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Volumn 67, Issue 1, 2005, Pages 33-39

Robust NADH-regenerator: Improved α-haloketone-resistant formate dehydrogenase

Author keywords

[No Author keywords available]

Indexed keywords

ALCOHOLS; CELLS; ENZYMES; ESCHERICHIA COLI; ESTERS; MUTAGENESIS; OPTIMIZATION;

EID: 17444424570     PISSN: 01757598     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00253-004-1728-x     Document Type: Article
Times cited : (53)

References (29)
  • 1
    • 0024042176 scopus 로고
    • Purification and properties of formate dehydrogenase from Moraxella sp. strain C-1
    • Asano Y, Sekiguchi T, Inukai H, Nakazawa A (1989) Purification and properties of formate dehydrogenase from Moraxella sp. strain C-1. J Bacteriol 170:3189-3193
    • (1989) J Bacteriol , vol.170 , pp. 3189-3193
    • Asano, Y.1    Sekiguchi, T.2    Inukai, H.3    Nakazawa, A.4
  • 2
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 3
    • 0031104963 scopus 로고    scopus 로고
    • Potential application of NAD(P)-dependent oxidoreductases in synthesis: A survey
    • Devaux-Basseguy R, Bergel A, Comta M (1997) Potential application of NAD(P)-dependent oxidoreductases in synthesis: a survey. Enzyme Microb Technol 20:248-258
    • (1997) Enzyme Microb Technol , vol.20 , pp. 248-258
    • Devaux-Basseguy, R.1    Bergel, A.2    Comta, M.3
  • 4
    • 0017146518 scopus 로고
    • S-Formylglutathione: The substrate for formate dehydrogenase in methanol-utilizing yeasts
    • Dijken JP van, Oostra-Demkes GJ, Otto R, Harder W (1976) S-Formylglutathione: the substrate for formate dehydrogenase in methanol-utilizing yeasts. Arch Microbiol 111:77-83
    • (1976) Arch Microbiol , vol.111 , pp. 77-83
    • Van Dijken, J.P.1    Oostra-Demkes, G.J.2    Otto, R.3    Harder, W.4
  • 6
    • 4243468814 scopus 로고
    • Isolation and properties of NAD-dependent formate dehydrogenase from the yeast Candida methylica
    • Egorova OA, Avilova TV, Platonenkova LS, Egorov AM (1981) Isolation and properties of NAD-dependent formate dehydrogenase from the yeast Candida methylica. Biokhimiya 46:1119-1126
    • (1981) Biokhimiya , vol.46 , pp. 1119-1126
    • Egorova, O.A.1    Avilova, T.V.2    Platonenkova, L.S.3    Egorov, A.M.4
  • 7
    • 0036946150 scopus 로고    scopus 로고
    • Effect of interactions between amino acid residues 43 and 61 of thermal stability of bacterial formate dehydrogenases
    • Moscow
    • Fedorchuk VV, Gallon AG, Yasny IE, Kulakova LB, Rojkova AM, Filippova AA, Tishlov VI (2002) Effect of interactions between amino acid residues 43 and 61 of thermal stability of bacterial formate dehydrogenases. Biochemistry (Moscow) 67:1385-1393
    • (2002) Biochemistry , vol.67 , pp. 1385-1393
    • Fedorchuk, V.V.1    Gallon, A.G.2    Yasny, I.E.3    Kulakova, L.B.4    Rojkova, A.M.5    Filippova, A.A.6    Tishlov, V.I.7
  • 8
    • 0029618234 scopus 로고
    • Cloning of formate dehydrogenase gene from a methanol-utilizing bacterium Mycobacterium vaccae N10
    • Galkin A, Kulakova L, Tishkov V, Esaki N, Soda K (1995) Cloning of formate dehydrogenase gene from a methanol-utilizing bacterium Mycobacterium vaccae N10. Appl Microbiol Biotechnol 44:479-483
    • (1995) Appl Microbiol Biotechnol , vol.44 , pp. 479-483
    • Galkin, A.1    Kulakova, L.2    Tishkov, V.3    Esaki, N.4    Soda, K.5
  • 9
    • 0020144640 scopus 로고
    • NAD-linked formate dehydrogenase from methanol-grown Pichia pastoris NRRL-Y-7556
    • Hou CT, Patel RN, Laskin AI, Barnabe H (1982) NAD-linked formate dehydrogenase from methanol-grown Pichia pastoris NRRL-Y-7556. Arch Biochem Biophys 216:296-305
    • (1982) Arch Biochem Biophys , vol.216 , pp. 296-305
    • Hou, C.T.1    Patel, R.N.2    Laskin, A.I.3    Barnabe, H.4
  • 10
    • 0033485581 scopus 로고    scopus 로고
    • Large scale applications of NAD(P)-dependent oxidoreductases: Recent developments
    • Hummel W (1999) Large scale applications of NAD(P)-dependent oxidoreductases: recent developments. Trends Biotechnol 17:487-492
    • (1999) Trends Biotechnol , vol.17 , pp. 487-492
    • Hummel, W.1
  • 12
    • 0024358439 scopus 로고
    • Characterization of crystalline formate dehydrogenase from Candida methanolica
    • Izumi Y, Kanzaki H, Morita S, Futazuka H, Yamada H (1989) Characterization of crystalline formate dehydrogenase from Candida methanolica. Eur J Biochem 182:333-341
    • (1989) Eur J Biochem , vol.182 , pp. 333-341
    • Izumi, Y.1    Kanzaki, H.2    Morita, S.3    Futazuka, H.4    Yamada, H.5
  • 14
    • 0031450596 scopus 로고    scopus 로고
    • Enzymatic production of ethyl (R)-4-chloro-3-hydroxybutanoate: Asymmetric reduction of ethyl 4-chloro-3-oxobutanoate by an Escherichia coli transformant expressing the aldehyde reductase gene from yeast
    • Kataoka M, Rohani LPS, Yamamoto K, Wada M, Kawabata H, Kita K, Yanase H, Shimizu S (1997) Enzymatic production of ethyl (R)-4-chloro-3-hydroxybutanoate: asymmetric reduction of ethyl 4-chloro-3-oxobutanoate by an Escherichia coli transformant expressing the aldehyde reductase gene from yeast. Appl Microbiol Biotechnol 48:699-703
    • (1997) Appl Microbiol Biotechnol , vol.48 , pp. 699-703
    • Kataoka, M.1    Rohani, L.P.S.2    Yamamoto, K.3    Wada, M.4    Kawabata, H.5    Kita, K.6    Yanase, H.7    Shimizu, S.8
  • 15
    • 0032951737 scopus 로고    scopus 로고
    • Stereoselective reduction of ethyl 4-chloro-3-oxobutanoate by Escherichia coli transformant cells coexpressing the aldehyde reductase and glucose dehydrogenase genes
    • Kataoka M, Yamamoto K, Kawabata H, Wada M, Kita K, Yanase H, Shimizu S (1999) Stereoselective reduction of ethyl 4-chloro-3-oxobutanoate by Escherichia coli transformant cells coexpressing the aldehyde reductase and glucose dehydrogenase genes. Appl Microbiol Biotechnol 51:486-490
    • (1999) Appl Microbiol Biotechnol , vol.51 , pp. 486-490
    • Kataoka, M.1    Yamamoto, K.2    Kawabata, H.3    Wada, M.4    Kita, K.5    Yanase, H.6    Shimizu, S.7
  • 18
    • 0041350368 scopus 로고    scopus 로고
    • Purification and characterization of formate dehydrogenase from Ancylobacter aquaticus strain KNK607M, and cloning of the gene
    • Nanba H, Takaoka Y, Hasegawa J (2003a) Purification and characterization of formate dehydrogenase from Ancylobacter aquaticus strain KNK607M, and cloning of the gene. Biosci Biotechnol Biochem 67:720-728
    • (2003) Biosci Biotechnol Biochem , vol.67 , pp. 720-728
    • Nanba, H.1    Takaoka, Y.2    Hasegawa, J.3
  • 19
    • 3142750085 scopus 로고    scopus 로고
    • Purification and characterization of an α-haloketone-resistant formate dehydrogenase from Thiobacillus sp. strain KNK65MA, and cloning of the gene
    • Nanba H, Takaoka Y, Hasegawa J (2003b) Purification and characterization of an α-haloketone-resistant formate dehydrogenase from Thiobacillus sp. strain KNK65MA, and cloning of the gene. Biosci Biotechnol Biochem 67:2145-2153
    • (2003) Biosci Biotechnol Biochem , vol.67 , pp. 2145-2153
    • Nanba, H.1    Takaoka, Y.2    Hasegawa, J.3
  • 20
    • 0027937347 scopus 로고
    • +-dependent formate dehydrogenase
    • +-dependent formate dehydrogenase. Biochem J 301:625-643
    • (1994) Biochem J , vol.301 , pp. 625-643
    • Popov, V.O.1    Lamzin, V.S.2
  • 22
    • 0017252385 scopus 로고
    • Purification and properties of formaldehyde dehydrogenase and formate dehydrogenase from Candida boidinu
    • Schutte H, Flossdorf J, Sahm H, Kula MR (1976) Purification and properties of formaldehyde dehydrogenase and formate dehydrogenase from Candida boidinu. Eur J Biochem 62:151-160
    • (1976) Eur J Biochem , vol.62 , pp. 151-160
    • Schutte, H.1    Flossdorf, J.2    Sahm, H.3    Kula, M.R.4
  • 23
    • 0034011107 scopus 로고    scopus 로고
    • Stabilization of NAD-dependent formate dehydrogenase from Candida boidinii by site-directed mutagenesis of cysteine residues
    • Slusarczyk H, Felber S, Kula M-R, Pohl M (2000) Stabilization of NAD-dependent formate dehydrogenase from Candida boidinii by site-directed mutagenesis of cysteine residues. Eur J Biochem 267:1280-1289
    • (2000) Eur J Biochem , vol.267 , pp. 1280-1289
    • Slusarczyk, H.1    Felber, S.2    Kula, M.-R.3    Pohl, M.4
  • 25
    • 0029367248 scopus 로고
    • Purification and characterization of (S)-1,3-butanediol dehydrogenase from Candida parapsilosis
    • Yamamoto H, Matsuyama A, Kobayashi Y, Kawada N (1995) Purification and characterization of (S)-1,3-butanediol dehydrogenase from Candida parapsilosis. Biosci Biotechnol Biochem 59:1769-1770
    • (1995) Biosci Biotechnol Biochem , vol.59 , pp. 1769-1770
    • Yamamoto, H.1    Matsuyama, A.2    Kobayashi, Y.3    Kawada, N.4
  • 26
    • 0036479364 scopus 로고    scopus 로고
    • Synthesis of ethyl (R)-4-chloro-3-hydroxybutanoate with recombinant Escherichia coli cells expressing (S)-specific secondary alcohol dehydrogenase
    • Yamamoto H, Matsuyama A, Kobayashi Y (2002) Synthesis of ethyl (R)-4-chloro-3-hydroxybutanoate with recombinant Escherichia coli cells expressing (S)-specific secondary alcohol dehydrogenase. Biosci Biotechnol Biochem 66:481-483
    • (2002) Biosci Biotechnol Biochem , vol.66 , pp. 481-483
    • Yamamoto, H.1    Matsuyama, A.2    Kobayashi, Y.3
  • 27
    • 0037393493 scopus 로고    scopus 로고
    • Synthesis of ethyl (S)-4-chloro-3-hydroxybutanoate using fabG-homologues
    • Yamamoto H, Matsuyama A, Kobayashi Y (2003) Synthesis of ethyl (S)-4-chloro-3-hydroxybutanoate using fabG-homologues. Appl Microbiol Biotechnol 61:133-139
    • (2003) Appl Microbiol Biotechnol , vol.61 , pp. 133-139
    • Yamamoto, H.1    Matsuyama, A.2    Kobayashi, Y.3
  • 28
    • 4544304906 scopus 로고    scopus 로고
    • A novel NADH-dependent carbonyl reductase from Kluyveromyces aestuarii and comparison of NADH-regeneration systems for the synthesis of ethyl (S)-4-chloro-3-hydroxybutanoate
    • Yamamoto H, Mitsuhashi K, Kimoto N, Matsuyama A, Esaki N, Kobayashi Y (2004) A novel NADH-dependent carbonyl reductase from Kluyveromyces aestuarii and comparison of NADH-regeneration systems for the synthesis of ethyl (S)-4-chloro-3-hydroxybutanoate. Biosci Biotechnol Biochem 68:638-649
    • (2004) Biosci Biotechnol Biochem , vol.68 , pp. 638-649
    • Yamamoto, H.1    Mitsuhashi, K.2    Kimoto, N.3    Matsuyama, A.4    Esaki, N.5    Kobayashi, Y.6
  • 29
    • 84941889613 scopus 로고
    • Continuous enzymatic transformation in an enzyme membrane reactor with simultaneous NAD(H) regeneration
    • Wichmann R, Wandrey C, Buckmann AF, Kula MR (1981) Continuous enzymatic transformation in an enzyme membrane reactor with simultaneous NAD(H) regeneration. Biotechnol Bioeng 23:2789-2802
    • (1981) Biotechnol Bioeng , vol.23 , pp. 2789-2802
    • Wichmann, R.1    Wandrey, C.2    Buckmann, A.F.3    Kula, M.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.