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Volumn 385, Issue 1, 2005, Pages 75-83

The coenzyme specificity of Candida tenuis xylose reductase (AKR2B5) explored by site-directed mutagenesis and X-ray crystallography

Author keywords

Aldo keto reductase; Coenzyme selectivity; NADH; NADPH; Site directed mutagenesis; Xylose fermentation

Indexed keywords

CATALYSIS; CHEMICAL BONDS; CONFORMATIONS; GROUND STATE; MUTAGENESIS; SUBSTRATES;

EID: 12844287005     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20040363     Document Type: Article
Times cited : (105)

References (48)
  • 1
    • 0034071629 scopus 로고    scopus 로고
    • Metabolic engineering applications to renewable resource utilization
    • Aristidou, A. and Penttilä, M. (2000) Metabolic engineering applications to renewable resource utilization. Curr. Opin. Biotechnol. 11, 187-198
    • (2000) Curr. Opin. Biotechnol. , vol.11 , pp. 187-198
    • Aristidou, A.1    Penttilä, M.2
  • 2
    • 1242264261 scopus 로고    scopus 로고
    • Metabolic engineering for improved fermentation of pentoses by yeasts
    • Jeffries, T. W. and Jin, Y. S. (2004) Metabolic engineering for improved fermentation of pentoses by yeasts. Appl. Microbiol. Biotechnol. 63, 495-509
    • (2004) Appl. Microbiol. Biotechnol. , vol.63 , pp. 495-509
    • Jeffries, T.W.1    Jin, Y.S.2
  • 4
    • 0036036461 scopus 로고    scopus 로고
    • Fermentation performance and intracellular metabolite patterns in laboratory and industrial xylose-fermenting Saccharomyces cerevisiae
    • Zaldivar, J., Borges, A., Johansson, B., Smits, H. P., Villas-Boas, S. G., Nielsen, J. and Olsson, L. (2002) Fermentation performance and intracellular metabolite patterns in laboratory and industrial xylose-fermenting Saccharomyces cerevisiae. Appl. Microbiol. Biotechnol. 59, 436-442
    • (2002) Appl. Microbiol. Biotechnol. , vol.59 , pp. 436-442
    • Zaldivar, J.1    Borges, A.2    Johansson, B.3    Smits, H.P.4    Villas-Boas, S.G.5    Nielsen, J.6    Olsson, L.7
  • 5
    • 0042371815 scopus 로고    scopus 로고
    • + and the basis for single and dual co-substrate specificity in family 2 aldo-keto reductases
    • + and the basis for single and dual co-substrate specificity in family 2 aldo-keto reductases. Biochem. J. 373, 319-326
    • (2003) Biochem. J. , vol.373 , pp. 319-326
    • Kavanagh, K.L.1    Klimacek, M.2    Nidetzky, B.3    Wilson, D.K.4
  • 6
    • 0347506028 scopus 로고    scopus 로고
    • It is all about metabolic fluxes
    • Nielsen, J. (2003) It is all about metabolic fluxes. J. Bacteriol. 185, 7031-7035
    • (2003) J. Bacteriol. , vol.185 , pp. 7031-7035
    • Nielsen, J.1
  • 7
    • 0038514106 scopus 로고    scopus 로고
    • Metabolic flux analysis of xylose metabolism in recombinant Saccharomyces cerevisiae using continuous culture
    • Pitkanen, J. P., Aristidou, A., Salusjarvi, L., Ruohonen, L. and Penttilä, M. (2003) Metabolic flux analysis of xylose metabolism in recombinant Saccharomyces cerevisiae using continuous culture. Metab. Eng. 5, 16-31
    • (2003) Metab. Eng. , vol.5 , pp. 16-31
    • Pitkanen, J.P.1    Aristidou, A.2    Salusjarvi, L.3    Ruohonen, L.4    Penttilä, M.5
  • 8
    • 0037118693 scopus 로고    scopus 로고
    • The structure of apo and holo forms of xylose reductase, a dimeric aldo-keto reductase from Candida tenuis
    • Kavanagh, K. L., Klimacek, M., Nidetzky, B. and Wilson, D. K. (2002) The structure of apo and holo forms of xylose reductase, a dimeric aldo-keto reductase from Candida tenuis. Biochemistry 41, 8785-8795
    • (2002) Biochemistry , vol.41 , pp. 8785-8795
    • Kavanagh, K.L.1    Klimacek, M.2    Nidetzky, B.3    Wilson, D.K.4
  • 9
    • 0030881429 scopus 로고    scopus 로고
    • NAD(P)H-dependent aldose reductase from the xylose-assimilating yeast Candida tenuis. Isolation, characterization and biochemical properties of the enzyme
    • Neuhauser, W., Haltrich, D., Kulbe, K. D. and Nidetzky, B. (1997) NAD(P)H-dependent aldose reductase from the xylose-assimilating yeast Candida tenuis. Isolation, characterization and biochemical properties of the enzyme. Biochem. J. 326, 683-692
    • (1997) Biochem. J. , vol.326 , pp. 683-692
    • Neuhauser, W.1    Haltrich, D.2    Kulbe, K.D.3    Nidetzky, B.4
  • 10
    • 0032570312 scopus 로고    scopus 로고
    • Noncovalent enzyme-substrate interactions in the catalytic mechanism of yeast aldose reductase
    • Neuhauser, W., Haltrich, D., Kulbe, K. D. and Nidetzky, B. (1998) Noncovalent enzyme-substrate interactions in the catalytic mechanism of yeast aldose reductase. Biochemistry 37, 1116-1123
    • (1998) Biochemistry , vol.37 , pp. 1116-1123
    • Neuhauser, W.1    Haltrich, D.2    Kulbe, K.D.3    Nidetzky, B.4
  • 11
    • 0035964171 scopus 로고    scopus 로고
    • Transient-state and steady-state kinetic studies of the mechanism of NADH-dependent aldehyde reduction catalyzed by xylose reductase from the yeast Candida tenuis
    • Nidetzky, B., Klimacek, M. and Mayr, P. (2001) Transient-state and steady-state kinetic studies of the mechanism of NADH-dependent aldehyde reduction catalyzed by xylose reductase from the yeast Candida tenuis. Biochemistry 40, 10371-10381
    • (2001) Biochemistry , vol.40 , pp. 10371-10381
    • Nidetzky, B.1    Klimacek, M.2    Mayr, P.3
  • 12
    • 0035969838 scopus 로고    scopus 로고
    • Structural and functional properties of aldose xylose reductase from the D-xylose-metabolizing yeast Candida tenuis
    • Nidetzky, B., Mayr, P., Neuhauser, W. and Puchberger, M. (2001) Structural and functional properties of aldose xylose reductase from the D-xylose-metabolizing yeast Candida tenuis. Chem. Biol. Interact. 130-132, 583-595
    • (2001) Chem. Biol. Interact. , vol.130-132 , pp. 583-595
    • Nidetzky, B.1    Mayr, P.2    Neuhauser, W.3    Puchberger, M.4
  • 14
    • 0024357799 scopus 로고
    • A simple method for site-directed mutagenesis using the polymerase chain reaction
    • Hemsley, A., Arnheim, N., Toney, M. D., Cortopassi, G. and Galas, D. J. (1989) A simple method for site-directed mutagenesis using the polymerase chain reaction. Nucleic Acids Res. 17, 6545-6551
    • (1989) Nucleic Acids Res. , vol.17 , pp. 6545-6551
    • Hemsley, A.1    Arnheim, N.2    Toney, M.D.3    Cortopassi, G.4    Galas, D.J.5
  • 15
    • 0342514615 scopus 로고    scopus 로고
    • D-Xylose metabolism by Candida intermedia: Isolation and characterisation of two forms of aldose reductase with different coenzyme specificities
    • Mayr, P., Brüggler, K., Kulbe, K. D. and Nidetzky, B. (2000) D-Xylose metabolism by Candida intermedia: isolation and characterisation of two forms of aldose reductase with different coenzyme specificities. J. Chromatogr. B 737, 195-202
    • (2000) J. Chromatogr. B , vol.737 , pp. 195-202
    • Mayr, P.1    Brüggler, K.2    Kulbe, K.D.3    Nidetzky, B.4
  • 16
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation model
    • Otwinowski, Z. and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation model. Methods Enzymol. 276, 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 18
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T. A., Zou, J. Y., Cowan, S. W. and Kjeldgaard, M. (1991) Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 19
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., MacArthur, M. W., Moss, D. S. and Thornton, J. M. (1993) PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 23, 283-291
    • (1993) J. Appl. Crystallogr. , vol.23 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 20
    • 0029562477 scopus 로고
    • NAD-binding domains of dehydrogenases
    • Lesk, A. M. (1995) NAD-binding domains of dehydrogenases. Curr. Opin. Struct. Biol. 5, 775-783
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 775-783
    • Lesk, A.M.1
  • 21
    • 0347480310 scopus 로고    scopus 로고
    • Crystal structure of a ternary complex of the alcohol dehydrogenase from Sulfolobus solfataricus
    • Esposito, L., Bruno, I., Sica, F., Raia, C. A., Giordano, A., Rossi, M., Mazzarella, L. and Zagari, A. (2003) Crystal structure of a ternary complex of the alcohol dehydrogenase from Sulfolobus solfataricus. Biochemistry 42, 14397-14407
    • (2003) Biochemistry , vol.42 , pp. 14397-14407
    • Esposito, L.1    Bruno, I.2    Sica, F.3    Raia, C.A.4    Giordano, A.5    Rossi, M.6    Mazzarella, L.7    Zagari, A.8
  • 22
    • 0037044776 scopus 로고    scopus 로고
    • Crystal structure of Pseudomonas fluorescens mannitol 2-dehydrogenase binary and ternary complexes. Specificity and catalytic mechanism
    • Kavanagh, K. L., Klimacek, M., Nidetzky, B. and Wilson, D. K. (2002) Crystal structure of Pseudomonas fluorescens mannitol 2-dehydrogenase binary and ternary complexes. Specificity and catalytic mechanism. J. Biol. Chem. 277, 43433-43442
    • (2002) J. Biol. Chem. , vol.277 , pp. 43433-43442
    • Kavanagh, K.L.1    Klimacek, M.2    Nidetzky, B.3    Wilson, D.K.4
  • 23
    • 0037018948 scopus 로고    scopus 로고
    • Crystal structure of the malic enzyme from Ascaris suum complexed with nicotinamide adenine dinucleotide at 2.3 Å resolution
    • Coleman, D. E., Rao, G. S., Goldsmith, E. J., Cook, P. F. and Harris, B. G. (2002) Crystal structure of the malic enzyme from Ascaris suum complexed with nicotinamide adenine dinucleotide at 2.3 Å resolution. Biochemistry 41, 6928-6938
    • (2002) Biochemistry , vol.41 , pp. 6928-6938
    • Coleman, D.E.1    Rao, G.S.2    Goldsmith, E.J.3    Cook, P.F.4    Harris, B.G.5
  • 24
    • 0038820015 scopus 로고    scopus 로고
    • The 2.3-Å crystal structure of the shikimate 5-dehydrogenase orthologue YdiB from Escherichia coli suggests a novel catalytic environment for an NAD-dependent dehydrogenase
    • Benach, J., Lee, I., Edstrom, W., Kuzin, A. P., Chiang, Y., Acton, T. B., Montelione, G. T. and Hunt, J. F. (2003) The 2.3-Å crystal structure of the shikimate 5-dehydrogenase orthologue YdiB from Escherichia coli suggests a novel catalytic environment for an NAD-dependent dehydrogenase. J. Biol. Chem. 278, 19176-19182
    • (2003) J. Biol. Chem. , vol.278 , pp. 19176-19182
    • Benach, J.1    Lee, I.2    Edstrom, W.3    Kuzin, A.P.4    Chiang, Y.5    Acton, T.B.6    Montelione, G.T.7    Hunt, J.F.8
  • 25
    • 0038265866 scopus 로고    scopus 로고
    • Structures of shikimate dehydrogenase AroE and its Paralog YdiB. A common structural framework for different activities
    • Michel, G., Roszak, A. W., Sauve, V., Maclean, J., Matte, A., Coggins, J. R., Cygler, M. and Lapthorn, A. J. (2003) Structures of shikimate dehydrogenase AroE and its Paralog YdiB. A common structural framework for different activities. J. Biol. Chem. 278, 19463-19472
    • (2003) J. Biol. Chem. , vol.278 , pp. 19463-19472
    • Michel, G.1    Roszak, A.W.2    Sauve, V.3    Maclean, J.4    Matte, A.5    Coggins, J.R.6    Cygler, M.7    Lapthorn, A.J.8
  • 27
    • 0030000879 scopus 로고    scopus 로고
    • Crystal structures of the binary and ternary complexes of 7 alpha-hydroxysteroid dehydrogenase from Escherichia coli
    • Tanaka, N., Nonaka, T., Tanabe, T., Yoshimoto, T., Tsuru, D. and Mitsui, Y. (1996) Crystal structures of the binary and ternary complexes of 7 alpha-hydroxysteroid dehydrogenase from Escherichia coli. Biochemistry 35, 7715-7730
    • (1996) Biochemistry , vol.35 , pp. 7715-7730
    • Tanaka, N.1    Nonaka, T.2    Tanabe, T.3    Yoshimoto, T.4    Tsuru, D.5    Mitsui, Y.6
  • 28
    • 0030002725 scopus 로고    scopus 로고
    • Redesigning secondary structure to invert coenzyme specificity in isopropylmalate dehydrogenase
    • Chen, R., Greet, A. and Dean, A. M. (1996) Redesigning secondary structure to invert coenzyme specificity in isopropylmalate dehydrogenase. Proc. Natl. Acad. Sci. U.S.A. 93, 12171-12176
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 12171-12176
    • Chen, R.1    Greet, A.2    Dean, A.M.3
  • 30
    • 0035969891 scopus 로고    scopus 로고
    • The aldo-keto reductase (AKR) superfamily: An update
    • Jez, J. M. and Penning, T. M. (2001) The aldo-keto reductase (AKR) superfamily: an update. Chem.-Biol. Interact. 130-132, 499-525
    • (2001) Chem.-Biol. Interact. , vol.130-132 , pp. 499-525
    • Jez, J.M.1    Penning, T.M.2
  • 31
    • 0038342696 scopus 로고    scopus 로고
    • Crystal structure of the vertebrate NADP(H)-dependent alcohol dehydrogenase (ADH8)
    • Rosell, A., Valencia, E., Pares, X., Fita, I., Farres, J. and Ochoa, W. F. (2003) Crystal structure of the vertebrate NADP(H)-dependent alcohol dehydrogenase (ADH8). J. Mol. Biol. 330, 75-85
    • (2003) J. Mol. Biol. , vol.330 , pp. 75-85
    • Rosell, A.1    Valencia, E.2    Pares, X.3    Fita, I.4    Farres, J.5    Ochoa, W.F.6
  • 32
    • 0032557624 scopus 로고    scopus 로고
    • NADP-dependent bacterial alcohol dehydrogenases: Crystal structure, cofactor-binding and cofactor specificity of the ADHs of Clostridium beijerinckii and Thermoanaerobacter brockii
    • Korkhin, Y., Kalb, A. J., Peretz, M., Bogin, O., Burstein, Y. and Frolow, F. (1998) NADP-dependent bacterial alcohol dehydrogenases: crystal structure, cofactor-binding and cofactor specificity of the ADHs of Clostridium beijerinckii and Thermoanaerobacter brockii. J. Mol. Biol. 278, 967-981
    • (1998) J. Mol. Biol. , vol.278 , pp. 967-981
    • Korkhin, Y.1    Kalb, A.J.2    Peretz, M.3    Bogin, O.4    Burstein, Y.5    Frolow, F.6
  • 33
    • 0142124355 scopus 로고    scopus 로고
    • Cloning and characterization of the xyl1 gene, encoding an NADH-preferring xylose reductase from Candida parapsilosis, and its functional expression in Candida tropicalis
    • Lee, J. K., Koo, B. S. and Kim, S. Y. (2003) Cloning and characterization of the xyl1 gene, encoding an NADH-preferring xylose reductase from Candida parapsilosis, and its functional expression in Candida tropicalis. Appl. Environ. Microbiol. 69, 6179-6188
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 6179-6188
    • Lee, J.K.1    Koo, B.S.2    Kim, S.Y.3
  • 34
    • 0036213581 scopus 로고    scopus 로고
    • Alteration of the specificity of the cofactor-binding pocket of Corynebacterium 2,5-diketo-D-gluconic acid reductase A
    • Banta, S., Swanson, B. A., Wu, S., Jarnagin, A. and Anderson, S. (2002) Alteration of the specificity of the cofactor-binding pocket of Corynebacterium 2,5-diketo-D-gluconic acid reductase A. Protein Eng. 15, 131-140
    • (2002) Protein Eng. , vol.15 , pp. 131-140
    • Banta, S.1    Swanson, B.A.2    Wu, S.3    Jarnagin, A.4    Anderson, S.5
  • 35
    • 0037150104 scopus 로고    scopus 로고
    • Optimizing an artificial metabolic pathway: Engineering the cofactor specificity of Corynebacterium 2,5-diketo-D-gluconic acid reductase for use in vitamin C biosynthesis
    • Banta, S., Swanson, B. A., Wu, S., Jarnagin, A. and Anderson, S. (2002) Optimizing an artificial metabolic pathway: engineering the cofactor specificity of Corynebacterium 2,5-diketo-D-gluconic acid reductase for use in vitamin C biosynthesis. Biochemistry 41, 6226-6236
    • (2002) Biochemistry , vol.41 , pp. 6226-6236
    • Banta, S.1    Swanson, B.A.2    Wu, S.3    Jarnagin, A.4    Anderson, S.5
  • 36
    • 0026344829 scopus 로고
    • Expression of human aldose and aldehyde reductases. Site-directed mutagenesis of a critical lysine 262
    • Bohren, K. M., Page, J. L., Shankar, R., Henry, S. P. and Gabbay, K. H. (1991) Expression of human aldose and aldehyde reductases. Site-directed mutagenesis of a critical lysine 262. J. Biol. Chem. 266, 24031-24037
    • (1991) J. Biol. Chem. , vol.266 , pp. 24031-24037
    • Bohren, K.M.1    Page, J.L.2    Shankar, R.3    Henry, S.P.4    Gabbay, K.H.5
  • 37
    • 0032008240 scopus 로고    scopus 로고
    • Mutational analysis of the role of the conserved lysine-270 in the Pichia stipitis xylose reductase
    • Kostrzynska, M., Sopher, C. R. and Lee, H. (1998) Mutational analysis of the role of the conserved lysine-270 in the Pichia stipitis xylose reductase. FEMS Microbiol. Lett. 159, 107-112
    • (1998) FEMS Microbiol. Lett. , vol.159 , pp. 107-112
    • Kostrzynska, M.1    Sopher, C.R.2    Lee, H.3
  • 38
    • 0028123784 scopus 로고
    • Studies on pig aldose reductase. Identification of an essential arginine in the primary and tertiary structure of the enzyme
    • Kubiseski, T. J., Green, N. C., Borhani, D. W. and Flynn, T. G. (1994) Studies on pig aldose reductase. Identification of an essential arginine in the primary and tertiary structure of the enzyme. J. Biol. Chem. 269, 2183-2188
    • (1994) J. Biol. Chem. , vol.269 , pp. 2183-2188
    • Kubiseski, T.J.1    Green, N.C.2    Borhani, D.W.3    Flynn, T.G.4
  • 39
    • 0029017363 scopus 로고
    • Studies on human aldose reductase. Probing the role of arginine 268 by site-directed mutagenesis
    • Kubiseski, T. J. and Flynn, T. G. (1995) Studies on human aldose reductase. Probing the role of arginine 268 by site-directed mutagenesis. J. Biol. Chem. 270, 16911-16917
    • (1995) J. Biol. Chem. , vol.270 , pp. 16911-16917
    • Kubiseski, T.J.1    Flynn, T.G.2
  • 40
    • 0031058232 scopus 로고    scopus 로고
    • Involvement of two basic residues (Lys-270 and Arg-276) of human liver 3 alpha-hydroxysteroid dehydrogenase in NADP(H) binding and activation by sulphobromophthalein: Site-directed mutagenesis and kinetic analysis
    • Matsuura, K., Tamada, Y., Sato, K., Iwasa, H., Miwa, G., Deyashiki, Y. and Hara, A. (1997) Involvement of two basic residues (Lys-270 and Arg-276) of human liver 3 alpha-hydroxysteroid dehydrogenase in NADP(H) binding and activation by sulphobromophthalein: site-directed mutagenesis and kinetic analysis. Biochem. J. 322, 89-93
    • (1997) Biochem. J. , vol.322 , pp. 89-93
    • Matsuura, K.1    Tamada, Y.2    Sato, K.3    Iwasa, H.4    Miwa, G.5    Deyashiki, Y.6    Hara, A.7
  • 41
    • 0033564742 scopus 로고    scopus 로고
    • The arginine 276 anchor for NADP(H) dictates fluorescence kinetic transients in 3α-hydroxysteroid dehydrogenase, a representative aldo-keto reductase
    • Ratnam, K., Ma, H. and Penning, T. M. (1999) The arginine 276 anchor for NADP(H) dictates fluorescence kinetic transients in 3α-hydroxysteroid dehydrogenase, a representative aldo-keto reductase. Biochemistry 38, 7856-7864
    • (1999) Biochemistry , vol.38 , pp. 7856-7864
    • Ratnam, K.1    Ma, H.2    Penning, T.M.3
  • 42
    • 0024552846 scopus 로고
    • Aldose reductase from human psoas muscle. Affinity labeling of an active site lysine by pyridoxal 5′-phosphate and pyridoxal 5′-diphospho- 5′-adenosine
    • Morjana, N. A., Lyons, C. and Flynn, T. G. (1989) Aldose reductase from human psoas muscle. Affinity labeling of an active site lysine by pyridoxal 5′-phosphate and pyridoxal 5′-diphospho-5′-adenosine. J. Biol. Chem. 264, 2912-2919
    • (1989) J. Biol. Chem. , vol.264 , pp. 2912-2919
    • Morjana, N.A.1    Lyons, C.2    Flynn, T.G.3
  • 43
    • 0032528442 scopus 로고    scopus 로고
    • Aldehyde reductase: The role of C-terminal residues in defining substrate and cofactor specificities
    • Rees-Milton, K. J., Jia, Z., Green, N. C., Bhatia, M., El-Kabbani, O. and Flynn, T. G. (1998) Aldehyde reductase: the role of C-terminal residues in defining substrate and cofactor specificities. Arch. Biochem. Biophys. 355, 137-144
    • (1998) Arch. Biochem. Biophys. , vol.355 , pp. 137-144
    • Rees-Milton, K.J.1    Jia, Z.2    Green, N.C.3    Bhatia, M.4    El-Kabbani, O.5    Flynn, T.G.6
  • 44
    • 1642452918 scopus 로고    scopus 로고
    • Structural alteration of cofactor specificity in Corynebacterium 2,5-diketo-D-gluconic acid reductase
    • Sanli, G., Banta, S., Anderson, S. and Blaber, M. (2004) Structural alteration of cofactor specificity in Corynebacterium 2,5-diketo-D-gluconic acid reductase. Protein Sci. 13, 504-512
    • (2004) Protein Sci. , vol.13 , pp. 504-512
    • Sanli, G.1    Banta, S.2    Anderson, S.3    Blaber, M.4
  • 45
    • 0032499712 scopus 로고    scopus 로고
    • Crystal structure of 2,5-diketo-D-gluconic acid reductase A complexed with NADPH at 2.1-Å resolution
    • Khurana, S., Powers, D. B., Anderson, S. and Blaber, M. (1998) Crystal structure of 2,5-diketo-D-gluconic acid reductase A complexed with NADPH at 2.1-Å resolution. Proc. Natl. Acad. Sci. U.S.A. 95, 6768-6773
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 6768-6773
    • Khurana, S.1    Powers, D.B.2    Anderson, S.3    Blaber, M.4
  • 47
    • 0030632239 scopus 로고    scopus 로고
    • New alcohol dehydrogenases for the synthesis of chiral compounds
    • Hummel, W. (1997) New alcohol dehydrogenases for the synthesis of chiral compounds. Adv. Biochem. Eng. Biotechnol. 58, 145-184
    • (1997) Adv. Biochem. Eng. Biotechnol. , vol.58 , pp. 145-184
    • Hummel, W.1
  • 48
    • 0345817539 scopus 로고
    • Regeneration of nicotinamide cofactors for use in organic synthesis
    • Chenault, H. K. and Whitesides, G. M. (1987) Regeneration of nicotinamide cofactors for use in organic synthesis. Appl. Biochem. Biotechnol. 14, 147-197
    • (1987) Appl. Biochem. Biotechnol. , vol.14 , pp. 147-197
    • Chenault, H.K.1    Whitesides, G.M.2


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