KR20000048776A - 직접발효 방법에 의한 디-아미노산의 제조방법 - Google Patents
직접발효 방법에 의한 디-아미노산의 제조방법 Download PDFInfo
- Publication number
- KR20000048776A KR20000048776A KR1019990702764A KR19997002764A KR20000048776A KR 20000048776 A KR20000048776 A KR 20000048776A KR 1019990702764 A KR1019990702764 A KR 1019990702764A KR 19997002764 A KR19997002764 A KR 19997002764A KR 20000048776 A KR20000048776 A KR 20000048776A
- Authority
- KR
- South Korea
- Prior art keywords
- gene
- cell
- aminodiaminase
- phenylalanine
- 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.)
- Withdrawn
Links
- 150000008574 D-amino acids Chemical class 0.000 title claims abstract description 60
- 238000002360 preparation method Methods 0.000 title abstract description 14
- 108090000623 proteins and genes Proteins 0.000 claims abstract description 114
- 238000000034 method Methods 0.000 claims abstract description 74
- 238000004519 manufacturing process Methods 0.000 claims abstract description 34
- COLNVLDHVKWLRT-MRVPVSSYSA-N D-phenylalanine Chemical compound OC(=O)[C@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-MRVPVSSYSA-N 0.000 claims abstract description 32
- 229930182832 D-phenylalanine Natural products 0.000 claims abstract description 32
- BTNMPGBKDVTSJY-UHFFFAOYSA-N keto-phenylpyruvic acid Chemical compound OC(=O)C(=O)CC1=CC=CC=C1 BTNMPGBKDVTSJY-UHFFFAOYSA-N 0.000 claims abstract description 18
- 239000006143 cell culture medium Substances 0.000 claims abstract description 15
- 230000001965 increasing effect Effects 0.000 claims abstract description 10
- 238000012258 culturing Methods 0.000 claims abstract description 6
- 239000013612 plasmid Substances 0.000 claims description 72
- 239000000758 substrate Substances 0.000 claims description 43
- QNAYBMKLOCPYGJ-UHFFFAOYSA-N D-alpha-Ala Natural products CC([NH3+])C([O-])=O QNAYBMKLOCPYGJ-UHFFFAOYSA-N 0.000 claims description 41
- QNAYBMKLOCPYGJ-UWTATZPHSA-N L-Alanine Natural products C[C@@H](N)C(O)=O QNAYBMKLOCPYGJ-UWTATZPHSA-N 0.000 claims description 41
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 claims description 36
- 229960003767 alanine Drugs 0.000 claims description 25
- 241000588724 Escherichia coli Species 0.000 claims description 24
- 150000008575 L-amino acids Chemical class 0.000 claims description 21
- 229960005190 phenylalanine Drugs 0.000 claims description 21
- 239000000203 mixture Substances 0.000 claims description 20
- 241000194110 Bacillus sp. (in: Bacteria) Species 0.000 claims description 15
- 235000020094 liqueur Nutrition 0.000 claims description 14
- 108010041525 Alanine racemase Proteins 0.000 claims description 13
- 108090001066 Racemases and epimerases Proteins 0.000 claims description 13
- 241000193830 Bacillus <bacterium> Species 0.000 claims description 11
- 230000001580 bacterial effect Effects 0.000 claims description 11
- 101150047092 dadA gene Proteins 0.000 claims description 11
- 206010064571 Gene mutation Diseases 0.000 claims description 8
- 101150018055 aroH gene Proteins 0.000 claims description 8
- 239000001963 growth medium Substances 0.000 claims description 8
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 claims description 8
- 235000014705 isoleucine Nutrition 0.000 claims description 7
- 229960000310 isoleucine Drugs 0.000 claims description 7
- AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 claims description 7
- 101150023849 pheA gene Proteins 0.000 claims description 7
- 241001087672 Cosenzaea myxofaciens Species 0.000 claims description 6
- 108700016167 Glutamate racemases Proteins 0.000 claims description 6
- AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 claims description 6
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 claims description 6
- 235000008729 phenylalanine Nutrition 0.000 claims description 6
- WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 0.000 claims description 5
- QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 claims description 5
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 claims description 5
- 241000588770 Proteus mirabilis Species 0.000 claims description 5
- 241000293869 Salmonella enterica subsp. enterica serovar Typhimurium Species 0.000 claims description 5
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 claims description 5
- 229960004441 tyrosine Drugs 0.000 claims description 5
- 235000002374 tyrosine Nutrition 0.000 claims description 5
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 claims description 5
- 241000894006 Bacteria Species 0.000 claims description 4
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 claims description 4
- 229930195714 L-glutamate Natural products 0.000 claims description 4
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 claims description 4
- KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 claims description 4
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 claims description 4
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 claims description 4
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 claims description 4
- 235000005772 leucine Nutrition 0.000 claims description 4
- 229960003136 leucine Drugs 0.000 claims description 4
- 235000014393 valine Nutrition 0.000 claims description 4
- 229960004295 valine Drugs 0.000 claims description 4
- 239000004474 valine Substances 0.000 claims description 4
- QDGAVODICPCDMU-UHFFFAOYSA-N 2-amino-3-[3-[bis(2-chloroethyl)amino]phenyl]propanoic acid Chemical compound OC(=O)C(N)CC1=CC=CC(N(CCCl)CCCl)=C1 QDGAVODICPCDMU-UHFFFAOYSA-N 0.000 claims description 3
- 239000004475 Arginine Substances 0.000 claims description 3
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 claims description 3
- 101000798396 Bacillus licheniformis Phenylalanine racemase [ATP hydrolyzing] Proteins 0.000 claims description 3
- 244000063299 Bacillus subtilis Species 0.000 claims description 3
- 235000014469 Bacillus subtilis Nutrition 0.000 claims description 3
- 241000186146 Brevibacterium Species 0.000 claims description 3
- 241000186216 Corynebacterium Species 0.000 claims description 3
- 241000588748 Klebsiella Species 0.000 claims description 3
- DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 claims description 3
- RHGKLRLOHDJJDR-BYPYZUCNSA-N L-citrulline Chemical compound NC(=O)NCCC[C@H]([NH3+])C([O-])=O RHGKLRLOHDJJDR-BYPYZUCNSA-N 0.000 claims description 3
- ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical compound OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 0.000 claims description 3
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 claims description 3
- LRQKBLKVPFOOQJ-YFKPBYRVSA-N L-norleucine Chemical compound CCCC[C@H]([NH3+])C([O-])=O LRQKBLKVPFOOQJ-YFKPBYRVSA-N 0.000 claims description 3
- RHGKLRLOHDJJDR-UHFFFAOYSA-N Ndelta-carbamoyl-DL-ornithine Natural products OC(=O)C(N)CCCNC(N)=O RHGKLRLOHDJJDR-UHFFFAOYSA-N 0.000 claims description 3
- 241000589516 Pseudomonas Species 0.000 claims description 3
- 241000607142 Salmonella Species 0.000 claims description 3
- 239000002253 acid Substances 0.000 claims description 3
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 claims description 3
- 229960003121 arginine Drugs 0.000 claims description 3
- 229960001230 asparagine Drugs 0.000 claims description 3
- 235000009582 asparagine Nutrition 0.000 claims description 3
- 238000004113 cell culture Methods 0.000 claims description 3
- 229960002173 citrulline Drugs 0.000 claims description 3
- 235000013477 citrulline Nutrition 0.000 claims description 3
- 229960002433 cysteine Drugs 0.000 claims description 3
- 235000018417 cysteine Nutrition 0.000 claims description 3
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 claims description 3
- 229960002885 histidine Drugs 0.000 claims description 3
- 235000014304 histidine Nutrition 0.000 claims description 3
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 claims description 3
- 229930182817 methionine Natural products 0.000 claims description 3
- 108090000554 phenylalanine racemase (ATP-hydrolyzing) Proteins 0.000 claims description 3
- 241000193385 Geobacillus stearothermophilus Species 0.000 claims description 2
- MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical compound OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 claims 2
- SNDPXSYFESPGGJ-BYPYZUCNSA-N L-2-aminopentanoic acid Chemical compound CCC[C@H](N)C(O)=O SNDPXSYFESPGGJ-BYPYZUCNSA-N 0.000 claims 2
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 claims 2
- WTDRDQBEARUVNC-LURJTMIESA-N L-DOPA Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C(O)=C1 WTDRDQBEARUVNC-LURJTMIESA-N 0.000 claims 2
- AHLPHDHHMVZTML-BYPYZUCNSA-N L-Ornithine Chemical compound NCCC[C@H](N)C(O)=O AHLPHDHHMVZTML-BYPYZUCNSA-N 0.000 claims 2
- 125000003412 L-alanyl group Chemical group [H]N([H])[C@@](C([H])([H])[H])(C(=O)[*])[H] 0.000 claims 2
- ODKSFYDXXFIFQN-BYPYZUCNSA-P L-argininium(2+) Chemical compound NC(=[NH2+])NCCC[C@H]([NH3+])C(O)=O ODKSFYDXXFIFQN-BYPYZUCNSA-P 0.000 claims 2
- HNDVDQJCIGZPNO-YFKPBYRVSA-N L-histidine Chemical compound OC(=O)[C@@H](N)CC1=CN=CN1 HNDVDQJCIGZPNO-YFKPBYRVSA-N 0.000 claims 2
- KDXKERNSBIXSRK-YFKPBYRVSA-N L-lysine Chemical compound NCCCC[C@H](N)C(O)=O KDXKERNSBIXSRK-YFKPBYRVSA-N 0.000 claims 2
- SNDPXSYFESPGGJ-UHFFFAOYSA-N L-norVal-OH Natural products CCCC(N)C(O)=O SNDPXSYFESPGGJ-UHFFFAOYSA-N 0.000 claims 2
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 claims 2
- 239000004472 Lysine Substances 0.000 claims 2
- 241000192041 Micrococcus Species 0.000 claims 2
- AHLPHDHHMVZTML-UHFFFAOYSA-N Orn-delta-NH2 Natural products NCCCC(N)C(O)=O AHLPHDHHMVZTML-UHFFFAOYSA-N 0.000 claims 2
- UTJLXEIPEHZYQJ-UHFFFAOYSA-N Ornithine Natural products OC(=O)C(C)CCCN UTJLXEIPEHZYQJ-UHFFFAOYSA-N 0.000 claims 2
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 claims 2
- 229940009098 aspartate Drugs 0.000 claims 2
- CKLJMWTZIZZHCS-REOHCLBHSA-L aspartate group Chemical group N[C@@H](CC(=O)[O-])C(=O)[O-] CKLJMWTZIZZHCS-REOHCLBHSA-L 0.000 claims 2
- 239000003795 chemical substances by application Substances 0.000 claims 2
- 229960002743 glutamine Drugs 0.000 claims 2
- 229960004502 levodopa Drugs 0.000 claims 2
- 235000018977 lysine Nutrition 0.000 claims 2
- 229960003646 lysine Drugs 0.000 claims 2
- 229960004452 methionine Drugs 0.000 claims 2
- 229960003104 ornithine Drugs 0.000 claims 2
- 229960001153 serine Drugs 0.000 claims 2
- 229960004799 tryptophan Drugs 0.000 claims 2
- 125000000741 isoleucyl group Chemical group [H]N([H])C(C(C([H])([H])[H])C([H])([H])C([H])([H])[H])C(=O)O* 0.000 claims 1
- 239000000463 material Substances 0.000 abstract description 4
- 210000004027 cell Anatomy 0.000 description 88
- 239000012634 fragment Substances 0.000 description 48
- 102000004190 Enzymes Human genes 0.000 description 43
- 108090000790 Enzymes Proteins 0.000 description 43
- 229940088598 enzyme Drugs 0.000 description 43
- 229940024606 amino acid Drugs 0.000 description 27
- 235000001014 amino acid Nutrition 0.000 description 27
- 150000001413 amino acids Chemical class 0.000 description 27
- 150000004715 keto acids Chemical class 0.000 description 26
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 23
- 238000000855 fermentation Methods 0.000 description 23
- 230000004151 fermentation Effects 0.000 description 23
- 239000002243 precursor Substances 0.000 description 21
- 108020004414 DNA Proteins 0.000 description 20
- 239000000047 product Substances 0.000 description 20
- 125000003277 amino group Chemical group 0.000 description 16
- 238000006243 chemical reaction Methods 0.000 description 11
- 239000002609 medium Substances 0.000 description 11
- 238000003556 assay Methods 0.000 description 10
- 210000000349 chromosome Anatomy 0.000 description 10
- 101150049467 dadX gene Proteins 0.000 description 10
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 10
- 101150012893 dat gene Proteins 0.000 description 9
- 239000000499 gel Substances 0.000 description 9
- 238000006276 transfer reaction Methods 0.000 description 9
- 239000000284 extract Substances 0.000 description 8
- 101150099953 ilvE gene Proteins 0.000 description 8
- LWIHDJKSTIGBAC-UHFFFAOYSA-K tripotassium phosphate Chemical compound [K+].[K+].[K+].[O-]P([O-])([O-])=O LWIHDJKSTIGBAC-UHFFFAOYSA-K 0.000 description 8
- 101150028338 tyrB gene Proteins 0.000 description 8
- 239000013598 vector Substances 0.000 description 8
- 229930195713 D-glutamate Natural products 0.000 description 7
- WHUUTDBJXJRKMK-GSVOUGTGSA-N D-glutamic acid Chemical compound OC(=O)[C@H](N)CCC(O)=O WHUUTDBJXJRKMK-GSVOUGTGSA-N 0.000 description 7
- 239000003155 DNA primer Substances 0.000 description 7
- 101100492609 Talaromyces wortmannii astC gene Proteins 0.000 description 7
- 101150116772 aatA gene Proteins 0.000 description 7
- 101150005925 aspC gene Proteins 0.000 description 7
- 230000015572 biosynthetic process Effects 0.000 description 7
- 238000003776 cleavage reaction Methods 0.000 description 7
- 101150100742 dapL gene Proteins 0.000 description 7
- 239000013615 primer Substances 0.000 description 7
- 230000007017 scission Effects 0.000 description 7
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 6
- CSNNHWWHGAXBCP-UHFFFAOYSA-L Magnesium sulfate Chemical compound [Mg+2].[O-][S+2]([O-])([O-])[O-] CSNNHWWHGAXBCP-UHFFFAOYSA-L 0.000 description 6
- 102000004879 Racemases and epimerases Human genes 0.000 description 6
- 101100055397 Wigglesworthia glossinidia brevipalpis alr gene Proteins 0.000 description 6
- 239000013611 chromosomal DNA Substances 0.000 description 6
- 238000001962 electrophoresis Methods 0.000 description 6
- 229920000936 Agarose Polymers 0.000 description 5
- 235000004279 alanine Nutrition 0.000 description 5
- 210000002421 cell wall Anatomy 0.000 description 5
- 238000005119 centrifugation Methods 0.000 description 5
- 238000009826 distribution Methods 0.000 description 5
- 241001302584 Escherichia coli str. K-12 substr. W3110 Species 0.000 description 4
- 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 4
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 4
- ISWSIDIOOBJBQZ-UHFFFAOYSA-N Phenol Chemical compound OC1=CC=CC=C1 ISWSIDIOOBJBQZ-UHFFFAOYSA-N 0.000 description 4
- 238000012181 QIAquick gel extraction kit Methods 0.000 description 4
- 229940041514 candida albicans extract Drugs 0.000 description 4
- 229960005091 chloramphenicol Drugs 0.000 description 4
- 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 4
- 238000010586 diagram Methods 0.000 description 4
- 239000012153 distilled water Substances 0.000 description 4
- 230000000694 effects Effects 0.000 description 4
- 239000008103 glucose Substances 0.000 description 4
- 229930027917 kanamycin Natural products 0.000 description 4
- 229960000318 kanamycin Drugs 0.000 description 4
- 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 4
- 229930182823 kanamycin A Natural products 0.000 description 4
- 230000000670 limiting effect Effects 0.000 description 4
- 229930027945 nicotinamide-adenine dinucleotide Natural products 0.000 description 4
- 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 4
- 230000003287 optical effect Effects 0.000 description 4
- 239000008188 pellet Substances 0.000 description 4
- 229910000160 potassium phosphate Inorganic materials 0.000 description 4
- 235000011009 potassium phosphates Nutrition 0.000 description 4
- 230000008569 process Effects 0.000 description 4
- 235000018102 proteins Nutrition 0.000 description 4
- 102000004169 proteins and genes Human genes 0.000 description 4
- 238000000926 separation method Methods 0.000 description 4
- 241000894007 species Species 0.000 description 4
- 239000000126 substance Substances 0.000 description 4
- 238000003786 synthesis reaction Methods 0.000 description 4
- RWQNBRDOKXIBIV-UHFFFAOYSA-N thymine Chemical compound CC1=CNC(=O)NC1=O RWQNBRDOKXIBIV-UHFFFAOYSA-N 0.000 description 4
- 239000012138 yeast extract Substances 0.000 description 4
- 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 3
- 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 3
- WEVYAHXRMPXWCK-UHFFFAOYSA-N Acetonitrile Chemical compound CC#N WEVYAHXRMPXWCK-UHFFFAOYSA-N 0.000 description 3
- 108700039691 Genetic Promoter Regions Proteins 0.000 description 3
- 102000003855 L-lactate dehydrogenase Human genes 0.000 description 3
- 108700023483 L-lactate dehydrogenases Proteins 0.000 description 3
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 3
- -1 Ornithine 5-amino-2-oxopentanoic acid Serine Chemical compound 0.000 description 3
- LCTONWCANYUPML-UHFFFAOYSA-M Pyruvate Chemical compound CC(=O)C([O-])=O LCTONWCANYUPML-UHFFFAOYSA-M 0.000 description 3
- 102000003929 Transaminases Human genes 0.000 description 3
- 108090000340 Transaminases Proteins 0.000 description 3
- 101150070828 alr gene Proteins 0.000 description 3
- FRHBOQMZUOWXQL-UHFFFAOYSA-L ammonium ferric citrate Chemical compound [NH4+].[Fe+3].[O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O FRHBOQMZUOWXQL-UHFFFAOYSA-L 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
- 238000004458 analytical method Methods 0.000 description 3
- 239000000872 buffer Substances 0.000 description 3
- 210000004899 c-terminal region Anatomy 0.000 description 3
- 230000008859 change Effects 0.000 description 3
- 238000012217 deletion Methods 0.000 description 3
- 230000037430 deletion Effects 0.000 description 3
- ZPWVASYFFYYZEW-UHFFFAOYSA-L dipotassium hydrogen phosphate Chemical compound [K+].[K+].OP([O-])([O-])=O ZPWVASYFFYYZEW-UHFFFAOYSA-L 0.000 description 3
- 229960004642 ferric ammonium citrate Drugs 0.000 description 3
- 238000010438 heat treatment Methods 0.000 description 3
- 238000003780 insertion Methods 0.000 description 3
- 230000037431 insertion Effects 0.000 description 3
- 239000004313 iron ammonium citrate Substances 0.000 description 3
- 235000000011 iron ammonium citrate Nutrition 0.000 description 3
- 238000002955 isolation Methods 0.000 description 3
- 229910052943 magnesium sulfate Inorganic materials 0.000 description 3
- 235000019341 magnesium sulphate Nutrition 0.000 description 3
- 230000004048 modification Effects 0.000 description 3
- 238000012986 modification Methods 0.000 description 3
- 238000012261 overproduction Methods 0.000 description 3
- 230000036961 partial effect Effects 0.000 description 3
- 229940076788 pyruvate Drugs 0.000 description 3
- 108091008146 restriction endonucleases Proteins 0.000 description 3
- 238000010561 standard procedure Methods 0.000 description 3
- 238000004809 thin layer chromatography Methods 0.000 description 3
- XNIHZNNZJHYHLC-UHFFFAOYSA-N 2-oxohexanoic acid Chemical compound CCCCC(=O)C(O)=O XNIHZNNZJHYHLC-UHFFFAOYSA-N 0.000 description 2
- QHKABHOOEWYVLI-UHFFFAOYSA-N 3-methyl-2-oxobutanoic acid Chemical compound CC(C)C(=O)C(O)=O QHKABHOOEWYVLI-UHFFFAOYSA-N 0.000 description 2
- 108700028369 Alleles Proteins 0.000 description 2
- 101000644386 Brevibacillus parabrevis Phenylalanine racemase [ATP-hydrolyzing] Proteins 0.000 description 2
- 101000906861 Chondromyces crocatus ATP-dependent tyrosine adenylase Proteins 0.000 description 2
- 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 2
- 241001646716 Escherichia coli K-12 Species 0.000 description 2
- 239000004471 Glycine Substances 0.000 description 2
- AYFVYJQAPQTCCC-GBXIJSLDSA-N L-threonine Chemical compound C[C@@H](O)[C@H](N)C(O)=O AYFVYJQAPQTCCC-GBXIJSLDSA-N 0.000 description 2
- 101500006448 Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97) Endonuclease PI-MboI Proteins 0.000 description 2
- 101100109871 Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) aro-8 gene Proteins 0.000 description 2
- 108091034117 Oligonucleotide Proteins 0.000 description 2
- 229910019142 PO4 Inorganic materials 0.000 description 2
- DTBNBXWJWCWCIK-UHFFFAOYSA-N Phosphoenolpyruvic acid Natural products OC(=O)C(=C)OP(O)(O)=O DTBNBXWJWCWCIK-UHFFFAOYSA-N 0.000 description 2
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 description 2
- VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 description 2
- DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical compound [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 description 2
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 2
- 239000004473 Threonine Substances 0.000 description 2
- 239000007983 Tris buffer Substances 0.000 description 2
- 238000010521 absorption reaction Methods 0.000 description 2
- 230000003321 amplification Effects 0.000 description 2
- 239000002518 antifoaming agent Substances 0.000 description 2
- 230000008901 benefit Effects 0.000 description 2
- 239000003990 capacitor Substances 0.000 description 2
- 125000004432 carbon atom Chemical group C* 0.000 description 2
- 230000029087 digestion Effects 0.000 description 2
- 230000014509 gene expression Effects 0.000 description 2
- 230000003834 intracellular effect Effects 0.000 description 2
- 230000002427 irreversible effect Effects 0.000 description 2
- 229940099596 manganese sulfate Drugs 0.000 description 2
- 239000011702 manganese sulphate Substances 0.000 description 2
- 235000007079 manganese sulphate Nutrition 0.000 description 2
- SQQMAOCOWKFBNP-UHFFFAOYSA-L manganese(II) sulfate Chemical compound [Mn+2].[O-]S([O-])(=O)=O SQQMAOCOWKFBNP-UHFFFAOYSA-L 0.000 description 2
- 239000003550 marker Substances 0.000 description 2
- 244000005700 microbiome Species 0.000 description 2
- 238000010369 molecular cloning Methods 0.000 description 2
- 238000003199 nucleic acid amplification method Methods 0.000 description 2
- 230000003647 oxidation Effects 0.000 description 2
- 238000007254 oxidation reaction Methods 0.000 description 2
- 230000037361 pathway Effects 0.000 description 2
- 239000010452 phosphate Substances 0.000 description 2
- 239000002244 precipitate Substances 0.000 description 2
- 238000000746 purification Methods 0.000 description 2
- 239000011541 reaction mixture Substances 0.000 description 2
- 239000001632 sodium acetate Substances 0.000 description 2
- 235000017281 sodium acetate Nutrition 0.000 description 2
- 239000000243 solution Substances 0.000 description 2
- 238000003860 storage Methods 0.000 description 2
- 229940113082 thymine Drugs 0.000 description 2
- 238000010361 transduction Methods 0.000 description 2
- 230000026683 transduction Effects 0.000 description 2
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 2
- OSBLTNPMIGYQGY-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;2-[2-[bis(carboxymethyl)amino]ethyl-(carboxymethyl)amino]acetic acid;boric acid Chemical compound OB(O)O.OCC(N)(CO)CO.OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O OSBLTNPMIGYQGY-UHFFFAOYSA-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
- PIMRQHMOUHWMDK-UHFFFAOYSA-N 3,3-dihydroxy-2-oxo-3-phenylpropanoic acid Chemical compound OC(=O)C(=O)C(O)(O)C1=CC=CC=C1 PIMRQHMOUHWMDK-UHFFFAOYSA-N 0.000 description 1
- 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 1
- 108010080376 3-Deoxy-7-Phosphoheptulonate Synthase Proteins 0.000 description 1
- HHDDCCUIIUWNGJ-UHFFFAOYSA-N 3-hydroxypyruvic acid Chemical compound OCC(=O)C(O)=O HHDDCCUIIUWNGJ-UHFFFAOYSA-N 0.000 description 1
- BKAJNAXTPSGJCU-UHFFFAOYSA-N 4-methyl-2-oxopentanoic acid Chemical compound CC(C)CC(=O)C(O)=O BKAJNAXTPSGJCU-UHFFFAOYSA-N 0.000 description 1
- SXFSQZDSUWACKX-UHFFFAOYSA-N 4-methylthio-2-oxobutanoic acid Chemical compound CSCCC(=O)C(O)=O SXFSQZDSUWACKX-UHFFFAOYSA-N 0.000 description 1
- ARBHXJXXVVHMET-UHFFFAOYSA-N 5-guanidino-2-oxopentanoic acid Chemical compound NC(=[NH2+])NCCCC(=O)C([O-])=O ARBHXJXXVVHMET-UHFFFAOYSA-N 0.000 description 1
- GWENQMVPLJAMAE-UHFFFAOYSA-N 6-amino-2-oxohexanoic acid Chemical compound [NH3+]CCCCC(=O)C([O-])=O GWENQMVPLJAMAE-UHFFFAOYSA-N 0.000 description 1
- PJWIPEXIFFQAQZ-PUFIMZNGSA-N 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonic acid Chemical compound OP(=O)(O)OC[C@@H](O)[C@@H](O)[C@H](O)CC(=O)C(O)=O PJWIPEXIFFQAQZ-PUFIMZNGSA-N 0.000 description 1
- 239000004254 Ammonium phosphate Substances 0.000 description 1
- 108020000946 Bacterial DNA Proteins 0.000 description 1
- 241000283690 Bos taurus Species 0.000 description 1
- 101000583086 Bunodosoma granuliferum Delta-actitoxin-Bgr2b Proteins 0.000 description 1
- 125000001433 C-terminal amino-acid group Chemical group 0.000 description 1
- RUCODEBXOVPJSO-JZGIKJSDSA-N C1(=CC=CC=C1)CC(C(=O)O)=O.N[C@@H](CC1=CC=CC=C1)C(=O)O.C(C(=O)C)(=O)O Chemical compound C1(=CC=CC=C1)CC(C(=O)O)=O.N[C@@H](CC1=CC=CC=C1)C(=O)O.C(C(=O)C)(=O)O RUCODEBXOVPJSO-JZGIKJSDSA-N 0.000 description 1
- 206010057248 Cell death Diseases 0.000 description 1
- 108091026890 Coding region Proteins 0.000 description 1
- MNQZXJOMYWMBOU-VKHMYHEASA-N D-glyceraldehyde Chemical compound OC[C@@H](O)C=O MNQZXJOMYWMBOU-VKHMYHEASA-N 0.000 description 1
- 102000016928 DNA-directed DNA polymerase Human genes 0.000 description 1
- 108010014303 DNA-directed DNA polymerase Proteins 0.000 description 1
- 108010067770 Endopeptidase K Proteins 0.000 description 1
- 241000701959 Escherichia virus Lambda Species 0.000 description 1
- 241000702191 Escherichia virus P1 Species 0.000 description 1
- 108010010803 Gelatin Proteins 0.000 description 1
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 1
- ZHLWCBHWYUISFY-UHFFFAOYSA-N Hydroxyphenylpyruvic acid Chemical compound OC(=O)C(=O)C(O)C1=CC=CC=C1 ZHLWCBHWYUISFY-UHFFFAOYSA-N 0.000 description 1
- 241000193386 Lysinibacillus sphaericus Species 0.000 description 1
- 241001529936 Murinae Species 0.000 description 1
- 101100202339 Mus musculus Slc6a13 gene Proteins 0.000 description 1
- 102000006746 NADH Dehydrogenase Human genes 0.000 description 1
- 108010086428 NADH Dehydrogenase Proteins 0.000 description 1
- 108091028043 Nucleic acid sequence Proteins 0.000 description 1
- 108020002230 Pancreatic Ribonuclease Proteins 0.000 description 1
- 102000005891 Pancreatic ribonuclease Human genes 0.000 description 1
- FSXRLASFHBWESK-HOTGVXAUSA-N Phe-Tyr Chemical compound C([C@H](N)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(O)=O)C1=CC=CC=C1 FSXRLASFHBWESK-HOTGVXAUSA-N 0.000 description 1
- 102000004160 Phosphoric Monoester Hydrolases Human genes 0.000 description 1
- 108090000608 Phosphoric Monoester Hydrolases Proteins 0.000 description 1
- 101100202330 Rattus norvegicus Slc6a11 gene Proteins 0.000 description 1
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 1
- 239000008051 TBE buffer Substances 0.000 description 1
- 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 1
- 239000011543 agarose gel Substances 0.000 description 1
- 150000004716 alpha keto acids Chemical class 0.000 description 1
- 229910000148 ammonium phosphate Inorganic materials 0.000 description 1
- 235000019289 ammonium phosphates Nutrition 0.000 description 1
- 238000000137 annealing Methods 0.000 description 1
- 239000003242 anti bacterial agent Substances 0.000 description 1
- 229940088710 antibiotic agent Drugs 0.000 description 1
- 239000007864 aqueous solution Substances 0.000 description 1
- 235000003704 aspartic acid Nutrition 0.000 description 1
- 230000008840 asymmetric binding Effects 0.000 description 1
- OQFSQFPPLPISGP-UHFFFAOYSA-N beta-carboxyaspartic acid Natural products OC(=O)C(N)C(C(O)=O)C(O)=O OQFSQFPPLPISGP-UHFFFAOYSA-N 0.000 description 1
- 230000002457 bidirectional effect Effects 0.000 description 1
- 230000006696 biosynthetic metabolic pathway Effects 0.000 description 1
- 229910052799 carbon Inorganic materials 0.000 description 1
- 230000015556 catabolic process Effects 0.000 description 1
- 238000006555 catalytic reaction Methods 0.000 description 1
- 230000032823 cell division Effects 0.000 description 1
- 230000010261 cell growth Effects 0.000 description 1
- 230000006037 cell lysis Effects 0.000 description 1
- 239000006285 cell suspension Substances 0.000 description 1
- 238000004587 chromatography analysis Methods 0.000 description 1
- 230000002759 chromosomal effect Effects 0.000 description 1
- 238000010367 cloning Methods 0.000 description 1
- 230000002860 competitive effect Effects 0.000 description 1
- 238000012937 correction Methods 0.000 description 1
- 230000009089 cytolysis Effects 0.000 description 1
- 230000001086 cytosolic effect Effects 0.000 description 1
- SUYVUBYJARFZHO-RRKCRQDMSA-N dATP Chemical compound C1=NC=2C(N)=NC=NC=2N1[C@H]1C[C@H](O)[C@@H](COP(O)(=O)OP(O)(=O)OP(O)(O)=O)O1 SUYVUBYJARFZHO-RRKCRQDMSA-N 0.000 description 1
- SUYVUBYJARFZHO-UHFFFAOYSA-N dATP Natural products C1=NC=2C(N)=NC=NC=2N1C1CC(O)C(COP(O)(=O)OP(O)(=O)OP(O)(O)=O)O1 SUYVUBYJARFZHO-UHFFFAOYSA-N 0.000 description 1
- RGWHQCVHVJXOKC-SHYZEUOFSA-J dCTP(4-) Chemical compound O=C1N=C(N)C=CN1[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OP([O-])([O-])=O)[C@@H](O)C1 RGWHQCVHVJXOKC-SHYZEUOFSA-J 0.000 description 1
- HAAZLUGHYHWQIW-KVQBGUIXSA-N dGTP Chemical compound C1=NC=2C(=O)NC(N)=NC=2N1[C@H]1C[C@H](O)[C@@H](COP(O)(=O)OP(O)(=O)OP(O)(O)=O)O1 HAAZLUGHYHWQIW-KVQBGUIXSA-N 0.000 description 1
- NHVNXKFIZYSCEB-XLPZGREQSA-N dTTP Chemical compound O=C1NC(=O)C(C)=CN1[C@@H]1O[C@H](COP(O)(=O)OP(O)(=O)OP(O)(O)=O)[C@@H](O)C1 NHVNXKFIZYSCEB-XLPZGREQSA-N 0.000 description 1
- 101150056924 dadA1 gene Proteins 0.000 description 1
- 238000006481 deamination reaction Methods 0.000 description 1
- 230000032798 delamination Effects 0.000 description 1
- 238000004925 denaturation Methods 0.000 description 1
- 230000036425 denaturation Effects 0.000 description 1
- 230000001419 dependent effect Effects 0.000 description 1
- MNNHAPBLZZVQHP-UHFFFAOYSA-N diammonium hydrogen phosphate Chemical compound [NH4+].[NH4+].OP([O-])([O-])=O MNNHAPBLZZVQHP-UHFFFAOYSA-N 0.000 description 1
- FSXRLASFHBWESK-UHFFFAOYSA-N dipeptide phenylalanyl-tyrosine Natural products C=1C=C(O)C=CC=1CC(C(O)=O)NC(=O)C(N)CC1=CC=CC=C1 FSXRLASFHBWESK-UHFFFAOYSA-N 0.000 description 1
- 238000004520 electroporation Methods 0.000 description 1
- 230000002708 enhancing effect Effects 0.000 description 1
- 238000001952 enzyme assay Methods 0.000 description 1
- 238000012869 ethanol precipitation Methods 0.000 description 1
- 238000000605 extraction Methods 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- 239000012467 final product Substances 0.000 description 1
- 239000008273 gelatin Substances 0.000 description 1
- 229920000159 gelatin Polymers 0.000 description 1
- 235000019322 gelatine Nutrition 0.000 description 1
- 235000011852 gelatine desserts Nutrition 0.000 description 1
- 238000007429 general method Methods 0.000 description 1
- 235000013922 glutamic acid Nutrition 0.000 description 1
- 239000004220 glutamic acid Substances 0.000 description 1
- 238000000338 in vitro Methods 0.000 description 1
- 230000005764 inhibitory process Effects 0.000 description 1
- 230000000968 intestinal effect Effects 0.000 description 1
- 229940116108 lactase Drugs 0.000 description 1
- 101150011498 lad gene Proteins 0.000 description 1
- 239000006166 lysate Substances 0.000 description 1
- 230000001404 mediated effect Effects 0.000 description 1
- 239000012528 membrane Substances 0.000 description 1
- 230000000813 microbial effect Effects 0.000 description 1
- 239000011259 mixed solution Substances 0.000 description 1
- 238000002156 mixing Methods 0.000 description 1
- 230000035772 mutation Effects 0.000 description 1
- 230000007935 neutral effect Effects 0.000 description 1
- FEMOMIGRRWSMCU-UHFFFAOYSA-N ninhydrin Chemical compound C1=CC=C2C(=O)C(O)(O)C(=O)C2=C1 FEMOMIGRRWSMCU-UHFFFAOYSA-N 0.000 description 1
- 230000002018 overexpression Effects 0.000 description 1
- 230000001590 oxidative effect Effects 0.000 description 1
- 229930029653 phosphoenolpyruvate Natural products 0.000 description 1
- 230000027086 plasmid maintenance Effects 0.000 description 1
- 239000013600 plasmid vector Substances 0.000 description 1
- 238000001556 precipitation Methods 0.000 description 1
- 238000000159 protein binding assay Methods 0.000 description 1
- 230000006340 racemization Effects 0.000 description 1
- 230000006798 recombination Effects 0.000 description 1
- 238000005215 recombination Methods 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 230000002829 reductive effect Effects 0.000 description 1
- 230000001105 regulatory effect Effects 0.000 description 1
- 230000010076 replication Effects 0.000 description 1
- 239000000377 silicon dioxide Substances 0.000 description 1
- 239000011780 sodium chloride Substances 0.000 description 1
- 239000002904 solvent Substances 0.000 description 1
- 239000007858 starting material Substances 0.000 description 1
- 238000003756 stirring Methods 0.000 description 1
- 239000006228 supernatant Substances 0.000 description 1
- 238000005891 transamination reaction Methods 0.000 description 1
- 230000002463 transducing effect Effects 0.000 description 1
- 238000012546 transfer Methods 0.000 description 1
- 230000001131 transforming effect Effects 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
- C12N9/90—Isomerases (5.)
-
- 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
- C12N9/14—Hydrolases (3)
- C12N9/78—Hydrolases (3) acting on carbon to nitrogen bonds other than peptide bonds (3.5)
-
- 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
- C12P13/04—Alpha- or beta- amino acids
-
- 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
- C12P13/22—Tryptophan; Tyrosine; Phenylalanine; 3,4-Dihydroxyphenylalanine
Landscapes
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- Health & Medical Sciences (AREA)
- Zoology (AREA)
- Engineering & Computer Science (AREA)
- Wood Science & Technology (AREA)
- Genetics & Genomics (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Microbiology (AREA)
- Biotechnology (AREA)
- Biochemistry (AREA)
- General Engineering & Computer Science (AREA)
- General Health & Medical Sciences (AREA)
- Biomedical Technology (AREA)
- Molecular Biology (AREA)
- Medicinal Chemistry (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Enzymes And Modification Thereof (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US08/723,896 US5728555A (en) | 1996-09-30 | 1996-09-30 | Preparation of d-amino acids by direct fermentative means |
| US8/723,896 | 1996-09-30 |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| KR20000048776A true KR20000048776A (ko) | 2000-07-25 |
Family
ID=24908159
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| KR1019990702764A Withdrawn KR20000048776A (ko) | 1996-09-30 | 1997-09-25 | 직접발효 방법에 의한 디-아미노산의 제조방법 |
Country Status (9)
| Country | Link |
|---|---|
| US (1) | US5728555A (enExample) |
| EP (1) | EP0937156B1 (enExample) |
| JP (1) | JP4548864B2 (enExample) |
| KR (1) | KR20000048776A (enExample) |
| AT (1) | ATE234933T1 (enExample) |
| AU (1) | AU728884B2 (enExample) |
| CA (1) | CA2267205A1 (enExample) |
| DE (1) | DE69720026T2 (enExample) |
| WO (1) | WO1998014602A2 (enExample) |
Families Citing this family (30)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US6358714B1 (en) * | 1995-04-03 | 2002-03-19 | The Nutrasweet Company | Materials and methods for the production of D-phenylalanine |
| JPH10286098A (ja) * | 1997-02-14 | 1998-10-27 | Daicel Chem Ind Ltd | Ｄ−アミノ酸の製造方法、ならびにアミンの製造方法 |
| WO2000023609A1 (en) * | 1998-10-19 | 2000-04-27 | Nsc Technologies Llc | Transaminase biotransformation process employing glutamic acid |
| US6365380B2 (en) * | 2000-02-23 | 2002-04-02 | Pcbu Services, Inc. | Method for stereoselectively inverting a chiral center of a chemical compound using an enzyme and a metal catalyst |
| AU2001285833A1 (en) * | 2000-07-24 | 2002-02-05 | Degussa A.G. | Process for the fermentative preparation of l-glutamic acid using coryneform bacteria |
| US8048665B2 (en) * | 2000-07-24 | 2011-11-01 | Evonik Degussa Gmbh | Nucleotide sequences encoding alanine racemase from coryneform |
| DE10046934A1 (de) * | 2000-09-21 | 2002-04-18 | Consortium Elektrochem Ind | Verfahren zur fermentativen Herstellung von nicht-proteinogenen L-Aminosäuren |
| JP4308521B2 (ja) | 2000-11-01 | 2009-08-05 | 協和発酵バイオ株式会社 | Ｄ−セリンの製造法 |
| US7297800B2 (en) * | 2001-12-27 | 2007-11-20 | Ajinomoto Co., Inc. | Process of producing glutamate derivatives |
| US7572607B2 (en) * | 2002-04-23 | 2009-08-11 | Cargill, Incorporated | Polypeptides and biosynthetic pathways for the production of monatin and its precursors |
| US8372989B2 (en) | 2002-04-23 | 2013-02-12 | Cargill, Incorporated | Polypeptides and biosynthetic pathways for the production of monatin and its precursors |
| CA2484871C (en) | 2002-08-26 | 2010-11-30 | Ajinomoto Co., Inc. | Novel aldolase and production process of substituted .alpha.-keto acids |
| DE10251184A1 (de) * | 2002-11-04 | 2004-05-13 | Degussa Ag | Mutanten zur Herstellung von D-Aminosäuren |
| AU2003289264A1 (en) | 2002-12-09 | 2004-06-30 | Ajinomoto Co., Inc. | Mutant d-aminotransferase and process for producing optically active glutamic acid derivative using the same |
| EP1648248A2 (en) * | 2003-08-01 | 2006-04-26 | Cargill, Incorporated | Monatin tabletop sweetener compositions and methods of making same |
| US20050106305A1 (en) * | 2003-08-25 | 2005-05-19 | Cargill, Inc. | Beverage compositions comprising monatin and methods of making same |
| US8206955B2 (en) * | 2003-10-21 | 2012-06-26 | Cargill, Incorporated | Production of monatin and monatin precursors |
| US7180370B2 (en) * | 2004-09-01 | 2007-02-20 | Micron Technology, Inc. | CMOS amplifiers with frequency compensating capacitors |
| US8158389B2 (en) * | 2005-04-20 | 2012-04-17 | Cargill, Incorporated | Products and methods for in vivo secretion of monatin |
| EP1883817A4 (en) * | 2005-04-20 | 2009-09-23 | Cargill Inc | PRODUCTS AND PROCEDURES FOR IN VIVO SECRETION OF MONATIN |
| AU2006341528A1 (en) | 2005-04-26 | 2007-12-06 | Cargill, Incorporated | Polypeptides and biosynthetic pathways for the production of stereoisomers of monatin and their precursors |
| ES2416104T3 (es) | 2006-03-07 | 2013-07-30 | Cargill, Incorporated | Aldolasas, ácidos nucleicos que las codifican y métodos para producir y usar las mismas |
| JP2009538145A (ja) * | 2006-05-24 | 2009-11-05 | カーギル・インコーポレイテッド | 平衡反応の収量を増加させるための方法およびシステム |
| US20090198072A1 (en) * | 2006-05-24 | 2009-08-06 | Cargill, Incorporated | Methods and systems for increasing production of equilibrium reactions |
| WO2008080138A1 (en) | 2006-12-22 | 2008-07-03 | Richmond Chemical Corporation | Stereoinversion of amino acids |
| EP2132322A4 (en) * | 2007-03-02 | 2013-02-20 | Richmond Chemical Corp | METHOD FOR INCREASING YIELD AND IMPROVING PURIFICATION OF PRODUCTS FROM REACTIONS WITH TRANSAMINASE |
| KR20120098235A (ko) * | 2011-02-28 | 2012-09-05 | 이화여자대학교 산학협력단 | 비천연 아미노산 생산 균주 및 이를 이용한 비천연 아미노산의 제조 방법 |
| CN104744278A (zh) * | 2015-03-09 | 2015-07-01 | 黄冈威尔曼生物科技有限责任公司 | 一种新型l-缬氨酸的制备工艺 |
| CN108384818A (zh) * | 2018-05-18 | 2018-08-10 | 南京大学 | 一种酶法转化制备d-组氨酸的方法 |
| USD1126465S1 (en) * | 2022-10-04 | 2026-05-12 | Trumpf Medizin Systeme Gmbh + Co. Kg | Surgical lighthead |
Family Cites Families (8)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPH0785718B2 (ja) * | 1986-03-07 | 1995-09-20 | ダイセル化学工業株式会社 | Ｄ−アミノ酸の製造方法 |
| US4753883A (en) * | 1986-05-07 | 1988-06-28 | Biotechnica International, Inc. | Enzyme deregulation |
| JPS63112978A (ja) * | 1986-10-31 | 1988-05-18 | Daicel Chem Ind Ltd | エシエリチア・コリ |
| JPH01285193A (ja) * | 1988-05-12 | 1989-11-16 | Daicel Chem Ind Ltd | Ｄ−アスパラギン酸の製造方法 |
| US5120837A (en) * | 1989-09-20 | 1992-06-09 | The Nutrasweet Company | Dna encoding phe a feedback inhibition resistant enzyme analogues |
| AU6603090A (en) * | 1989-10-17 | 1991-05-16 | Rockefeller University, The | Enzymatic production of d-amino acids |
| US5354672A (en) * | 1992-11-24 | 1994-10-11 | Ian Fotheringham | Materials and methods for hypersecretion of amino acids |
| JP3151075B2 (ja) * | 1992-12-22 | 2001-04-03 | 協和醗酵工業株式会社 | アラニンの製造法 |
-
1996
- 1996-09-30 US US08/723,896 patent/US5728555A/en not_active Expired - Lifetime
-
1997
- 1997-09-25 WO PCT/US1997/017133 patent/WO1998014602A2/en not_active Ceased
- 1997-09-25 JP JP51665098A patent/JP4548864B2/ja not_active Expired - Fee Related
- 1997-09-25 KR KR1019990702764A patent/KR20000048776A/ko not_active Withdrawn
- 1997-09-25 CA CA002267205A patent/CA2267205A1/en not_active Abandoned
- 1997-09-25 AU AU44995/97A patent/AU728884B2/en not_active Ceased
- 1997-09-25 DE DE69720026T patent/DE69720026T2/de not_active Expired - Lifetime
- 1997-09-25 EP EP97943546A patent/EP0937156B1/en not_active Expired - Lifetime
- 1997-09-25 AT AT97943546T patent/ATE234933T1/de not_active IP Right Cessation
Also Published As
| Publication number | Publication date |
|---|---|
| EP0937156A2 (en) | 1999-08-25 |
| WO1998014602A3 (en) | 1998-07-09 |
| ATE234933T1 (de) | 2003-04-15 |
| AU728884B2 (en) | 2001-01-18 |
| CA2267205A1 (en) | 1998-04-09 |
| US5728555A (en) | 1998-03-17 |
| DE69720026D1 (de) | 2003-04-24 |
| WO1998014602A2 (en) | 1998-04-09 |
| JP4548864B2 (ja) | 2010-09-22 |
| JP2001505048A (ja) | 2001-04-17 |
| EP0937156B1 (en) | 2003-03-19 |
| AU4499597A (en) | 1998-04-24 |
| DE69720026T2 (de) | 2004-01-15 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| US5728555A (en) | Preparation of d-amino acids by direct fermentative means | |
| CA2235752C (en) | Process for preparing o-acetylserine, l-cysteine and l-cysteine-related products | |
| RU2207376C2 (ru) | Способ получения l-аминокислоты методом ферментации, штамм бактерии escherichia coli - продуцент l-аминокислоты (варианты) | |
| Cho et al. | Asymmetric synthesis of l‐homophenylalanine by equilibrium‐shift using recombinant aromatic l‐amino acid transaminase | |
| KR19990022521A (ko) | L-리신의 제조 방법 | |
| JP4108766B2 (ja) | 改良されたトランスアミナーゼ生物学的変換方法 | |
| CN100526457C (zh) | L-丝氨酸的抑制性被降低的3-磷酸甘油酸脱氢酶变体及其编码基因 | |
| US20230407351A1 (en) | Recombinant host cells to produce anthranilic acid | |
| US6358714B1 (en) | Materials and methods for the production of D-phenylalanine | |
| CN100523197C (zh) | 反馈抗性乙酰羟酸合成酶突变体 | |
| CN101952418A (zh) | 生产(2s，3r，4s)-4-羟基-l-异亮氨酸的方法 | |
| CN100569950C (zh) | 发酵生产d-对羟基苯基甘氨酸和d-苯基甘氨酸 | |
| EP1249494B1 (en) | Process for the biological production of l-pipecolic acid | |
| JP4118687B2 (ja) | Ａｒｔｈｒｏｂａｃｔｅｒ ｃｒｙｓｔａｌｌｏｐｏｉｅｔｅｓ（アリスロバクテリア クリスタロポイテス）ＤＳＭ２０１１７株由来のＤ−カルバモイラーゼ | |
| US7235388B2 (en) | Isolated nucleic acid encoding L-lysine: 2-oxoglutaric acid 6-aminotransferase | |
| JP2006524032A (ja) | コリネ型バクテリアの脱調節されたホスホグリセラート−デヒドロゲナーゼをコードするヌクレオチド配列並びにｌ−セリンの製造方法 | |
| JPS62143691A (ja) | アミノ酸の製造法 | |
| TW541315B (en) | A novel D-amino acid aminotransferase for simultaneously producing glutaryl-7- aminocephalosporanic acid and D-amino acid |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| PA0105 | International application |
Patent event date: 19990330 Patent event code: PA01051R01D Comment text: International Patent Application |
|
| PG1501 | Laying open of application | ||
| N231 | Notification of change of applicant | ||
| PN2301 | Change of applicant |
Patent event date: 20011213 Comment text: Notification of Change of Applicant Patent event code: PN23011R01D |
|
| PC1203 | Withdrawal of no request for examination | ||
| WITN | Application deemed withdrawn, e.g. because no request for examination was filed or no examination fee was paid |