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Volumn 65, Issue 12, 1999, Pages 5207-5211

Cloning, overexpression, and mutagenesis of the Sporobolomyces salmonicolor AKU4429 gene encoding a new aldehyde reductase, which catalyzes the stereoselective reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (S)- 4-chloro-3-hydroxybutanoate

Author keywords

[No Author keywords available]

Indexed keywords

ALDEHYDE REDUCTASE; AMINO ACID; BUTYRIC ACID DERIVATIVE; FLAVANONE DERIVATIVE; HYDROXYSTEROID DEHYDROGENASE;

EID: 0032735706     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/aem.65.12.5207-5211.1999     Document Type: Article
Times cited : (38)

References (35)
  • 1
    • 0026521505 scopus 로고
    • Expansion of the mammalian 3β-hydroxysteroid dehydrogenase/plant dihydroflavonol reductase superfamily to include a bacterial cholesterol dehydrogenase, a bacterial UDP-galactose 4-epimerase, and open reading frames in vaccinia virus and fish lymphocystis disease virus
    • Baker, M. E., and R. Blasco. 1992. Expansion of the mammalian 3β-hydroxysteroid dehydrogenase/plant dihydroflavonol reductase superfamily to include a bacterial cholesterol dehydrogenase, a bacterial UDP-galactose 4-epimerase, and open reading frames in vaccinia virus and fish lymphocystis disease virus. FEBS Lett. 301:89-93.
    • (1992) FEBS Lett. , vol.301 , pp. 89-93
    • Baker, M.E.1    Blasco, R.2
  • 2
    • 0025338352 scopus 로고
    • A common ancester for mammalian 3β-hydroxysteroid dehydrogenase and plant dihydroflavonol reductase
    • Baker, M. E., V. Luu-The, J. Simard, and F. Labri. 1990. A common ancester for mammalian 3β-hydroxysteroid dehydrogenase and plant dihydroflavonol reductase. Biochem. J. 269:558-559.
    • (1990) Biochem. J. , vol.269 , pp. 558-559
    • Baker, M.E.1    Luu-The, V.2    Simard, J.3    Labri, F.4
  • 3
    • 0026736606 scopus 로고
    • The molecular structure of UDP-galactose 4-epimerase from Escherichia coli determined at 2.5Å resolution
    • Bauer, A. J., I. Rayment, P. A. Frey, and H. M. Holden. 1992. The molecular structure of UDP-galactose 4-epimerase from Escherichia coli determined at 2.5Å resolution. Proteins 12:372-381.
    • (1992) Proteins , vol.12 , pp. 372-381
    • Bauer, A.J.1    Rayment, I.2    Frey, P.A.3    Holden, H.M.4
  • 5
    • 0028947904 scopus 로고
    • An oligodeoxyribonucleotide-directed dual amber method for site-directed mutagenesis
    • Hashimoto-Gotoh, T., T. Mizuno, Y. Ogasahara, and M. Nakagawa. 1995. An oligodeoxyribonucleotide-directed dual amber method for site-directed mutagenesis. Gene 152:271-275.
    • (1995) Gene , vol.152 , pp. 271-275
    • Hashimoto-Gotoh, T.1    Mizuno, T.2    Ogasahara, Y.3    Nakagawa, M.4
  • 6
    • 0026605537 scopus 로고
    • CLUSTAL V: Improved software for multiple sequence alignment
    • Higgins, D. G., A. J. Bleasby, and R. Fuchs. 1992. CLUSTAL V: improved software for multiple sequence alignment. Comput. Appl. Biosci. 8:189-191.
    • (1992) Comput. Appl. Biosci. , vol.8 , pp. 189-191
    • Higgins, D.G.1    Bleasby, A.J.2    Fuchs, R.3
  • 7
    • 0025896737 scopus 로고
    • Cloning, nucleotide sequence, and transcriptional analysis of the NAD(P)-dependent cholesterol dehydrogenase gene from a Nocardia sp. and its hyperexpression in Streptomyces spp
    • Horinouchi, S., H. Ishizuka, and T. Beppu. 1991. Cloning, nucleotide sequence, and transcriptional analysis of the NAD(P)-dependent cholesterol dehydrogenase gene from a Nocardia sp. and its hyperexpression in Streptomyces spp. Appl. Environ. Microbiol. 57:1386-1393.
    • (1991) Appl. Environ. Microbiol. , vol.57 , pp. 1386-1393
    • Horinouchi, S.1    Ishizuka, H.2    Beppu, T.3
  • 10
    • 0031450596 scopus 로고    scopus 로고
    • Enzymatic production ot 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., L. P. S. Rohani, K. Yakamnto, M. Wada, H. Kawabata, K. Kita, H. Yanase, and S. Shimizu. 1997. Enzymatic production ot 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    Yakamnto, K.3    Wada, M.4    Kawabata, H.5    Kita, K.6    Yanase, H.7    Shimizu, S.8
  • 11
    • 0031606997 scopus 로고    scopus 로고
    • Escherichia coli transformant expressing the glucose dehydrogenase gene from Bacillus megaterium as a cofactor regenerator in a chiral alcohol production system
    • Kataoka, M., L. P. S. Rohani, M. Wada, K. Kita, H. Yanase, I. Urabe, and S. Shimizu. 1998. Escherichia coli transformant expressing the glucose dehydrogenase gene from Bacillus megaterium as a cofactor regenerator in a chiral alcohol production system. Biosci. Biotechnol. Biochem. 62:167-169.
    • (1998) Biosci. Biotechnol. Biochem. , vol.62 , pp. 167-169
    • Kataoka, M.1    Rohani, L.P.S.2    Wada, M.3    Kita, K.4    Yanase, H.5    Urabe, I.6    Shimizu, S.7
  • 12
    • 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., K. Yamamoto, H. Kawabata, M. Wada, K. Kita, H. Yanase, and S. Shimizu. 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
  • 13
    • 0029959335 scopus 로고    scopus 로고
    • Cloning of the aldehyde reductase gene from a red yeast, Sporobolomyces salmonicolor. and characterization of the gene and its product
    • Kita, K., K. Matsuzaki, T. Hashimoto, H. Yanase, N. Kato, M. C-M. Chung, M. Kataoka, and S. Shimizu. 1996. Cloning of the aldehyde reductase gene from a red yeast, Sporobolomyces salmonicolor. and characterization of the gene and its product. Appl. Environ. Microbiol. 62:2303-2310.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 2303-2310
    • Kita, K.1    Matsuzaki, K.2    Hashimoto, T.3    Yanase, H.4    Kato, N.5    Chung, M.C.-M.6    Kataoka, M.7    Shimizu, S.8
  • 14
    • 0033545524 scopus 로고    scopus 로고
    • Purification and characterization of new aldehyde reductases from Sporobolomyces salmonicolor AKU4429
    • Kita, K., K. Nakase, H. Yanase, M. Kataoka, and S. Shimizu. 1999. Purification and characterization of new aldehyde reductases from Sporobolomyces salmonicolor AKU4429. J. Mol. Catal. B Enzym. 6:305-313.
    • (1999) J. Mol. Catal. B Enzym. , vol.6 , pp. 305-313
    • Kita, K.1    Nakase, K.2    Yanase, H.3    Kataoka, M.4    Shimizu, S.5
  • 15
    • 0031105944 scopus 로고    scopus 로고
    • Cinnamoyl-CoA reductase, the first committed enzyme of the lignin branch biosynthetic pathway: Cloning, expression and phylogenetic relationships
    • Lacombe, E., S. Hawkins, J. Van Doorsselaere, J. Piquemal, D. Goffner, O. Poeydomenge, A. E. Boudet, and J. Grima-Pettenati. 1997. Cinnamoyl-CoA reductase, the first committed enzyme of the lignin branch biosynthetic pathway: cloning, expression and phylogenetic relationships. Plant J. 11:429-441.
    • (1997) Plant J. , vol.11 , pp. 429-441
    • Lacombe, E.1    Hawkins, S.2    Van Doorsselaere, J.3    Piquemal, J.4    Goffner, D.5    Poeydomenge, O.6    Boudet, A.E.7    Grima-Pettenati, J.8
  • 16
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227:680-685.
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 17
    • 0023046226 scopus 로고
    • Nucleotide sequences of the gaIE gene and the gaIT gene of E. coli
    • Lemaire, H. G., and B. Muller-Hill. 1986. Nucleotide sequences of the gaIE gene and the gaIT gene of E. coli. Nucleic Acids Res. 14:77115-7711.
    • (1986) Nucleic Acids Res. , vol.14 , pp. 77115-77711
    • Lemaire, H.G.1    Muller-Hill, B.2
  • 18
    • 0000499776 scopus 로고    scopus 로고
    • A cDNA encoding cinnamoyl-CoA reductase from Populus trichocarpa
    • Leple, J. C., J. Grima-Pettenati, M. Montagu, and W. Boerjan. 1998. A cDNA encoding cinnamoyl-CoA reductase from Populus trichocarpa. Plant Physiol. 117:1126.
    • (1998) Plant Physiol. , vol.117 , pp. 1126
    • Leple, J.C.1    Grima-Pettenati, J.2    Montagu, M.3    Boerjan, W.4
  • 19
    • 0025295774 scopus 로고
    • Human 3β-hydroxysteroid dehydrogenase/δ 5-4 isomerase from placenta: Expression in nonsteoidogenic cells of a protein that catalyzes the dehydrogenation/ isomerization of C21 and C19 steroids
    • Lorence, M. C., B. A. Murry, J. M. Trant, and J. I. Mason. 1990. Human 3β-hydroxysteroid dehydrogenase/δ 5-4 isomerase from placenta: expression in nonsteoidogenic cells of a protein that catalyzes the dehydrogenation/ isomerization of C21 and C19 steroids. Endocrinology 126:2493-2498.
    • (1990) Endocrinology , vol.126 , pp. 2493-2498
    • Lorence, M.C.1    Murry, B.A.2    Trant, J.M.3    Mason, J.I.4
  • 20
    • 0020362615 scopus 로고
    • A new pair of M13 vectors for selecting either DNA strand of double-digest restriction fragments
    • Messing, J., and J. Vieira. 1982. A new pair of M13 vectors for selecting either DNA strand of double-digest restriction fragments. Gene 19:269-276.
    • (1982) Gene , vol.19 , pp. 269-276
    • Messing, J.1    Vieira, J.2
  • 21
    • 0027415645 scopus 로고
    • Alteration of coenzyme specificity of malate dehydrogenase from Thermus flavus, by site-directed mutagenesis
    • Nishiyama, M., J. J. Birktoft, and T. Beppu. 1993. Alteration of coenzyme specificity of malate dehydrogenase from Thermus flavus, by site-directed mutagenesis. J. Biol. Chem. 268:4656-4660.
    • (1993) J. Biol. Chem. , vol.268 , pp. 4656-4660
    • Nishiyama, M.1    Birktoft, J.J.2    Beppu, T.3
  • 22
    • 0032210896 scopus 로고    scopus 로고
    • Cloning and characterization of two maize cDNAs encoding cinnamoyl-CoA reductase (CCR) and differential expression of the corresponding genes
    • Pichon, M., I. Courbou, M. Beckert, A. M. Boudet, and J. Grima-Pettenati. 1998. Cloning and characterization of two maize cDNAs encoding cinnamoyl-CoA reductase (CCR) and differential expression of the corresponding genes. Plant Mol. Biol. 38:671-676.
    • (1998) Plant Mol. Biol. , vol.38 , pp. 671-676
    • Pichon, M.1    Courbou, I.2    Beckert, M.3    Boudet, A.M.4    Grima-Pettenati, J.5
  • 26
    • 0025019734 scopus 로고
    • Redesign of the coenzyme specificity of a dehydrogenase by protein engineering
    • Scrutton, N. S., A. Berry, and R. N. Perham. 1990. Redesign of the coenzyme specificity of a dehydrogenase by protein engineering. Nature (London) 343:38-43.
    • (1990) Nature (London) , vol.343 , pp. 38-43
    • Scrutton, N.S.1    Berry, A.2    Perham, R.N.3
  • 29
    • 0016154301 scopus 로고
    • The 3′-terminal sequence of Escherichia coli 16S ribosomal RNA: Complementarity to nonsense triplets and ribosome binding sites
    • Shine, J., and L. Dalgamo. 1974. The 3′-terminal sequence of Escherichia coli 16S ribosomal RNA: complementarity to nonsense triplets and ribosome binding sites. Proc. Natl. Acad. Sci. USA 71:1342-1346.
    • (1974) Proc. Natl. Acad. Sci. USA , vol.71 , pp. 1342-1346
    • Shine, J.1    Dalgamo, L.2
  • 30
    • 0029877040 scopus 로고    scopus 로고
    • Crystal structures of the oxidized and reduced forms of UDP-galactose 4-epimerase isolated from Escherichia coli
    • Thoden, J. M., P. A. Frey, and H. M. Holden. 1996. Crystal structures of the oxidized and reduced forms of UDP-galactose 4-epimerase isolated from Escherichia coli. Biochemistry 35:2557-2566.
    • (1996) Biochemistry , vol.35 , pp. 2557-2566
    • Thoden, J.M.1    Frey, P.A.2    Holden, H.M.3
  • 31
    • 0031989518 scopus 로고    scopus 로고
    • Purification and characterization of NADPH-dependent carbonyl reductase, involved in stereoselective reduction of ethyl 4-chloro-3-oxobutanoate, from Candida magnoliae
    • Wada, M., M. Kataoka, H. Kawabata, Y. Yasohara, N. Kizaki, J. Hasegawa, and S. Shimizu. 1998. Purification and characterization of NADPH-dependent carbonyl reductase, involved in stereoselective reduction of ethyl 4-chloro-3-oxobutanoate, from Candida magnoliae. Biosci. Biotechnol. Biochem. 62:280-285.
    • (1998) Biosci. Biotechnol. Biochem. , vol.62 , pp. 280-285
    • Wada, M.1    Kataoka, M.2    Kawabata, H.3    Yasohara, Y.4    Kizaki, N.5    Hasegawa, J.6    Shimizu, S.7
  • 32
    • 0023768323 scopus 로고
    • Human carbonyl reductase. Nucleotide sequence analysis of a cDNa and amino acid sequence of the encoded protein
    • Wermuth, B., K. M. Bohren, G. Heinemann, J.-P. Von Wartburg, and K. H. Gabbay. 1988. Human carbonyl reductase. Nucleotide sequence analysis of a cDNA and amino acid sequence of the encoded protein. J. Biol. Chem. 263:16185-16188.
    • (1988) J. Biol. Chem. , vol.263 , pp. 16185-16188
    • Wermuth, B.1    Bohren, K.M.2    Heinemann, G.3    Von Wartburg, J.-P.4    Gabbay, K.H.5
  • 33
    • 33845318295 scopus 로고
    • Interaction of pyrophosphate moieties with α-helixes in dinucleotide binding proteins
    • Wierenga, R. K., M. C. H. De Maeyer, and W. G. J. Hol. 1985. Interaction of pyrophosphate moieties with α-helixes in dinucleotide binding proteins. Biochemistry 24:1346-1357.
    • (1985) Biochemistry , vol.24 , pp. 1346-1357
    • Wierenga, R.K.1    De Maeyer, M.C.H.2    Hol, W.G.J.3
  • 34
    • 0025294272 scopus 로고
    • A novel NADPH-dependent aldehyde reductase, catalyzing asymmetric reduction of β-keto acid esters, from Sporobolomyces salmonicolor: Purification and characterization
    • Yamada, H., S. Shimizu, M. Kataoka, H. Sakai, and T. Miyoshi. 1990. A novel NADPH-dependent aldehyde reductase, catalyzing asymmetric reduction of β-keto acid esters, from Sporobolomyces salmonicolor: purification and characterization. FEMS Microhiol. Lett. 70:45-48.
    • (1990) FEMS Microhiol. Lett. , vol.70 , pp. 45-48
    • Yamada, H.1    Shimizu, S.2    Kataoka, M.3    Sakai, H.4    Miyoshi, T.5
  • 35
    • 0030008575 scopus 로고    scopus 로고
    • Conversion of the coenzyme specificity of isocitrate dehydrogenase by module replacement
    • Yaoi, T., K. Miyazaki, T. Oshima, Y. Komukai, and M. Go. 1996. Conversion of the coenzyme specificity of isocitrate dehydrogenase by module replacement. J. Biochem. 119:1014-1018.
    • (1996) J. Biochem. , vol.119 , pp. 1014-1018
    • Yaoi, T.1    Miyazaki, K.2    Oshima, T.3    Komukai, Y.4    Go, M.5


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