메뉴 건너뛰기




Volumn 19, Issue 11, 2012, Pages 1471-1482

Active site plasticity within the glycoside hydrolase NagZ underlies a dynamic mechanism of substrate distortion

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; GLYCOSIDASE; HISTIDINE; NAGZ PROTEIN; UNCLASSIFIED DRUG;

EID: 84870006158     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chembiol.2012.09.016     Document Type: Article
Times cited : (67)

References (62)
  • 2
    • 67049107914 scopus 로고    scopus 로고
    • Inactivation of the glycoside hydrolase NagZ attenuates antipseudomonal β-lactam resistance in Pseudomonas aeruginosa
    • A. Asgarali, K.A. Stubbs, A. Oliver, D.J. Vocadlo, and B.L. Mark Inactivation of the glycoside hydrolase NagZ attenuates antipseudomonal β-lactam resistance in Pseudomonas aeruginosa Antimicrob. Agents Chemother. 53 2009 2274 2282
    • (2009) Antimicrob. Agents Chemother. , vol.53 , pp. 2274-2282
    • Asgarali, A.1    Stubbs, K.A.2    Oliver, A.3    Vocadlo, D.J.4    Mark, B.L.5
  • 3
    • 67650070343 scopus 로고    scopus 로고
    • Insight into a strategy for attenuating AmpC-mediated β-lactam resistance: Structural basis for selective inhibition of the glycoside hydrolase NagZ
    • M.D. Balcewich, K.A. Stubbs, Y. He, T.W. James, G.J. Davies, D.J. Vocadlo, and B.L. Mark Insight into a strategy for attenuating AmpC-mediated β-lactam resistance: structural basis for selective inhibition of the glycoside hydrolase NagZ Protein Sci. 18 2009 1541 1551
    • (2009) Protein Sci. , vol.18 , pp. 1541-1551
    • Balcewich, M.D.1    Stubbs, K.A.2    He, Y.3    James, T.W.4    Davies, G.J.5    Vocadlo, D.J.6    Mark, B.L.7
  • 4
    • 0025015612 scopus 로고
    • Synthesis of 2-acetamido-2-deoxy-D-gluconhydroximolactone-derived and chitobionhydroximolactone-derived N-phenylcarbamates, potential inhibitors of β-N-acetylglucosaminidase
    • D. Beer, J.L. Maloisel, D.M. Rast, and A. Vasella Synthesis of 2-acetamido-2-deoxy-D-gluconhydroximolactone-derived and chitobionhydroximolactone-derived N-phenylcarbamates, potential inhibitors of β-N-acetylglucosaminidase Helv. Chim. Acta 73 1990 1918 1922
    • (1990) Helv. Chim. Acta , vol.73 , pp. 1918-1922
    • Beer, D.1    Maloisel, J.L.2    Rast, D.M.3    Vasella, A.4
  • 5
    • 33644967069 scopus 로고    scopus 로고
    • Substrate distortion in the Michaelis complex of Bacillus 1,3-1,4-β-glucanase. Insight from first principles molecular dynamics simulations
    • X. Biarnés, J. Nieto, A. Planas, and C. Rovira Substrate distortion in the Michaelis complex of Bacillus 1,3-1,4-β-glucanase. Insight from first principles molecular dynamics simulations J. Biol. Chem. 281 2006 1432 1441
    • (2006) J. Biol. Chem. , vol.281 , pp. 1432-1441
    • Biarnés, X.1    Nieto, J.2    Planas, A.3    Rovira, C.4
  • 6
    • 34848879539 scopus 로고    scopus 로고
    • The conformational free energy landscape of β-D-glucopyranose. Implications for substrate preactivation in β-glucoside hydrolases
    • X. Biarnés, A. Ardèvol, A. Planas, C. Rovira, A. Laio, and M. Parrinello The conformational free energy landscape of β-D- glucopyranose. Implications for substrate preactivation in β-glucoside hydrolases J. Am. Chem. Soc. 129 2007 10686 10693
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 10686-10693
    • Biarnés, X.1    Ardèvol, A.2    Planas, A.3    Rovira, C.4    Laio, A.5    Parrinello, M.6
  • 7
    • 0026597444 scopus 로고
    • Free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • A.T. Brünger Free R value: a novel statistical quantity for assessing the accuracy of crystal structures Nature 355 1992 472 475
    • (1992) Nature , vol.355 , pp. 472-475
    • Brünger, A.T.1
  • 11
    • 0033897724 scopus 로고    scopus 로고
    • Molecular characterization of the β-N-acetylglucosaminidase of Escherichia coli and its role in cell wall recycling
    • Q. Cheng, H. Li, K. Merdek, and J.T. Park Molecular characterization of the β-N-acetylglucosaminidase of Escherichia coli and its role in cell wall recycling J. Bacteriol. 182 2000 4836 4840
    • (2000) J. Bacteriol. , vol.182 , pp. 4836-4840
    • Cheng, Q.1    Li, H.2    Merdek, K.3    Park, J.T.4
  • 12
    • 0036685303 scopus 로고    scopus 로고
    • Identification of the two essential groups in the family 3 β-glucosidase from Flavobacterium meningosepticum by labelling and tandem mass spectrometric analysis
    • J. Chir, S. Withers, C.-F. Wan, and Y.-K. Li Identification of the two essential groups in the family 3 β-glucosidase from Flavobacterium meningosepticum by labelling and tandem mass spectrometric analysis Biochem. J. 365 2002 857 863
    • (2002) Biochem. J. , vol.365 , pp. 857-863
    • Chir, J.1    Withers, S.2    Wan, C.-F.3    Li, Y.-K.4
  • 13
    • 0034681333 scopus 로고    scopus 로고
    • Cloning, expression, characterization, and nucleophile identification of family 3, Aspergillus niger β-glucosidase
    • S. Dan, I. Marton, M. Dekel, B.-A. Bravdo, S. He, S.G. Withers, and O. Shoseyov Cloning, expression, characterization, and nucleophile identification of family 3, Aspergillus niger β-glucosidase J. Biol. Chem. 275 2000 4973 4980
    • (2000) J. Biol. Chem. , vol.275 , pp. 4973-4980
    • Dan, S.1    Marton, I.2    Dekel, M.3    Bravdo, B.-A.4    He, S.5    Withers, S.G.6    Shoseyov, O.7
  • 14
    • 0031015902 scopus 로고    scopus 로고
    • Nomenclature for sugar-binding subsites in glycosyl hydrolases
    • G.J. Davies, K.S. Wilson, and B. Henrissat Nomenclature for sugar-binding subsites in glycosyl hydrolases Biochem. J. 321 1997 557 559
    • (1997) Biochem. J. , vol.321 , pp. 557-559
    • Davies, G.J.1    Wilson, K.S.2    Henrissat, B.3
  • 16
    • 84860298921 scopus 로고    scopus 로고
    • Conformational analyses of the reaction coordinate of glycosidases
    • G.J. Davies, A. Planas, and C. Rovira Conformational analyses of the reaction coordinate of glycosidases Acc. Chem. Res. 45 2012 308 316
    • (2012) Acc. Chem. Res. , vol.45 , pp. 308-316
    • Davies, G.J.1    Planas, A.2    Rovira, C.3
  • 18
    • 0030802782 scopus 로고    scopus 로고
    • The signal molecule for β-lactamase induction in Enterobacter cloacae is the anhydromuramyl-pentapeptide
    • H. Dietz, D. Pfeifle, and B. Wiedemann The signal molecule for β-lactamase induction in Enterobacter cloacae is the anhydromuramyl- pentapeptide Antimicrob. Agents Chemother. 41 1997 2113 2120
    • (1997) Antimicrob. Agents Chemother. , vol.41 , pp. 2113-2120
    • Dietz, H.1    Pfeifle, D.2    Wiedemann, B.3
  • 21
    • 0021881891 scopus 로고
    • Recycling of murein by Escherichia coli
    • E.W. Goodell Recycling of murein by Escherichia coli J. Bacteriol. 163 1985 305 310
    • (1985) J. Bacteriol. , vol.163 , pp. 305-310
    • Goodell, E.W.1
  • 23
    • 0037858060 scopus 로고    scopus 로고
    • Growth of the stress-bearing and shape-maintaining murein sacculus of Escherichia coli
    • J.-V. Höltje Growth of the stress-bearing and shape-maintaining murein sacculus of Escherichia coli Microbiol. Mol. Biol. Rev. 62 1998 181 203
    • (1998) Microbiol. Mol. Biol. Rev. , vol.62 , pp. 181-203
    • Höltje, J.-V.1
  • 24
    • 0035183914 scopus 로고    scopus 로고
    • Catalytic mechanisms and reaction intermediates along the hydrolytic pathway of a plant β-D-glucan glucohydrolase
    • M. Hrmova, J.N. Varghese, R. De Gori, B.J. Smith, H. Driguez, and G.B. Fincher Catalytic mechanisms and reaction intermediates along the hydrolytic pathway of a plant β-D-glucan glucohydrolase Structure 9 2001 1005 1016
    • (2001) Structure , vol.9 , pp. 1005-1016
    • Hrmova, M.1    Varghese, J.N.2    De Gori, R.3    Smith, B.J.4    Driguez, H.5    Fincher, G.B.6
  • 26
    • 84863337895 scopus 로고    scopus 로고
    • NagZ-dependent and NagZ-independent mechanisms for β-lactamase expression in Stenotrophomonas maltophilia
    • Y.-W. Huang, R.-M. Hu, C.-W. Lin, T.-C. Chung, and T.-C. Yang NagZ-dependent and NagZ-independent mechanisms for β-lactamase expression in Stenotrophomonas maltophilia Antimicrob. Agents Chemother. 56 2012 1936 1941
    • (2012) Antimicrob. Agents Chemother. , vol.56 , pp. 1936-1941
    • Huang, Y.-W.1    Hu, R.-M.2    Lin, C.-W.3    Chung, T.-C.4    Yang, T.-C.5
  • 28
    • 0343632366 scopus 로고    scopus 로고
    • Cytosolic intermediates for cell wall biosynthesis and degradation control inducible β-lactam resistance in Gram-negative bacteria
    • C. Jacobs, J.M. Frère, and S. Normark Cytosolic intermediates for cell wall biosynthesis and degradation control inducible β-lactam resistance in Gram-negative bacteria Cell 88 1997 823 832
    • (1997) Cell , vol.88 , pp. 823-832
    • Jacobs, C.1    Frère, J.M.2    Normark, S.3
  • 29
    • 76449106188 scopus 로고    scopus 로고
    • Integration, scaling, space-group assignment and post-refinement
    • W. Kabsch Integration, scaling, space-group assignment and post-refinement Acta Crystallogr. D Biol. Crystallogr. 66 2010 133 144
    • (2010) Acta Crystallogr. D Biol. Crystallogr. , vol.66 , pp. 133-144
    • Kabsch, W.1
  • 30
    • 33845471322 scopus 로고
    • Stereoelectronic effects on acetal hydrolysis
    • A.J. Kirby Stereoelectronic effects on acetal hydrolysis Acc. Chem. Res. 17 1984 305 311
    • (1984) Acc. Chem. Res. , vol.17 , pp. 305-311
    • Kirby, A.J.1
  • 32
    • 67649607268 scopus 로고    scopus 로고
    • Bacterial AmpD at the crossroads of peptidoglycan recycling and manifestation of antibiotic resistance
    • M. Lee, W. Zhang, D. Hesek, B.C. Noll, B. Boggess, and S. Mobashery Bacterial AmpD at the crossroads of peptidoglycan recycling and manifestation of antibiotic resistance J. Am. Chem. Soc. 131 2009 8742 8743
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 8742-8743
    • Lee, M.1    Zhang, W.2    Hesek, D.3    Noll, B.C.4    Boggess, B.5    Mobashery, S.6
  • 34
    • 77953985367 scopus 로고    scopus 로고
    • Muropeptide rescue in Bacillus subtilis involves sequential hydrolysis by β-N-acetylglucosaminidase and N-acetylmuramyl-L-alanine amidase
    • S. Litzinger, A. Duckworth, K. Nitzsche, C. Risinger, V. Wittmann, and C. Mayer Muropeptide rescue in Bacillus subtilis involves sequential hydrolysis by β-N-acetylglucosaminidase and N-acetylmuramyl-L-alanine amidase J. Bacteriol. 192 2010 3132 3143
    • (2010) J. Bacteriol. , vol.192 , pp. 3132-3143
    • Litzinger, S.1    Duckworth, A.2    Nitzsche, K.3    Risinger, C.4    Wittmann, V.5    Mayer, C.6
  • 35
    • 78149234937 scopus 로고    scopus 로고
    • Structural and kinetic analysis of Bacillus subtilis N- acetylglucosaminidase reveals a unique Asp-His dyad mechanism
    • S. Litzinger, S. Fischer, P. Polzer, K. Diederichs, W. Welte, and C. Mayer Structural and kinetic analysis of Bacillus subtilis N- acetylglucosaminidase reveals a unique Asp-His dyad mechanism J. Biol. Chem. 285 2010 35675 35684
    • (2010) J. Biol. Chem. , vol.285 , pp. 35675-35684
    • Litzinger, S.1    Fischer, S.2    Polzer, P.3    Diederichs, K.4    Welte, W.5    Mayer, C.6
  • 36
    • 0028883511 scopus 로고
    • β-lactamases in laboratory and clinical resistance
    • D.M. Livermore β-lactamases in laboratory and clinical resistance Clin. Microbiol. Rev. 8 1995 557 584
    • (1995) Clin. Microbiol. Rev. , vol.8 , pp. 557-584
    • Livermore, D.M.1
  • 37
    • 82455192469 scopus 로고    scopus 로고
    • Providing β-lactams a helping hand: Targeting the AmpC β-lactamase induction pathway
    • B.L. Mark, D.J. Vocadlo, and A. Oliver Providing β-lactams a helping hand: targeting the AmpC β-lactamase induction pathway Future Microbiol. 6 2011 1415 1427
    • (2011) Future Microbiol. , vol.6 , pp. 1415-1427
    • Mark, B.L.1    Vocadlo, D.J.2    Oliver, A.3
  • 39
    • 84856110191 scopus 로고    scopus 로고
    • Structure and activity of exo-1,3/1,4-β-glucanase from marine bacterium Pseudoalteromonas sp. BB1 showing a novel C-terminal domain
    • Y. Nakatani, S.M. Cutfield, N.P. Cowieson, and J.F. Cutfield Structure and activity of exo-1,3/1,4-β-glucanase from marine bacterium Pseudoalteromonas sp. BB1 showing a novel C-terminal domain FEBS J. 279 2012 464 478
    • (2012) FEBS J. , vol.279 , pp. 464-478
    • Nakatani, Y.1    Cutfield, S.M.2    Cowieson, N.P.3    Cutfield, J.F.4
  • 40
    • 0031715607 scopus 로고    scopus 로고
    • Insights into transition state stabilization of the β-1,4- glycosidase Cex by covalent intermediate accumulation in active site mutants
    • V. Notenboom, C. Birsan, M. Nitz, D.R. Rose, R.A.J. Warren, and S.G. Withers Insights into transition state stabilization of the β-1,4- glycosidase Cex by covalent intermediate accumulation in active site mutants Nat. Struct. Biol. 5 1998 812 818
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 812-818
    • Notenboom, V.1    Birsan, C.2    Nitz, M.3    Rose, D.R.4    Warren, R.A.J.5    Withers, S.G.6
  • 41
    • 0035949643 scopus 로고    scopus 로고
    • High resolution structural analyses of mutant chitinase A complexes with substrates provide new insight into the mechanism of catalysis
    • Y. Papanikolau, G. Prag, G. Tavlas, C.E. Vorgias, A.B. Oppenheim, and K. Petratos High resolution structural analyses of mutant chitinase A complexes with substrates provide new insight into the mechanism of catalysis Biochemistry 40 2001 11338 11343
    • (2001) Biochemistry , vol.40 , pp. 11338-11343
    • Papanikolau, Y.1    Prag, G.2    Tavlas, G.3    Vorgias, C.E.4    Oppenheim, A.B.5    Petratos, K.6
  • 42
    • 44949258242 scopus 로고    scopus 로고
    • How bacteria consume their own exoskeletons (turnover and recycling of cell wall peptidoglycan)
    • J.T. Park, and T. Uehara How bacteria consume their own exoskeletons (turnover and recycling of cell wall peptidoglycan) Microbiol. Mol. Biol. Rev. 72 2008 211 227
    • (2008) Microbiol. Mol. Biol. Rev. , vol.72 , pp. 211-227
    • Park, J.T.1    Uehara, T.2
  • 43
    • 0022628618 scopus 로고
    • Building units of oligosaccharides. 69. Synthesis of 1,6-anhydromuramyl peptides
    • H. Paulsen, P. Himpkamp, and T. Peters Building units of oligosaccharides. 69. Synthesis of 1,6-anhydromuramyl peptides Liebigs Ann. Chem. 1986 1986 664 674
    • (1986) Liebigs Ann. Chem. , vol.1986 , pp. 664-674
    • Paulsen, H.1    Himpkamp, P.2    Peters, T.3
  • 44
    • 77649336582 scopus 로고    scopus 로고
    • Structural and functional analyses of β-glucosidase 3B from Thermotoga neapolitana: A thermostable three-domain representative of glycoside hydrolase 3
    • T. Pozzo, J.L. Pasten, E.N. Karlsson, and D.T. Logan Structural and functional analyses of β-glucosidase 3B from Thermotoga neapolitana: a thermostable three-domain representative of glycoside hydrolase 3 J. Mol. Biol. 397 2010 724 739
    • (2010) J. Mol. Biol. , vol.397 , pp. 724-739
    • Pozzo, T.1    Pasten, J.L.2    Karlsson, E.N.3    Logan, D.T.4
  • 45
    • 79960663578 scopus 로고    scopus 로고
    • Peptidoglycan turnover and recycling in Gram-positive bacteria
    • J. Reith, and C. Mayer Peptidoglycan turnover and recycling in Gram-positive bacteria Appl. Microbiol. Biotechnol. 92 2011 1 11
    • (2011) Appl. Microbiol. Biotechnol. , vol.92 , pp. 1-11
    • Reith, J.1    Mayer, C.2
  • 46
    • 34547125795 scopus 로고    scopus 로고
    • Small molecule inhibitors of a glycoside hydrolase attenuate inducible AmpC-mediated β-lactam resistance
    • K.A. Stubbs, M. Balcewich, B.L. Mark, and D.J. Vocadlo Small molecule inhibitors of a glycoside hydrolase attenuate inducible AmpC-mediated β-lactam resistance J. Biol. Chem. 282 2007 21382 21391
    • (2007) J. Biol. Chem. , vol.282 , pp. 21382-21391
    • Stubbs, K.A.1    Balcewich, M.2    Mark, B.L.3    Vocadlo, D.J.4
  • 47
    • 38349018251 scopus 로고    scopus 로고
    • Synthesis and use of mechanism-based protein-profiling probes for retaining β-D-glucosaminidases facilitate identification of Pseudomonas aeruginosa NagZ
    • K.A. Stubbs, A. Scaffidi, A.W. Debowski, B.L. Mark, R.V. Stick, and D.J. Vocadlo Synthesis and use of mechanism-based protein-profiling probes for retaining β-D-glucosaminidases facilitate identification of Pseudomonas aeruginosa NagZ J. Am. Chem. Soc. 130 2008 327 335
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 327-335
    • Stubbs, K.A.1    Scaffidi, A.2    Debowski, A.W.3    Mark, B.L.4    Stick, R.V.5    Vocadlo, D.J.6
  • 48
    • 0029856409 scopus 로고    scopus 로고
    • Structure of the Fusarium oxysporum endoglucanase i with a nonhydrolyzable substrate analogue: Substrate distortion gives rise to the preferred axial orientation for the leaving group
    • G. Sulzenbacher, H. Driguez, B. Henrissat, M. Schülein, and G.J. Davies Structure of the Fusarium oxysporum endoglucanase I with a nonhydrolyzable substrate analogue: substrate distortion gives rise to the preferred axial orientation for the leaving group Biochemistry 35 1996 15280 15287
    • (1996) Biochemistry , vol.35 , pp. 15280-15287
    • Sulzenbacher, G.1    Driguez, H.2    Henrissat, B.3    Schülein, M.4    Davies, G.J.5
  • 51
    • 84855889658 scopus 로고    scopus 로고
    • From the regulation of peptidoglycan synthesis to bacterial growth and morphology
    • A. Typas, M. Banzhaf, C.A. Gross, and W. Vollmer From the regulation of peptidoglycan synthesis to bacterial growth and morphology Nat. Rev. Microbiol. 10 2012 123 136
    • (2012) Nat. Rev. Microbiol. , vol.10 , pp. 123-136
    • Typas, A.1    Banzhaf, M.2    Gross, C.A.3    Vollmer, W.4
  • 52
    • 84455162073 scopus 로고    scopus 로고
    • Peptidoglycan hydrolases of Escherichia coli
    • J. van Heijenoort Peptidoglycan hydrolases of Escherichia coli Microbiol. Mol. Biol. Rev. 75 2011 636 663
    • (2011) Microbiol. Mol. Biol. Rev. , vol.75 , pp. 636-663
    • Van Heijenoort, J.1
  • 53
    • 0033081517 scopus 로고    scopus 로고
    • Three-dimensional structure of a barley β-D-glucan exohydrolase, a family 3 glycosyl hydrolase
    • J.N. Varghese, M. Hrmova, and G.B. Fincher Three-dimensional structure of a barley β-D-glucan exohydrolase, a family 3 glycosyl hydrolase Structure 7 1999 179 190
    • (1999) Structure , vol.7 , pp. 179-190
    • Varghese, J.N.1    Hrmova, M.2    Fincher, G.B.3
  • 54
    • 25444533563 scopus 로고    scopus 로고
    • Detailed comparative analysis of the catalytic mechanisms of β-N-acetylglucosaminidases from families 3 and 20 of glycoside hydrolases
    • D.J. Vocadlo, and S.G. Withers Detailed comparative analysis of the catalytic mechanisms of β-N-acetylglucosaminidases from families 3 and 20 of glycoside hydrolases Biochemistry 44 2005 12809 12818
    • (2005) Biochemistry , vol.44 , pp. 12809-12818
    • Vocadlo, D.J.1    Withers, S.G.2
  • 55
    • 53849121583 scopus 로고    scopus 로고
    • Mechanistic insights into glycosidase chemistry
    • D.J. Vocadlo, and G.J. Davies Mechanistic insights into glycosidase chemistry Curr. Opin. Chem. Biol. 12 2008 539 555
    • (2008) Curr. Opin. Chem. Biol. , vol.12 , pp. 539-555
    • Vocadlo, D.J.1    Davies, G.J.2
  • 56
    • 0034635169 scopus 로고    scopus 로고
    • Mechanism of action and identification of Asp242 as the catalytic nucleophile of Vibrio furnisii N-acetyl-β-D-glucosaminidase using 2-acetamido-2-deoxy-5-fluoro-α-L-idopyranosyl fluoride
    • D.J. Vocadlo, C. Mayer, S. He, and S.G. Withers Mechanism of action and identification of Asp242 as the catalytic nucleophile of Vibrio furnisii N-acetyl-β-D-glucosaminidase using 2-acetamido-2-deoxy-5-fluoro-α-L- idopyranosyl fluoride Biochemistry 39 2000 117 126
    • (2000) Biochemistry , vol.39 , pp. 117-126
    • Vocadlo, D.J.1    Mayer, C.2    He, S.3    Withers, S.G.4
  • 57
    • 0035939953 scopus 로고    scopus 로고
    • Catalysis by hen egg-white lysozyme proceeds via a covalent intermediate
    • D.J. Vocadlo, G.J. Davies, R. Laine, and S.G. Withers Catalysis by hen egg-white lysozyme proceeds via a covalent intermediate Nature 412 2001 835 838
    • (2001) Nature , vol.412 , pp. 835-838
    • Vocadlo, D.J.1    Davies, G.J.2    Laine, R.3    Withers, S.G.4
  • 59
    • 0034671524 scopus 로고    scopus 로고
    • Characterization of a β-N-acetylglucosaminidase of Escherichia coli and elucidation of its role in muropeptide recycling and β-lactamase induction
    • W. Vötsch, and M.F. Templin Characterization of a β-N-acetylglucosaminidase of Escherichia coli and elucidation of its role in muropeptide recycling and β-lactamase induction J. Biol. Chem. 275 2000 39032 39038
    • (2000) J. Biol. Chem. , vol.275 , pp. 39032-39038
    • Vötsch, W.1    Templin, M.F.2
  • 61
    • 77956642710 scopus 로고    scopus 로고
    • Role of a PA14 domain in determining substrate specificity of a glycoside hydrolase family 3 β-glucosidase from Kluyveromyces marxianus
    • E. Yoshida, M. Hidaka, S. Fushinobu, T. Koyanagi, H. Minami, H. Tamaki, M. Kitaoka, T. Katayama, and H. Kumagai Role of a PA14 domain in determining substrate specificity of a glycoside hydrolase family 3 β-glucosidase from Kluyveromyces marxianus Biochem. J. 431 2010 39 49
    • (2010) Biochem. J. , vol.431 , pp. 39-49
    • Yoshida, E.1    Hidaka, M.2    Fushinobu, S.3    Koyanagi, T.4    Minami, H.5    Tamaki, H.6    Kitaoka, M.7    Katayama, T.8    Kumagai, H.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.