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Volumn 289, Issue 48, 2014, Pages 33198-33214

Structure-based conversion of the coenzyme requirement of a short-chain dehydrogenase/reductase involved in bacterial alginate metabolism

Author keywords

[No Author keywords available]

Indexed keywords

ALGINATE; AMINO ACIDS; CHAINS; COENZYMES; DEHYDROGENATION; ENZYME ACTIVITY; GLUCOSE;

EID: 84912128137     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.585661     Document Type: Article
Times cited : (39)

References (70)
  • 1
    • 0001889582 scopus 로고
    • Avramovic, D. D., and Poulson, R., eds John Wiley & Sons, Inc., New York
    • Moat, A. G., and Foster, J. W. (1987) in Pyridine Nucleotide Coenzymes Part A (Avramovic, D. D., and Poulson, R., eds) pp. 1-24, John Wiley & Sons, Inc., New York
    • (1987) Pyridine Nucleotide Coenzymes Part A , pp. 1-24
    • Moat, A.G.1    Foster, J.W.2
  • 3
    • 84855161202 scopus 로고    scopus 로고
    • The role of synthetic biology in the design of microbial cell factories for biofuel production
    • Colin, V. L., Rodriguez, A., and Cristobal, H. A. (2011) The role of synthetic biology in the design of microbial cell factories for biofuel production. J. Biomed. Biotechnol. 10.1155/2011/601834
    • (2011) J. Biomed. Biotechnol.
    • Colin, V.L.1    Rodriguez, A.2    Cristobal, H.A.3
  • 4
    • 2442587515 scopus 로고    scopus 로고
    • Metabolic engineering of Escherichia coli: Construction of an efficient biocatalyst for D-mannitol formation in a whole-cell biotransformation
    • Kaup, B., Bringer-Meyer, S., and Sahm, H. (2004) Metabolic engineering of Escherichia coli: construction of an efficient biocatalyst for D-mannitol formation in a whole-cell biotransformation. Appl. Microbiol. Biotechnol. 64, 333-339
    • (2004) Appl. Microbiol. Biotechnol. , vol.64 , pp. 333-339
    • Kaup, B.1    Bringer-Meyer, S.2    Sahm, H.3
  • 7
    • 12844287005 scopus 로고    scopus 로고
    • The coenzyme specificity of Candida tenuis xylose reductase (AKR2B5) explored by site-directed mutagenesis and x-ray crystallography
    • Petschacher, B., Leitgeb, S., Kavanagh, K. L., Wilson, D. K., and Nidetzky, B. (2005) The coenzyme specificity of Candida tenuis xylose reductase (AKR2B5) explored by site-directed mutagenesis and x-ray crystallography. Biochem. J. 385, 75-83
    • (2005) Biochem. J. , vol.385 , pp. 75-83
    • Petschacher, B.1    Leitgeb, S.2    Kavanagh, K.L.3    Wilson, D.K.4    Nidetzky, B.5
  • 8
    • 0027383390 scopus 로고
    • Determinants of coenzyme specificity in glyceraldehyde-3-phosphate dehydrogenase: Role of the acidic residue in the fingerprint region of the nucleotide binding fold
    • Clermont, S., Corbier, C., Mely, Y., Gerard, D., Wonacott, A., and Branlant, G. (1993) Determinants of coenzyme specificity in glyceraldehyde-3-phosphate dehydrogenase: role of the acidic residue in the fingerprint region of the nucleotide binding fold. Biochemistry 32, 10178-10184
    • (1993) Biochemistry , vol.32 , pp. 10178-10184
    • Clermont, S.1    Corbier, C.2    Mely, Y.3    Gerard, D.4    Wonacott, A.5    Branlant, G.6
  • 9
    • 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
  • 10
    • 0032744506 scopus 로고    scopus 로고
    • Redesign of the coenzyme specificity in L-lactate dehydrogenase from Bacillus stearothermophilus using site-directed mutagenesis and media engineering
    • Holmberg, N., Ryde, U., and Bülow, L. (1999) Redesign of the coenzyme specificity in L-lactate dehydrogenase from Bacillus stearothermophilus using site-directed mutagenesis and media engineering. Protein Eng. 12, 851-856
    • (1999) Protein Eng. , vol.12 , pp. 851-856
    • Holmberg, N.1    Ryde, U.2    Bülow, L.3
  • 11
    • 0030008575 scopus 로고    scopus 로고
    • Conversion of the coenzyme specificity of isocitrate dehydrogenase by module replacement
    • Yaoi, T., Miyazaki, K., Oshima, T., Komukai, Y., and Go, M. (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
  • 12
    • 0030906828 scopus 로고    scopus 로고
    • Reversal of the nucleotide specificity of ketol acid reductoisomerase by site-directed mutagenesis identifies the NADPH binding site
    • Rane, M. J., and Calvo, K. C. (1997) Reversal of the nucleotide specificity of ketol acid reductoisomerase by site-directed mutagenesis identifies the NADPH binding site. Arch. Biochem. Biophys. 338, 83-89
    • (1997) Arch. Biochem. Biophys. , vol.338 , pp. 83-89
    • Rane, M.J.1    Calvo, K.C.2
  • 13
    • 0032188938 scopus 로고    scopus 로고
    • Engineering of pyridine nucleotide specificity of nitrate reductase: Mutagenesis of recombinant cytochrome b reductase fragment of Neurospora crassa NADPH: Nitrate reductase
    • Shiraishi, N., Croy, C., Kaur, J., and Campbell, W. H. (1998) Engineering of pyridine nucleotide specificity of nitrate reductase: mutagenesis of recombinant cytochrome b reductase fragment of Neurospora crassa NADPH: nitrate reductase. Arch. Biochem. Biophys. 358, 104-115
    • (1998) Arch. Biochem. Biophys. , vol.358 , pp. 104-115
    • Shiraishi, N.1    Croy, C.2    Kaur, J.3    Campbell, W.H.4
  • 15
    • 0037073754 scopus 로고    scopus 로고
    • Modification of the nucleotide cofactor-binding site of cytochrome P-450 reductase to enhance turnover with NADH in vivo
    • Elmore, C. L., and Porter, T. D. (2002) Modification of the nucleotide cofactor-binding site of cytochrome P-450 reductase to enhance turnover with NADH in vivo. J. Biol. Chem. 277, 48960-48964
    • (2002) J. Biol. Chem. , vol.277 , pp. 48960-48964
    • Elmore, C.L.1    Porter, T.D.2
  • 16
    • 33947148555 scopus 로고    scopus 로고
    • Rational design of novel mutants of fungal 17β-hydroxysteroid dehydrogenase
    • Kristan, K., Stojan, J., Adamski, J., and Lanisnik Rizner, T. (2007) Rational design of novel mutants of fungal 17β-hydroxysteroid dehydrogenase. J. Biotechnol. 129, 123-130
    • (2007) J. Biotechnol. , vol.129 , pp. 123-130
    • Kristan, K.1    Stojan, J.2    Adamski, J.3    Lanisnik Rizner, T.4
  • 17
    • 33747460737 scopus 로고    scopus 로고
    • Crystal structure of NADP(H)-dependent 1,5-anhydro-D-fructose reductase from Sinorhizobium morelense at 2.2 A˚ resolution: Construction of a NADH-accepting mutant and its application in rare sugar synthesis
    • Dambe, T. R., Kühn, A. M., Brossette, T., Giffhorn, F., and Scheidig, A. J. (2006) Crystal structure of NADP(H)-dependent 1,5-anhydro-D-fructose reductase from Sinorhizobium morelense at 2.2 A˚ resolution: construction of a NADH-accepting mutant and its application in rare sugar synthesis. Biochemistry 45, 10030-10042
    • (2006) Biochemistry , vol.45 , pp. 10030-10042
    • Dambe, T.R.1    Kühn, A.M.2    Brossette, T.3    Giffhorn, F.4    Scheidig, A.J.5
  • 19
    • 0029557251 scopus 로고
    • A highly active decarboxylating dehydrogenase with rationally inverted coenzyme specificity
    • Chen, R., Greer, A., and Dean, A. M. (1995) A highly active decarboxylating dehydrogenase with rationally inverted coenzyme specificity. Proc. Natl. Acad. Sci. U.S.A. 92, 11666-11670
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 11666-11670
    • Chen, R.1    Greer, A.2    Dean, A.M.3
  • 20
    • 84878874888 scopus 로고    scopus 로고
    • Engineering of formate dehydrogenase: Synergistic effect of mutations affecting cofactor specificity and chemical stability
    • Hoelsch, K., Sührer, I., Heusel, M., and Weuster-Botz, D. (2013) Engineering of formate dehydrogenase: synergistic effect of mutations affecting cofactor specificity and chemical stability. Appl. Microbiol. Biotechnol. 97, 2473-2481
    • (2013) Appl. Microbiol. Biotechnol. , vol.97 , pp. 2473-2481
    • Hoelsch, K.1    Sührer, I.2    Heusel, M.3    Weuster-Botz, D.4
  • 21
    • 0028904688 scopus 로고
    • D175 discriminates between NADH and NADPH in the coenzyme binding site of Lactobacillus delbrueckii subsp. Bulgaricus D-lactate dehydrogenase
    • Bernard, N., Johnsen, K., Holbrook, J. J., and Delcour, J. (1995) D175 discriminates between NADH and NADPH in the coenzyme binding site of Lactobacillus delbrueckii subsp. Bulgaricus D-lactate dehydrogenase. Biochem. Biophys. Res. Commun. 208, 895-900
    • (1995) Biochem. Biophys. Res. Commun. , vol.208 , pp. 895-900
    • Bernard, N.1    Johnsen, K.2    Holbrook, J.J.3    Delcour, J.4
  • 22
    • 0036845955 scopus 로고    scopus 로고
    • Engineering of coenzyme specificity of formate dehydrogenase from Saccharomyces cerevisiae
    • Serov, A. E., Popova, A. S., Fedorchuk, V. V., and Tishkov, V. I. (2002) Engineering of coenzyme specificity of formate dehydrogenase from Saccharomyces cerevisiae. Biochem. J. 367, 841-847
    • (2002) Biochem. J. , vol.367 , pp. 841-847
    • Serov, A.E.1    Popova, A.S.2    Fedorchuk, V.V.3    Tishkov, V.I.4
  • 23
    • 79959923488 scopus 로고    scopus 로고
    • + in clostridial glutamate dehydrogenase and a thorough reappraisal of the coenzyme specificity of the wild-type enzyme
    • + in clostridial glutamate dehydrogenase and a thorough reappraisal of the coenzyme specificity of the wild-type enzyme. FEBS J. 278, 2460-2468
    • (2011) FEBS J. , vol.278 , pp. 2460-2468
    • Capone, M.1    Scanlon, D.2    Griffin, J.3    Engel, P.C.4
  • 25
    • 84884533760 scopus 로고    scopus 로고
    • Crystallographic analysis and structure-guided engineering of NADPH-dependent Ralstonia sp. Alcohol dehydrogenase toward NADH cosubstrate specificity
    • Lerchner, A., Jarasch, A., Meining, W., Schiefner, A., and Skerra, A. (2013) Crystallographic analysis and structure-guided engineering of NADPH-dependent Ralstonia sp. alcohol dehydrogenase toward NADH cosubstrate specificity. Biotechnol. Bioeng. 110, 2803-2814
    • (2013) Biotechnol. Bioeng. , vol.110 , pp. 2803-2814
    • Lerchner, A.1    Jarasch, A.2    Meining, W.3    Schiefner, A.4    Skerra, A.5
  • 26
    • 0025019734 scopus 로고
    • Redesign of the coenzyme specificity of a dehydrogenase by protein engineering
    • Scrutton, N. S., Berry, A., and Perham, R. N. (1990) Redesign of the coenzyme specificity of a dehydrogenase by protein engineering. Nature 343, 38-43
    • (1990) Nature , vol.343 , pp. 38-43
    • Scrutton, N.S.1    Berry, A.2    Perham, R.N.3
  • 28
    • 0033621096 scopus 로고    scopus 로고
    • Change of nucleotide specificity and enhancement of catalytic efficiency in single point mutants of Vibrio harveyi aldehyde dehydrogenase
    • Zhang, L., Ahvazi, B., Szittner, R., Vrielink, A., and Meighen, E. (1999) Change of nucleotide specificity and enhancement of catalytic efficiency in single point mutants of Vibrio harveyi aldehyde dehydrogenase. Biochemistry 38, 11440-11447
    • (1999) Biochemistry , vol.38 , pp. 11440-11447
    • Zhang, L.1    Ahvazi, B.2    Szittner, R.3    Vrielink, A.4    Meighen, E.5
  • 30
    • 33750287639 scopus 로고    scopus 로고
    • Direct demonstration of an adaptive constraint
    • Miller, S. P., Lunzer, M., and Dean, A. M. (2006) Direct demonstration of an adaptive constraint. Science 314, 458-461
    • (2006) Science , vol.314 , pp. 458-461
    • Miller, S.P.1    Lunzer, M.2    Dean, A.M.3
  • 31
    • 33745907556 scopus 로고    scopus 로고
    • Structural basis for the alteration of coenzyme specificity in a malate dehydrogenase mutant
    • Tomita, T., Fushinobu, S., Kuzuyama, T., and Nishiyama, M. (2006) Structural basis for the alteration of coenzyme specificity in a malate dehydrogenase mutant. Biochem. Biophys. Res. Commun. 347, 502-508
    • (2006) Biochem. Biophys. Res. Commun. , vol.347 , pp. 502-508
    • Tomita, T.1    Fushinobu, S.2    Kuzuyama, T.3    Nishiyama, M.4
  • 32
    • 15544372361 scopus 로고    scopus 로고
    • Complete reversal of coenzyme specificity of xylitol dehydrogenase and increase of thermostability by the introduction of structural zinc
    • Watanabe, S., Kodaki, T., and Makino, K. (2005) Complete reversal of coenzyme specificity of xylitol dehydrogenase and increase of thermostability by the introduction of structural zinc. J. Biol. Chem. 280, 10340-10349
    • (2005) J. Biol. Chem. , vol.280 , pp. 10340-10349
    • Watanabe, S.1    Kodaki, T.2    Makino, K.3
  • 33
    • 33644843318 scopus 로고    scopus 로고
    • Structure-guided engineering of xylitol dehydrogenase cosubstrate specificity
    • Ehrensberger, A. H., Elling, R. A., and Wilson, D. K. (2006) Structure-guided engineering of xylitol dehydrogenase cosubstrate specificity. Structure 14, 567-575
    • (2006) Structure , vol.14 , pp. 567-575
    • Ehrensberger, A.H.1    Elling, R.A.2    Wilson, D.K.3
  • 34
    • 0030002725 scopus 로고    scopus 로고
    • Redesigning secondary structure to invert coenzyme specificity in isopropylmalate dehydrogenase
    • Chen, R., Greer, 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    Greer, A.2    Dean, A.M.3
  • 35
    • 84883220663 scopus 로고    scopus 로고
    • Converting NAD-specific inositol dehydrogenase to an efficient NADP-selective catalyst, with a surprising twist
    • Zheng, H., Bertwistle, D., Sanders, D. A., and Palmer, D. R. (2013) Converting NAD-specific inositol dehydrogenase to an efficient NADP-selective catalyst, with a surprising twist. Biochemistry 52, 5876-5883
    • (2013) Biochemistry , vol.52 , pp. 5876-5883
    • Zheng, H.1    Bertwistle, D.2    Sanders, D.A.3    Palmer, D.R.4
  • 38
    • 84856070797 scopus 로고    scopus 로고
    • Biofuels. Engineered superbugs boost hopes of turning seaweed into fuel
    • Stokstad, E. (2012) Biofuels. Engineered superbugs boost hopes of turning seaweed into fuel. Science 335, 273
    • (2012) Science , vol.335 , pp. 273
    • Stokstad, E.1
  • 40
    • 0033932250 scopus 로고    scopus 로고
    • A novel bacterial ATP-binding cassette transporter system that allows uptake of macromolecules
    • Momma, K., Okamoto, M., Mishima, Y., Mori, S., Hashimoto, W., and Murata, K. (2000) A novel bacterial ATP-binding cassette transporter system that allows uptake of macromolecules. J. Bacteriol. 182, 3998-4004
    • (2000) J. Bacteriol. , vol.182 , pp. 3998-4004
    • Momma, K.1    Okamoto, M.2    Mishima, Y.3    Mori, S.4    Hashimoto, W.5    Murata, K.6
  • 41
    • 0034084571 scopus 로고    scopus 로고
    • Overexpression in Escherichia coli, purification, and characterization of Sphingomonas sp. A1 alginate lyases
    • Yoon, H.-J., Hashimoto, W., Miyake, O., Okamoto, M., Mikami, B., and Murata, K. (2000) Overexpression in Escherichia coli, purification, and characterization of Sphingomonas sp. A1 alginate lyases. Protein Expr. Purif. 19, 84-90
    • (2000) Protein Expr. Purif. , vol.19 , pp. 84-90
    • Yoon, H.-J.1    Hashimoto, W.2    Miyake, O.3    Okamoto, M.4    Mikami, B.5    Murata, K.6
  • 42
    • 0033905713 scopus 로고    scopus 로고
    • Molecular identification of oligoalginate lyase of Sphingomonas sp. Strain A1 as one of the enzymes required for complete depolymerization of alginate
    • Hashimoto, W., Miyake, O., Momma, K., Kawai, S., and Murata, K. (2000) Molecular identification of oligoalginate lyase of Sphingomonas sp. strain A1 as one of the enzymes required for complete depolymerization of alginate. J. Bacteriol. 182, 4572-4577
    • (2000) J. Bacteriol. , vol.182 , pp. 4572-4577
    • Hashimoto, W.1    Miyake, O.2    Momma, K.3    Kawai, S.4    Murata, K.5
  • 43
    • 77955093827 scopus 로고    scopus 로고
    • Molecular identification of unsaturated uronate reductase prerequisite for alginate metabolism in Sphingomonas sp. A1
    • Takase, R., Ochiai, A., Mikami, B., Hashimoto, W., and Murata, K. (2010) Molecular identification of unsaturated uronate reductase prerequisite for alginate metabolism in Sphingomonas sp. A1. Biochim. Biophys. Acta 1804, 1925-1936
    • (2010) Biochim. Biophys. Acta , vol.1804 , pp. 1925-1936
    • Takase, R.1    Ochiai, A.2    Mikami, B.3    Hashimoto, W.4    Murata, K.5
  • 44
    • 79959823684 scopus 로고    scopus 로고
    • Bioethanol production from marine biomass alginate by metabolically engineered bacteria
    • Takeda, H., Yoneyama, F., Kawai, S., Hashimoto, W., and Murata, K. (2011) Bioethanol production from marine biomass alginate by metabolically engineered bacteria. Energy Environ. Sci. 4, 2575-2581
    • (2011) Energy Environ. Sci. , vol.4 , pp. 2575-2581
    • Takeda, H.1    Yoneyama, F.2    Kawai, S.3    Hashimoto, W.4    Murata, K.5
  • 47
    • 58149133711 scopus 로고    scopus 로고
    • Medium- and short-chain dehydrogenase/reductase gene and protein families: The SDR superfamily: Functional and structural diversity within a family of metabolic and regulatory enzymes
    • Kavanagh, K. L., Jörnvall, H., Persson, B., and Oppermann, U. (2008) Medium- and short-chain dehydrogenase/reductase gene and protein families: the SDR superfamily: functional and structural diversity within a family of metabolic and regulatory enzymes. Cell. Mol. Life Sci. 65, 3895-3906
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 3895-3906
    • Kavanagh, K.L.1    Jörnvall, H.2    Persson, B.3    Oppermann, U.4
  • 48
    • 84875232324 scopus 로고    scopus 로고
    • Classification and nomenclature of the superfamily of short-chain dehydrogenases/reductases (SDRs)
    • Persson, B., and Kallberg, Y. (2013) Classification and nomenclature of the superfamily of short-chain dehydrogenases/reductases (SDRs). Chem. Biol. Interact. 202, 111-115
    • (2013) Chem. Biol. Interact. , vol.202 , pp. 111-115
    • Persson, B.1    Kallberg, Y.2
  • 50
    • 65649108985 scopus 로고    scopus 로고
    • Structural determinants responsible for substrate recognition and mode of action in family 11 polysaccharide lyases
    • Ochiai, A., Itoh, T., Mikami, B., Hashimoto, W., and Murata, K. (2009) Structural determinants responsible for substrate recognition and mode of action in family 11 polysaccharide lyases. J. Biol. Chem. 284, 10181-10189
    • (2009) J. Biol. Chem. , vol.284 , pp. 10181-10189
    • Ochiai, A.1    Itoh, T.2    Mikami, B.3    Hashimoto, W.4    Murata, K.5
  • 51
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (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
  • 52
    • 0024562664 scopus 로고
    • Cloning and sequencing of two tandem genes involved in degradation of 2,3-dihydroxybiphenyl to benzoic acid in the polychlorinated biphenyl-degrading soil bacterium Pseudomonas sp. Strain KKS102
    • Kimbara, K., Hashimoto, T., Fukuda, M., Koana, T., Takagi, M., Oishi, M., and Yano, K. (1989) Cloning and sequencing of two tandem genes involved in degradation of 2,3-dihydroxybiphenyl to benzoic acid in the polychlorinated biphenyl-degrading soil bacterium Pseudomonas sp. strain KKS102. J. Bacteriol. 171, 2740-2747
    • (1989) J. Bacteriol. , vol.171 , pp. 2740-2747
    • Kimbara, K.1    Hashimoto, T.2    Fukuda, M.3    Koana, T.4    Takagi, M.5    Oishi, M.6    Yano, K.7
  • 53
    • 0019365279 scopus 로고
    • A general method for site-directed mutagenesis in prokaryotes
    • Ruvkun, G. B., and Ausubel, F. M. (1981) A general method for site-directed mutagenesis in prokaryotes. Nature 289, 85-88
    • (1981) Nature , vol.289 , pp. 85-88
    • Ruvkun, G.B.1    Ausubel, F.M.2
  • 55
    • 0031059866 scopus 로고    scopus 로고
    • Processing of x-ray diffraction data
    • Otwinowski, Z., and Minor, W. (1997) Processing of x-ray diffraction data. Methods Enzymol. 276, 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 57
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project No. 4 (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50, 760-763
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 59
  • 60
    • 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. 26, 283-291
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 61
    • 12944249776 scopus 로고
    • A discussion of the solution for the best rotation to relate two sets of vectors
    • Kabsch, W. (1978) A discussion of the solution for the best rotation to relate two sets of vectors. Acta Crystallogr. A 34, 827-828
    • (1978) Acta Crystallogr. A , vol.34 , pp. 827-828
    • Kabsch, W.1
  • 63
    • 33747181070 scopus 로고    scopus 로고
    • A biosystem for alginate metabolism in Agrobacterium tumefaciens strain C58: Molecular identification of Atu3025 as an exotype family PL-15 alginate lyase
    • Ochiai, A., Hashimoto, W., and Murata, K. (2006) A biosystem for alginate metabolism in Agrobacterium tumefaciens strain C58: molecular identification of Atu3025 as an exotype family PL-15 alginate lyase. Res. Microbiol. 157, 642-649
    • (2006) Res. Microbiol. , vol.157 , pp. 642-649
    • Ochiai, A.1    Hashimoto, W.2    Murata, K.3
  • 64
    • 0035871109 scopus 로고    scopus 로고
    • Selective and sensitive detection of pectin lyase activity using a colorimetric test: Application to the screening of microorganisms possessing pectin lyase activity
    • Nedjma, M., Hoffmann, N., and Belarbi, A. (2001) Selective and sensitive detection of pectin lyase activity using a colorimetric test: application to the screening of microorganisms possessing pectin lyase activity. Anal. Biochem. 291, 290-296
    • (2001) Anal. Biochem. , vol.291 , pp. 290-296
    • Nedjma, M.1    Hoffmann, N.2    Belarbi, A.3
  • 65
    • 0001433809 scopus 로고
    • Method for determination of the amino acid sequence in peptides
    • Edman, P. (1950) Method for determination of the amino acid sequence in peptides. Acta Chem. Scand. 4, 283-293
    • (1950) Acta Chem. Scand. , vol.4 , pp. 283-293
    • Edman, P.1
  • 66
    • 84860463104 scopus 로고    scopus 로고
    • Recognition of heteropolysaccharide alginate by periplasmic solute-binding proteins of a bacterial ABC transporter
    • Nishitani, Y., Maruyama, Y., Itoh, T., Mikami, B., Hashimoto, W., and Murata, K. (2012) Recognition of heteropolysaccharide alginate by periplasmic solute-binding proteins of a bacterial ABC transporter. Biochemistry 51, 3622-3633
    • (2012) Biochemistry , vol.51 , pp. 3622-3633
    • Nishitani, Y.1    Maruyama, Y.2    Itoh, T.3    Mikami, B.4    Hashimoto, W.5    Murata, K.6
  • 67
    • 20444407677 scopus 로고    scopus 로고
    • Structure and function of bacterial super-biosystem responsible for import and depolymerization of macromolecules
    • Hashimoto, W., Momma, K., Maruyama, Y., Yamasaki, M., Mikami, B., and Murata, K. (2005) Structure and function of bacterial super-biosystem responsible for import and depolymerization of macromolecules. Biosci. Biotechnol. Biochem. 69, 673-692
    • (2005) Biosci. Biotechnol. Biochem. , vol.69 , pp. 673-692
    • Hashimoto, W.1    Momma, K.2    Maruyama, Y.3    Yamasaki, M.4    Mikami, B.5    Murata, K.6
  • 68
    • 0016345760 scopus 로고
    • Chemical and biological evolution of nucleotide-binding protein
    • Rossmann, M. G., Moras, D., and Olsen, K. W. (1974) Chemical and biological evolution of nucleotide-binding protein. Nature 250, 194-199
    • (1974) Nature , vol.250 , pp. 194-199
    • Rossmann, M.G.1    Moras, D.2    Olsen, K.W.3
  • 69
    • 33847083503 scopus 로고    scopus 로고
    • Carbonyl reductases and pluripotent hydroxysteroid dehydrogenases of the short-chain dehydrogenase/reductase superfamily
    • Hoffmann, F., and Maser, E. (2007) Carbonyl reductases and pluripotent hydroxysteroid dehydrogenases of the short-chain dehydrogenase/reductase superfamily. Drug Metab. Rev. 39, 87-144
    • (2007) Drug Metab. Rev. , vol.39 , pp. 87-144
    • Hoffmann, F.1    Maser, E.2
  • 70
    • 77957588597 scopus 로고    scopus 로고
    • Bacterial supersystem for alginate import/metabolism and its environmental and bioenergy applications
    • Hashimoto, W., Kawai, S., and Murata, K. (2010) Bacterial supersystem for alginate import/metabolism and its environmental and bioenergy applications. Bioeng. Bugs 1, 97-109
    • (2010) Bioeng. Bugs , vol.1 , pp. 97-109
    • Hashimoto, W.1    Kawai, S.2    Murata, K.3


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