gel extraction kit Methods 0.000 description 4
- 238000003556 assay Methods 0.000 description 4
- 229910052799 carbon Inorganic materials 0.000 description 4
- 238000003776 cleavage reaction Methods 0.000 description 4
- 239000002299 complementary DNA Substances 0.000 description 4
- 238000000151 deposition Methods 0.000 description 4
- 238000005516 engineering process Methods 0.000 description 4
- 238000001914 filtration Methods 0.000 description 4
- 238000001917 fluorescence detection Methods 0.000 description 4
- 125000005842 heteroatom Chemical group 0.000 description 4
- 239000007788 liquid Substances 0.000 description 4
- 239000000463 material Substances 0.000 description 4
- 238000005259 measurement Methods 0.000 description 4
- 239000013642 negative control Substances 0.000 description 4
- 229940054441 o-phthalaldehyde Drugs 0.000 description 4
- ZWLUXSQADUDCSB-UHFFFAOYSA-N phthalaldehyde Chemical compound O=CC1=CC=CC=C1C=O ZWLUXSQADUDCSB-UHFFFAOYSA-N 0.000 description 4
- 230000007017 scission Effects 0.000 description 4
- 238000000527 sonication Methods 0.000 description 4
- 125000001424 substituent group Chemical group 0.000 description 4
- 239000006228 supernatant Substances 0.000 description 4
- 238000005406 washing Methods 0.000 description 4
- JKMHFZQWWAIEOD-UHFFFAOYSA-N 2-[4-(2-hydroxyethyl)piperazin-1-yl]ethanesulfonic acid Chemical compound OCC[NH+]1CCN(CCS([O-])(=O)=O)CC1 JKMHFZQWWAIEOD-UHFFFAOYSA-N 0.000 description 3
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 3
- 241000894006 Bacteria Species 0.000 description 3
- 101100283604 Caenorhabditis elegans pigk-1 gene Proteins 0.000 description 3
- 108010067770 Endopeptidase K Proteins 0.000 description 3
- 108010093488 His-His-His-His-His-His Proteins 0.000 description 3
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 3
- 108091034117 Oligonucleotide Proteins 0.000 description 3
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 3
- 229930006000 Sucrose Natural products 0.000 description 3
- CZMRCDWAGMRECN-UGDNZRGBSA-N Sucrose Chemical compound O[C@H]1[C@H](O)[C@@H](CO)O[C@@]1(CO)O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 CZMRCDWAGMRECN-UGDNZRGBSA-N 0.000 description 3
- JLCPHMBAVCMARE-UHFFFAOYSA-N [3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methyl [5-(6-aminopurin-9-yl)-2-(hydroxymethyl)oxolan-3-yl] hydrogen phosphate Polymers Cc1cn(C2CC(OP(O)(=O)OCC3OC(CC3OP(O)(=O)OCC3OC(CC3O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c3nc(N)[nH]c4=O)C(COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3CO)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cc(C)c(=O)[nH]c3=O)n3cc(C)c(=O)[nH]c3=O)n3ccc(N)nc3=O)n3cc(C)c(=O)[nH]c3=O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)O2)c(=O)[nH]c1=O JLCPHMBAVCMARE-UHFFFAOYSA-N 0.000 description 3
- 229960000723 ampicillin Drugs 0.000 description 3
- 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 3
- 239000012472 biological sample Substances 0.000 description 3
- 230000015572 biosynthetic process Effects 0.000 description 3
- 229940041514 candida albicans extract Drugs 0.000 description 3
- -1 carboxy, amino, imino Chemical group 0.000 description 3
- 101150102092 ccdB gene Proteins 0.000 description 3
- 238000012790 confirmation Methods 0.000 description 3
- 230000003247 decreasing effect Effects 0.000 description 3
- 230000002255 enzymatic effect Effects 0.000 description 3
- 230000007062 hydrolysis Effects 0.000 description 3
- 238000006460 hydrolysis reaction Methods 0.000 description 3
- 230000000977 initiatory effect Effects 0.000 description 3
- 238000002156 mixing Methods 0.000 description 3
- 238000001556 precipitation Methods 0.000 description 3
- 230000035484 reaction time Effects 0.000 description 3
- 238000012163 sequencing technique Methods 0.000 description 3
- 238000010561 standard procedure Methods 0.000 description 3
- 238000003756 stirring Methods 0.000 description 3
- 239000005720 sucrose Substances 0.000 description 3
- 238000012360 testing method Methods 0.000 description 3
- 239000012138 yeast extract Substances 0.000 description 3
- BCFZIUVRIDQCHF-UHFFFAOYSA-N 2-amino-5-(1,3-dioxolan-2-yl)pentanamide Chemical compound NC(=O)C(N)CCCC1OCCO1 BCFZIUVRIDQCHF-UHFFFAOYSA-N 0.000 description 2
- 108091026890 Coding region Proteins 0.000 description 2
- 241000282326 Felis catus Species 0.000 description 2
- 229930182566 Gentamicin Natural products 0.000 description 2
- CEAZRRDELHUEMR-URQXQFDESA-N Gentamicin Chemical compound O1[C@H](C(C)NC)CC[C@@H](N)[C@H]1O[C@H]1[C@H](O)[C@@H](O[C@@H]2[C@@H]([C@@H](NC)[C@@](C)(O)CO2)O)[C@H](N)C[C@@H]1N CEAZRRDELHUEMR-URQXQFDESA-N 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
- 239000007995 HEPES buffer Substances 0.000 description 2
- JLSKPBDKNIXMBS-VIFPVBQESA-N L-tryptophanamide Chemical compound C1=CC=C2C(C[C@H](N)C(N)=O)=CNC2=C1 JLSKPBDKNIXMBS-VIFPVBQESA-N 0.000 description 2
- LESXFEZIFXFIQR-LURJTMIESA-N Leu-Gly Chemical compound CC(C)C[C@H](N)C(=O)NCC(O)=O LESXFEZIFXFIQR-LURJTMIESA-N 0.000 description 2
- TWRXJAOTZQYOKJ-UHFFFAOYSA-L Magnesium chloride Chemical compound [Mg+2].[Cl-].[Cl-] TWRXJAOTZQYOKJ-UHFFFAOYSA-L 0.000 description 2
- 229910021380 Manganese Chloride Inorganic materials 0.000 description 2
- GLFNIEUTAYBVOC-UHFFFAOYSA-L Manganese chloride Chemical compound Cl[Mn]Cl GLFNIEUTAYBVOC-UHFFFAOYSA-L 0.000 description 2
- NBIIXXVUZAFLBC-UHFFFAOYSA-N Phosphoric acid Chemical compound OP(O)(O)=O NBIIXXVUZAFLBC-UHFFFAOYSA-N 0.000 description 2
- 238000012300 Sequence Analysis Methods 0.000 description 2
- VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 description 2
- 239000007984 Tris EDTA buffer Substances 0.000 description 2
- HSRXSKHRSXRCFC-WDSKDSINSA-N Val-Ala Chemical compound CC(C)[C@H](N)C(=O)N[C@@H](C)C(O)=O HSRXSKHRSXRCFC-WDSKDSINSA-N 0.000 description 2
- 229960003767 alanine Drugs 0.000 description 2
- 150000001371 alpha-amino acids Chemical class 0.000 description 2
- BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 description 2
- 229910052921 ammonium sulfate Inorganic materials 0.000 description 2
- 235000011130 ammonium sulphate Nutrition 0.000 description 2
- 238000013459 approach Methods 0.000 description 2
- PYMYPHUHKUWMLA-UHFFFAOYSA-N arabinose Natural products OCC(O)C(O)C(O)C=O PYMYPHUHKUWMLA-UHFFFAOYSA-N 0.000 description 2
- 125000004429 atom Chemical group 0.000 description 2
- 230000008901 benefit Effects 0.000 description 2
- SRBFZHDQGSBBOR-UHFFFAOYSA-N beta-D-Pyranose-Lyxose Natural products OC1COC(O)C(O)C1O SRBFZHDQGSBBOR-UHFFFAOYSA-N 0.000 description 2
- 239000011942 biocatalyst Substances 0.000 description 2
- 235000008429 bread Nutrition 0.000 description 2
- 238000004364 calculation method Methods 0.000 description 2
- 239000012069 chiral reagent Substances 0.000 description 2
- 229960005091 chloramphenicol Drugs 0.000 description 2
- 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 2
- 239000013611 chromosomal DNA Substances 0.000 description 2
- 150000001875 compounds Chemical class 0.000 description 2
- 230000009089 cytolysis Effects 0.000 description 2
- 238000004520 electroporation Methods 0.000 description 2
- 239000000499 gel Substances 0.000 description 2
- 238000002523 gelfiltration Methods 0.000 description 2
- 229960002518 gentamicin Drugs 0.000 description 2
- 239000008103 glucose Substances 0.000 description 2
- 238000000338 in vitro Methods 0.000 description 2
- 230000002401 inhibitory effect Effects 0.000 description 2
- 239000006166 lysate Substances 0.000 description 2
- 239000011565 manganese chloride Substances 0.000 description 2
- 235000002867 manganese chloride Nutrition 0.000 description 2
- 230000004048 modification Effects 0.000 description 2
- 238000012986 modification Methods 0.000 description 2
- 230000035772 mutation Effects 0.000 description 2
- 230000036961 partial effect Effects 0.000 description 2
- VLTRZXGMWDSKGL-UHFFFAOYSA-N perchloric acid Chemical compound OCl(=O)(=O)=O VLTRZXGMWDSKGL-UHFFFAOYSA-N 0.000 description 2
- 235000011007 phosphoric acid Nutrition 0.000 description 2
- 239000012460 protein solution Substances 0.000 description 2
- LXNHXLLTXMVWPM-UHFFFAOYSA-N pyridoxine Chemical compound CC1=NC=C(CO)C(CO)=C1O LXNHXLLTXMVWPM-UHFFFAOYSA-N 0.000 description 2
- 150000003839 salts Chemical class 0.000 description 2
- 238000000926 separation method Methods 0.000 description 2
- 239000001632 sodium acetate Substances 0.000 description 2
- 235000017281 sodium acetate Nutrition 0.000 description 2
- 239000007787 solid Substances 0.000 description 2
- 238000003860 storage Methods 0.000 description 2
- 238000010257 thawing Methods 0.000 description 2
- 239000012137 tryptone Substances 0.000 description 2
- 238000011144 upstream manufacturing Methods 0.000 description 2
- 229960004295 valine Drugs 0.000 description 2
- OBSIQMZKFXFYLV-MRVPVSSYSA-N (2r)-2-amino-3-phenylpropanamide Chemical compound NC(=O)[C@H](N)CC1=CC=CC=C1 OBSIQMZKFXFYLV-MRVPVSSYSA-N 0.000 description 1
- BCFZIUVRIDQCHF-ZCFIWIBFSA-N (2r)-2-amino-5-(1,3-dioxolan-2-yl)pentanamide Chemical compound NC(=O)[C@H](N)CCCC1OCCO1 BCFZIUVRIDQCHF-ZCFIWIBFSA-N 0.000 description 1
- RQULWPSGQYZREI-ZCFIWIBFSA-N (2r)-2-azaniumyl-5-(1,3-dioxolan-2-yl)pentanoate Chemical compound OC(=O)[C@H](N)CCCC1OCCO1 RQULWPSGQYZREI-ZCFIWIBFSA-N 0.000 description 1
- NPDBDJFLKKQMCM-SCSAIBSYSA-N (2s)-2-amino-3,3-dimethylbutanoic acid Chemical compound CC(C)(C)[C@H](N)C(O)=O NPDBDJFLKKQMCM-SCSAIBSYSA-N 0.000 description 1
- RQULWPSGQYZREI-UHFFFAOYSA-N 2-azaniumyl-5-(1,3-dioxolan-2-yl)pentanoate Chemical compound OC(=O)C(N)CCCC1OCCO1 RQULWPSGQYZREI-UHFFFAOYSA-N 0.000 description 1
- 229920001817 Agar Polymers 0.000 description 1
- 241000589158 Agrobacterium Species 0.000 description 1
- QGZKDVFQNNGYKY-UHFFFAOYSA-N Ammonia Chemical compound N QGZKDVFQNNGYKY-UHFFFAOYSA-N 0.000 description 1
- QGZKDVFQNNGYKY-UHFFFAOYSA-O Ammonium Chemical compound [NH4+] QGZKDVFQNNGYKY-UHFFFAOYSA-O 0.000 description 1
- 241000186063 Arthrobacter Species 0.000 description 1
- 101000950981 Bacillus subtilis (strain 168) Catabolic NAD-specific glutamate dehydrogenase RocG Proteins 0.000 description 1
- 241000186146 Brevibacterium Species 0.000 description 1
- 241001112695 Clostridiales Species 0.000 description 1
- 241000186216 Corynebacterium Species 0.000 description 1
- 241000186249 Corynebacterium sp. Species 0.000 description 1
- 150000008574 D-amino acids Chemical class 0.000 description 1
- COLNVLDHVKWLRT-MRVPVSSYSA-N D-phenylalanine Chemical compound OC(=O)[C@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-MRVPVSSYSA-N 0.000 description 1
- 229930182832 D-phenylalanine Natural products 0.000 description 1
- 238000007400 DNA extraction Methods 0.000 description 1
- 238000007399 DNA isolation Methods 0.000 description 1
- 239000003155 DNA primer Substances 0.000 description 1
- 238000001712 DNA sequencing Methods 0.000 description 1
- 241000620209 Escherichia coli DH5[alpha] Species 0.000 description 1
- 108091092584 GDNA Proteins 0.000 description 1
- 102000016901 Glutamate dehydrogenase Human genes 0.000 description 1
- 108010043121 Green Fluorescent Proteins Proteins 0.000 description 1
- 102000004144 Green Fluorescent Proteins Human genes 0.000 description 1
- 241000588748 Klebsiella Species 0.000 description 1
- 241000588754 Klebsiella sp. Species 0.000 description 1
- ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical compound OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 0.000 description 1
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 1
- OBSIQMZKFXFYLV-QMMMGPOBSA-N L-phenylalanine amide Chemical compound NC(=O)[C@@H](N)CC1=CC=CC=C1 OBSIQMZKFXFYLV-QMMMGPOBSA-N 0.000 description 1
- VLJNHYLEOZPXFW-BYPYZUCNSA-N L-prolinamide Chemical compound NC(=O)[C@@H]1CCCN1 VLJNHYLEOZPXFW-BYPYZUCNSA-N 0.000 description 1
- 239000007987 MES buffer Substances 0.000 description 1
- 241001467578 Microbacterium Species 0.000 description 1
- 241000192041 Micrococcus Species 0.000 description 1
- 102000016943 Muramidase Human genes 0.000 description 1
- 108010014251 Muramidase Proteins 0.000 description 1
- 108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 description 1
- 239000000020 Nitrocellulose Substances 0.000 description 1
- 241000187580 Nocardioides Species 0.000 description 1
- 241000588843 Ochrobactrum Species 0.000 description 1
- 241001314535 Ophrys apifera Species 0.000 description 1
- LGRFSURHDFAFJT-UHFFFAOYSA-N Phthalic anhydride Natural products C1=CC=C2C(=O)OC(=O)C2=C1 LGRFSURHDFAFJT-UHFFFAOYSA-N 0.000 description 1
- 229940124158 Protease/peptidase inhibitor Drugs 0.000 description 1
- 241000589516 Pseudomonas Species 0.000 description 1
- 241000316848 Rhodococcus <scale insect> Species 0.000 description 1
- 108010083644 Ribonucleases Proteins 0.000 description 1
- 102000006382 Ribonucleases Human genes 0.000 description 1
- 241000144007 Rubrobacter Species 0.000 description 1
- 108010034546 Serratia marcescens nuclease Proteins 0.000 description 1
- 239000012505 Superdex™ Substances 0.000 description 1
- 241000520166 Terrabacter Species 0.000 description 1
- IOUPEELXVYPCPG-LURJTMIESA-N Val-Gly Chemical compound CC(C)[C@H]([NH3+])C(=O)NCC([O-])=O IOUPEELXVYPCPG-LURJTMIESA-N 0.000 description 1
- IOUPEELXVYPCPG-UHFFFAOYSA-N Valylglycine Chemical compound CC(C)C(N)C(=O)NCC(O)=O IOUPEELXVYPCPG-UHFFFAOYSA-N 0.000 description 1
- 230000009471 action Effects 0.000 description 1
- 125000002252 acyl group Chemical group 0.000 description 1
- 238000005273 aeration Methods 0.000 description 1
- 239000008272 agar Substances 0.000 description 1
- 125000003545 alkoxy group Chemical group 0.000 description 1
- 229940061720 alpha hydroxy acid Drugs 0.000 description 1
- 150000001280 alpha hydroxy acids Chemical class 0.000 description 1
- 230000003321 amplification Effects 0.000 description 1
- 125000000129 anionic group Chemical group 0.000 description 1
- PYMYPHUHKUWMLA-WDCZJNDASA-N arabinose Chemical compound OC[C@@H](O)[C@@H](O)[C@H](O)C=O PYMYPHUHKUWMLA-WDCZJNDASA-N 0.000 description 1
- 239000007853 buffer solution Substances 0.000 description 1
- JHIWVOJDXOSYLW-UHFFFAOYSA-N butyl 2,2-difluorocyclopropane-1-carboxylate Chemical compound CCCCOC(=O)C1CC1(F)F JHIWVOJDXOSYLW-UHFFFAOYSA-N 0.000 description 1
- 210000004899 c-terminal region Anatomy 0.000 description 1
- 125000003917 carbamoyl group Chemical group [H]N([H])C(*)=O 0.000 description 1
- 150000001732 carboxylic acid derivatives Chemical class 0.000 description 1
- 238000004113 cell culture Methods 0.000 description 1
- 230000006037 cell lysis Effects 0.000 description 1
- 210000002421 cell wall Anatomy 0.000 description 1
- 230000001413 cellular effect Effects 0.000 description 1
- 239000002738 chelating agent Substances 0.000 description 1
- 238000004296 chiral HPLC Methods 0.000 description 1
- 238000004587 chromatography analysis Methods 0.000 description 1
- 235000019506 cigar Nutrition 0.000 description 1
- 238000012411 cloning technique Methods 0.000 description 1
- 238000012937 correction Methods 0.000 description 1
- 150000003983 crown ethers Chemical class 0.000 description 1
- 239000000287 crude extract Substances 0.000 description 1
- 238000012258 culturing Methods 0.000 description 1
- 125000004093 cyano group Chemical group *C#N 0.000 description 1
- 238000001212 derivatisation Methods 0.000 description 1
- 238000010612 desalination reaction Methods 0.000 description 1
- 229940079919 digestives enzyme preparation Drugs 0.000 description 1
- 239000012153 distilled water Substances 0.000 description 1
- 239000003814 drug Substances 0.000 description 1
- 239000000975 dye Substances 0.000 description 1
- 238000001962 electrophoresis Methods 0.000 description 1
- 238000010828 elution Methods 0.000 description 1
- 238000003821 enantio-separation Methods 0.000 description 1
- 230000007613 environmental effect Effects 0.000 description 1
- 230000007071 enzymatic hydrolysis Effects 0.000 description 1
- 238000006047 enzymatic hydrolysis reaction Methods 0.000 description 1
- 238000009585 enzyme analysis Methods 0.000 description 1
- 238000011067 equilibration Methods 0.000 description 1
- 238000000605 extraction Methods 0.000 description 1
- 239000000706 filtrate Substances 0.000 description 1
- 239000012737 fresh medium Substances 0.000 description 1
- 238000001502 gel electrophoresis Methods 0.000 description 1
- 229960002743 glutamine Drugs 0.000 description 1
- 108010050848 glycylleucine Proteins 0.000 description 1
- 239000005090 green fluorescent protein Substances 0.000 description 1
- 229910052736 halogen Inorganic materials 0.000 description 1
- 150000002367 halogens Chemical class 0.000 description 1
- 230000003301 hydrolyzing effect Effects 0.000 description 1
- 125000002887 hydroxy group Chemical group [H]O* 0.000 description 1
- 230000000984 immunochemical effect Effects 0.000 description 1
- 230000002779 inactivation Effects 0.000 description 1
- 239000003112 inhibitor Substances 0.000 description 1
- 238000011081 inoculation Methods 0.000 description 1
- 239000002054 inoculum Substances 0.000 description 1
- 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 1
- BRHPBVXVOVMTIQ-ZLELNMGESA-N l-leucine l-leucine Chemical compound CC(C)C[C@H](N)C(O)=O.CC(C)C[C@H](N)C(O)=O BRHPBVXVOVMTIQ-ZLELNMGESA-N 0.000 description 1
- 239000004325 lysozyme Substances 0.000 description 1
- 229960000274 lysozyme Drugs 0.000 description 1
- 235000010335 lysozyme Nutrition 0.000 description 1
- 229910001629 magnesium chloride Inorganic materials 0.000 description 1
- 229910052943 magnesium sulfate Inorganic materials 0.000 description 1
- 108020004999 messenger RNA Proteins 0.000 description 1
- 229930182817 methionine Natural products 0.000 description 1
- 230000002906 microbiologic effect Effects 0.000 description 1
- 238000002703 mutagenesis Methods 0.000 description 1
- 231100000350 mutagenesis Toxicity 0.000 description 1
- 229930027945 nicotinamide-adenine dinucleotide Natural products 0.000 description 1
- BOPGDPNILDQYTO-NNYOXOHSSA-N nicotinamide-adenine dinucleotide Chemical compound C1=CCC(C(=O)N)=CN1[C@H]1[C@H](O)[C@H](O)[C@@H](COP(O)(=O)OP(O)(=O)OC[C@@H]2[C@H]([C@@H](O)[C@@H](O2)N2C3=NC=NC(N)=C3N=C2)O)O1 BOPGDPNILDQYTO-NNYOXOHSSA-N 0.000 description 1
- 125000000449 nitro group Chemical group [O-][N+](*)=O 0.000 description 1
- 229920001220 nitrocellulos Polymers 0.000 description 1
- 125000004433 nitrogen atom Chemical group N* 0.000 description 1
- 238000003199 nucleic acid amplification method Methods 0.000 description 1
- 229940046166 oligodeoxynucleotide Drugs 0.000 description 1
- 239000000137 peptide hydrolase inhibitor Substances 0.000 description 1
- 230000008823 permeabilization Effects 0.000 description 1
- 125000000864 peroxy group Chemical group O(O*)* 0.000 description 1
- 238000011533 pre-incubation Methods 0.000 description 1
- 239000002243 precursor Substances 0.000 description 1
- 238000002203 pretreatment Methods 0.000 description 1
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 1
- 230000006920 protein precipitation Effects 0.000 description 1
- RADKZDMFGJYCBB-UHFFFAOYSA-N pyridoxal hydrochloride Natural products CC1=NC=C(CO)C(C=O)=C1O RADKZDMFGJYCBB-UHFFFAOYSA-N 0.000 description 1
- 230000005855 radiation Effects 0.000 description 1
- 238000002708 random mutagenesis Methods 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 238000012552 review Methods 0.000 description 1
- 239000012488 sample solution Substances 0.000 description 1
- 229920006395 saturated elastomer Polymers 0.000 description 1
- 230000028327 secretion Effects 0.000 description 1
- 238000004062 sedimentation Methods 0.000 description 1
- 238000011218 seed culture Methods 0.000 description 1
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 1
- 230000000707 stereoselective effect Effects 0.000 description 1
- PXQLVRUNWNTZOS-UHFFFAOYSA-N sulfanyl Chemical class [SH] PXQLVRUNWNTZOS-UHFFFAOYSA-N 0.000 description 1
- 125000000020 sulfo group Chemical group O=S(=O)([*])O[H] 0.000 description 1
- 125000004001 thioalkyl group Chemical group 0.000 description 1
- 235000019158 vitamin B6 Nutrition 0.000 description 1
- 239000011726 vitamin B6 Substances 0.000 description 1
- 229940011671 vitamin b6 Drugs 0.000 description 1
- 239000002351 wastewater Substances 0.000 description 1
- 238000001262 western blot Methods 0.000 description 1
Classifications
-
- 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
- C12P41/00—Processes using enzymes or microorganisms to separate optical isomers from a racemic mixture
- C12P41/006—Processes using enzymes or microorganisms to separate optical isomers from a racemic mixture by reactions involving C-N bonds, e.g. nitriles, amides, hydantoins, carbamates, lactames, transamination reactions, or keto group formation from racemic mixtures
- C12P41/007—Processes using enzymes or microorganisms to separate optical isomers from a racemic mixture by reactions involving C-N bonds, e.g. nitriles, amides, hydantoins, carbamates, lactames, transamination reactions, or keto group formation from racemic mixtures by reactions involving acyl derivatives of racemic amines
-
- 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
- C12P13/00—Preparation of nitrogen-containing organic compounds
- C12P13/02—Amides, e.g. chloramphenicol or polyamides; Imides or polyimides; Urethanes, i.e. compounds comprising N-C=O structural element or polyurethanes
-
- 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
- C12P13/00—Preparation of nitrogen-containing organic compounds
- C12P13/04—Alpha- or beta- amino acids
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
Landscapes
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- Engineering & Computer Science (AREA)
- Wood Science & Technology (AREA)
- Zoology (AREA)
- Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Biotechnology (AREA)
- General Health & Medical Sciences (AREA)
- General Engineering & Computer Science (AREA)
- Microbiology (AREA)
- Biochemistry (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Analytical Chemistry (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- Biomedical Technology (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Peptides Or Proteins (AREA)
- Enzymes And Modification Thereof (AREA)
- Organic Low-Molecular-Weight Compounds And Preparation Thereof (AREA)
- Immobilizing And Processing Of Enzymes And Microorganisms (AREA)
Applications Claiming Priority (4)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| EP02100711 | 2002-06-14 | ||
| EP02100711 | 2002-06-14 | ||
| EP02080631 | 2002-12-20 | ||
| EP02080631 | 2002-12-20 |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| ES2285128T3 true ES2285128T3 (es) | 2007-11-16 |
Family
ID=29737945
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| ES03733629T Expired - Lifetime ES2285128T3 (es) | 2002-06-14 | 2003-06-13 | Polipeptidos que tienen actividad amida del alfa-h-alfa aminoacido racemasa y los acidos nucleicos que codifican los mismos. |
Country Status (9)
| Country | Link |
|---|---|
| US (1) | US7371555B2 (enExample) |
| EP (1) | EP1513946B1 (enExample) |
| JP (1) | JP4402587B2 (enExample) |
| CN (1) | CN100471950C (enExample) |
| AT (1) | ATE362544T1 (enExample) |
| AU (1) | AU2003238717A1 (enExample) |
| DE (1) | DE60313866T2 (enExample) |
| ES (1) | ES2285128T3 (enExample) |
| WO (1) | WO2003106691A1 (enExample) |
Families Citing this family (18)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US20050166498A1 (en) * | 1999-12-17 | 2005-08-04 | Oakey David D. | Carpet tile with cutout section, method and apparatus for production and method of installation |
| US7491520B2 (en) * | 2004-01-19 | 2009-02-17 | Dsm Ip Assets B.V. | Biochemical synthesis of 6-amino caproic acid |
| DE102004013842A1 (de) | 2004-03-20 | 2005-10-13 | Degussa Ag | Nitrilhydratasen aus Metagenombibliotheken |
| CN107090424A (zh) | 2008-01-22 | 2017-08-25 | 基因组股份公司 | 利用合成气或其它气态碳源和甲醇的方法和有机体 |
| CA3081506A1 (en) | 2008-03-05 | 2009-09-11 | Genomatica, Inc. | Long chain alcohol-producing organisms |
| EP2172545A1 (en) | 2008-09-24 | 2010-04-07 | DSM IP Assets B.V. | Preparation of purified peptide deformylase |
| WO2010068944A2 (en) | 2008-12-12 | 2010-06-17 | Celexion, Llc | Biological synthesis of difunctional alkanes from carbohydrate feedstocks |
| US8404465B2 (en) | 2009-03-11 | 2013-03-26 | Celexion, Llc | Biological synthesis of 6-aminocaproic acid from carbohydrate feedstocks |
| JP2012525156A (ja) | 2009-04-30 | 2012-10-22 | ゲノマチカ， インク． | イソプロパノール、ｎ−ブタノール、及びイソブタノールの産生のための微生物 |
| CN102625846B (zh) | 2009-04-30 | 2016-08-03 | 基因组股份公司 | 用于生产1,3-丁二醇的生物 |
| WO2011017560A1 (en) | 2009-08-05 | 2011-02-10 | Genomatica, Inc. | Semi-synthetic terephthalic acid via microorganisms that produce muconic acid |
| WO2011050326A1 (en) | 2009-10-23 | 2011-04-28 | Genomatica, Inc. | Microorganisms for the production of aniline |
| CA2787314A1 (en) | 2010-01-29 | 2011-08-04 | Genomatica, Inc. | Microorganisms and methods for the biosynthesis of p-toluate and terephthalate |
| US9023636B2 (en) | 2010-04-30 | 2015-05-05 | Genomatica, Inc. | Microorganisms and methods for the biosynthesis of propylene |
| ES2650245T3 (es) | 2010-07-14 | 2018-01-17 | Dpx Holdings B.V. | Método enzimático para aminación (R)-selectiva |
| BR112013001635A2 (pt) | 2010-07-26 | 2016-05-24 | Genomatica Inc | micro-organismo e métodos para a biossíntese de aromáticos, 2, 4-pentadienoato e 1,3-butadieno |
| CN109337832B (zh) * | 2018-03-14 | 2021-06-15 | 重庆理工大学 | 一种耐高氨氮异养硝化-好氧反硝化的苍白杆菌及其应用 |
| CN110317742B (zh) * | 2019-03-22 | 2021-01-01 | 厦门大学 | 一株耐铬的石油烃降解菌株Tph3-32及其应用 |
Family Cites Families (8)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DK261685A (da) * | 1985-06-11 | 1986-12-12 | Novo Industri As | Fremgangsmaade til fremstilling af optisk aktive, organiske forbindelser |
| JPS63129984A (ja) * | 1986-11-21 | 1988-06-02 | Toray Ind Inc | α−アミノ−ε−カプロラクタム・ラセマ−ゼ |
| KR890701753A (ko) * | 1987-08-17 | 1989-12-21 | 원본미기재 | 아미노산 아미드의 라세미화 방법 |
| DE3816063A1 (de) * | 1988-05-06 | 1989-11-23 | Schering Ag | Verfahren zur herstellung von l-aminosaeuren und aminosaeure-amiden |
| EP0383403A1 (en) * | 1989-02-16 | 1990-08-22 | Stamicarbon B.V. | Process for preparation of organic chemicals |
| NL9100038A (nl) * | 1991-01-11 | 1992-08-03 | Stamicarbon | Enzym-gekatalyseerde bereiding van optisch aktieve carbonzuren. |
| WO2000066751A1 (en) | 1999-04-29 | 2000-11-09 | Dsm N.V. | Expression cassette for efficient production of a protein |
| WO2005080584A1 (ja) | 2004-02-24 | 2005-09-01 | Kansai Technology Licensing Organization Co., Ltd. | α-アミノ-ε-カプロラクタムラセマーゼを用いた、D及びL-アミノ酸アミドの混合物の製造方法、D又はL-アミノ酸の製造方法、D又はL-アミノ酸アミドの製造方法 |
-
2003
- 2003-06-13 ES ES03733629T patent/ES2285128T3/es not_active Expired - Lifetime
- 2003-06-13 AU AU2003238717A patent/AU2003238717A1/en not_active Abandoned
- 2003-06-13 EP EP03733629A patent/EP1513946B1/en not_active Expired - Lifetime
- 2003-06-13 CN CNB038189984A patent/CN100471950C/zh not_active Expired - Fee Related
- 2003-06-13 DE DE60313866T patent/DE60313866T2/de not_active Expired - Lifetime
- 2003-06-13 AT AT03733629T patent/ATE362544T1/de not_active IP Right Cessation
- 2003-06-13 JP JP2004513504A patent/JP4402587B2/ja not_active Expired - Fee Related
- 2003-06-13 WO PCT/NL2003/000423 patent/WO2003106691A1/en not_active Ceased
- 2003-12-09 US US10/732,011 patent/US7371555B2/en not_active Expired - Fee Related
Also Published As
| Publication number | Publication date |
|---|---|
| ATE362544T1 (de) | 2007-06-15 |
| US7371555B2 (en) | 2008-05-13 |
| WO2003106691A1 (en) | 2003-12-24 |
| DE60313866T2 (de) | 2008-04-17 |
| EP1513946A1 (en) | 2005-03-16 |
| JP2005529611A (ja) | 2005-10-06 |
| US20040248274A1 (en) | 2004-12-09 |
| CN1675371A (zh) | 2005-09-28 |
| AU2003238717A1 (en) | 2003-12-31 |
| EP1513946B1 (en) | 2007-05-16 |
| CN100471950C (zh) | 2009-03-25 |
| JP4402587B2 (ja) | 2010-01-20 |
| DE60313866D1 (de) | 2007-06-28 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| ES2285128T3 (es) | Polipeptidos que tienen actividad amida del alfa-h-alfa aminoacido racemasa y los acidos nucleicos que codifican los mismos. | |
| US7098019B2 (en) | DNA for encoding D-hydantoin hydrolases, DNA for encoding N-carbamyl-D-amino acid hydrolases, recombinant DNA containing the genes, cells transformed with the recombinant DNA, methods for producing proteins utilizing the transformed cells and methods for producing D-amino acids | |
| KR100266920B1 (ko) | 내열성이 향상된 데카르바밀라아제를 코딩하는 dna 및 그의 용도 | |
| Nanba et al. | Isolation of Agrobacterium sp. strain KNK712 that produces N-carbamyl-D-amino acid amidohydrolase, cloning of the gene for this enzyme, and properties of the enzyme | |
| US8460902B1 (en) | DNA encoding hydantoinase, DNA encoding N-carbamyl-L-amino acid hydrolase, recombinant DNA, transformed cell, method of producing protein, and method of producing optically active amino acid | |
| CN100406553C (zh) | 生产D-N-氨基甲酰基-α-氨基酸的方法 | |
| US20030148472A1 (en) | DNA for encoding D-hydantoin hydrolases, DNA for encoding N-carbamyl-D-amino acid hydrolases, recombinant DNA containing the genes, cells transformed with the recombinant DNA, methods for producing proteins utilizing the transformed cells and methods for producing D-amino acids | |
| JPH0851992A (ja) | Ｄ−α−アミノ酸の製造方法 | |
| EP1249494B1 (en) | Process for the biological production of l-pipecolic acid | |
| ES2286262T3 (es) | Secuencias de uh acido nucleico que codifican para amidasas enantio-selectivas. | |
| JPH09173068A (ja) | Ｄ‐Ｎ‐α‐カルバモイラーゼの熱安定性変異体 | |
| EP1506294B1 (en) | Hydantoin racemase | |
| JP2007189949A (ja) | 新規ヒダントイナーゼ及び光学活性アミノ酸誘導体の製造方法 | |
| WO2025241319A1 (zh) | 二氨基庚二酸脱氢酶突变体及在d-氨基酸合成中的应用 | |
| KR100244055B1 (ko) | 디-엔-카르바모일-알파-아미노산의 제조법 | |
| JP4081124B2 (ja) | Ｄ−Ｎ−カルバモイル−α−アミノ酸の製造法 | |
| Jiwaji et al. | Enhanced hydantoin-hydrolyzing enzyme activity in an Agrobacterium tumefaciens strain with two distinct N-carbamoylases | |
| US20080261268A1 (en) | 5-Substituted Hydantoin Racemase, Dna Encoding the Same, Recombinant Dna, Transformed Cell, and Process for Production of Optically Active N-Carbamylamino Acid or Optically Active Amino Acid | |
| Nojiri | Studies on enzymatic synthesis of optically active amides for pharmaceutical intermediates | |
| JPWO1996020275A1 (ja) | Ｄ−Ｎ−カルバモイル−α−アミノ酸の製造法 |