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Volumn 29, Issue 2, 1997, Pages 228-239

Correlation of the enzyme activities of Bacillus stearothermophilus lactate dehydrogenase on three substrates with the results of molecular dynamics/energy minimization conformational searching

Author keywords

2 keto acid; Activity prediction; Energy minimization; Enzyme; Hydride transfer; Molecular dynamics; Proton transfer

Indexed keywords

BACTERIAL ENZYME; LACTATE DEHYDROGENASE;

EID: 0030961102     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(199710)29:2<228::AID-PROT10>3.0.CO;2-Q     Document Type: Article
Times cited : (7)

References (35)
  • 1
    • 0021774501 scopus 로고
    • Source of catalysis in the lactate dehydrogenase system: Ground-state interactions in the enzyme-substrate complex
    • Burgner, J.W., Ray, W.J. Source of catalysis in the lactate dehydrogenase system: ground-state interactions in the enzyme-substrate complex. Biochemistry 23:3636-3648, 1984.
    • (1984) Biochemistry , vol.23 , pp. 3636-3648
    • Burgner, J.W.1    Ray, W.J.2
  • 2
    • 0001321698 scopus 로고
    • Transition-state structural variation in a model for carbonyl reduction by lactate-dehydrogenase: Computational validation of empirical predictions based upon Albery-More O'Ferrall-Jencks diagrams
    • Wilkie, J., Williams, I.H. Transition-state structural variation in a model for carbonyl reduction by lactate-dehydrogenase: computational validation of empirical predictions based upon Albery-More O'Ferrall-Jencks diagrams. J. Am. Chem. Soc. 114:5423-5425, 1992.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 5423-5425
    • Wilkie, J.1    Williams, I.H.2
  • 3
    • 0027443522 scopus 로고
    • A PM3 quantum-chemical study of the pyruvate reduction-mechanism catalyzed by lactate-dehydrogenase
    • Andres, J., Moliner, V., Krechl, J., Silla, E. A PM3 quantum-chemical study of the pyruvate reduction-mechanism catalyzed by lactate-dehydrogenase. Bioorg. Chem. 21:260-274, 1993.
    • (1993) Bioorg. Chem. , vol.21 , pp. 260-274
    • Andres, J.1    Moliner, V.2    Krechl, J.3    Silla, E.4
  • 4
    • 0022978194 scopus 로고
    • Site-directed mutagenesis reveals role of mobile arginine residue in lactate dehydrognase catalysis
    • Clarke, A.R., Wigley, D.B., Chia, W.N., Barstow, D.A., Atkinson, T., Holbrook, J.J. Site-directed mutagenesis reveals role of mobile arginine residue in lactate dehydrognase catalysis. Nature 324:699-702, 1986.
    • (1986) Nature , vol.324 , pp. 699-702
    • Clarke, A.R.1    Wigley, D.B.2    Chia, W.N.3    Barstow, D.A.4    Atkinson, T.5    Holbrook, J.J.6
  • 5
    • 0028271650 scopus 로고
    • Source of catalysis in the lactate dehydrogenase system: Ground-state interactions in the enzyme-substrate complex
    • Deng, H., Zheng, J., Clarke, A.R., Holbrook, J.J., Callender, R., Burgner, J.W. Source of catalysis in the lactate dehydrogenase system: Ground-state interactions in the enzyme-substrate complex. Biochemistry. 33:2297-2305, 1994.
    • (1994) Biochemistry , vol.33 , pp. 2297-2305
    • Deng, H.1    Zheng, J.2    Clarke, A.R.3    Holbrook, J.J.4    Callender, R.5    Burgner, J.W.6
  • 6
    • 0023858354 scopus 로고
    • An investigation of the contribution made by the carboxylate group of an active site histidine-aspartate couple to binding and catalysis in lactate dehydrogenase
    • Clarke, A.R., Wilks, H.M., Barstow, D.A., Atkinson, T., Chia, W.N., Holbrook, J.J. An investigation of the contribution made by the carboxylate group of an active site histidine-aspartate couple to binding and catalysis in lactate dehydrogenase. Biochemistry 27:1617-1622, 1988.
    • (1988) Biochemistry , vol.27 , pp. 1617-1622
    • Clarke, A.R.1    Wilks, H.M.2    Barstow, D.A.3    Atkinson, T.4    Chia, W.N.5    Holbrook, J.J.6
  • 9
    • 0028043092 scopus 로고
    • From analysis to the synthesis of a general purpose catalysts for the production of chirons
    • Warwick, UK: Institution of Chemical Engineers, [ISBN 0 85295 334 8]
    • Hawrani, A.S., El, Moreton, K.M., Clarke, A.R., Holbrook, J.J., Wiseman A. From analysis to the synthesis of a general purpose catalysts for the production of chirons. "Proceedings of the First U.K. Conference of Applied Biocatalysis." Vol. 1. Warwick, UK: Institution of Chemical Engineers, 1994:1-3 [ISBN 0 85295 334 8].
    • (1994) Proceedings of the First U.K. Conference of Applied Biocatalysis , vol.1 , pp. 1-3
    • El Hawrani, A.S.1    Moreton, K.M.2    Clarke, A.R.3    Holbrook, J.J.4    Wiseman, A.5
  • 15
    • 0026666697 scopus 로고
    • Design of a phenyl-lactate dehydrogenase by peptide loop exchange on the B. stearothermophilus lactate dehydrogenase framework
    • Wilks, H.M., Moreton, K.M., Halsall, D.J., Hart, K.W., Sessions, R.B., Clarke, A.R., Holbrook, J.J. Design of a phenyl-lactate dehydrogenase by peptide loop exchange on the B. stearothermophilus lactate dehydrogenase framework. Biochemistry 31:7802-7806, 1992.
    • (1992) Biochemistry , vol.31 , pp. 7802-7806
    • Wilks, H.M.1    Moreton, K.M.2    Halsall, D.J.3    Hart, K.W.4    Sessions, R.B.5    Clarke, A.R.6    Holbrook, J.J.7
  • 16
    • 0028954931 scopus 로고
    • Improved specificity toward substrates with positively charged side-chains by site-directed mutagenesis of the L-lactate dehydrogenase of Bacillus-stearothermophilus
    • Hogan, J.K., Pittol, C.A., Jones, J.B., Gold, M. Improved specificity toward substrates with positively charged side-chains by site-directed mutagenesis of the L-lactate dehydrogenase of Bacillus-stearothermophilus. Biochemistry 34:4225-4230, 1995.
    • (1995) Biochemistry , vol.34 , pp. 4225-4230
    • Hogan, J.K.1    Pittol, C.A.2    Jones, J.B.3    Gold, M.4
  • 17
    • 0029137716 scopus 로고
    • Partial reversal of the substrate stereospecificity of an L-lactate dehydrogenase by site-directed mutagenesis
    • Sakowicz, R., Gold, M., Jones, J.B. Partial reversal of the substrate stereospecificity of an L-lactate dehydrogenase by site-directed mutagenesis. J. Am. Chem. Soc. 117:2387-2394, 1995.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 2387-2394
    • Sakowicz, R.1    Gold, M.2    Jones, J.B.3
  • 18
    • 0026512524 scopus 로고
    • Structure of a ternary complex of an allosteric lactate dehydrogenase from Bacillus stearothermophilus at 2.5 Å resolution
    • Wigley, D.B., Gamblin, S.J., Turkenburg, J.P., Dodson, E.J., Piontek, K., Muirhead, H., Holbrook, J.J. Structure of a ternary complex of an allosteric lactate dehydrogenase from Bacillus stearothermophilus at 2.5 Å resolution. J. Mol. Biol. 223:317-335, 1992.
    • (1992) J. Mol. Biol. , vol.223 , pp. 317-335
    • Wigley, D.B.1    Gamblin, S.J.2    Turkenburg, J.P.3    Dodson, E.J.4    Piontek, K.5    Muirhead, H.6    Holbrook, J.J.7
  • 19
    • 0028362842 scopus 로고
    • Allosteric activation in Bacillus stearothermophilus Lactate dehydrogenase investigated by x-ray crystallographic analysis of a mutant designed to prevent tetramerization of the enzyme
    • Cameron, A.D., Roper, D.I., Moreton, K.M., Muirhead, H., Holbrook, J.J., Wigley, D.B. Allosteric activation in Bacillus stearothermophilus Lactate dehydrogenase investigated by x-ray crystallographic analysis of a mutant designed to prevent tetramerization of the enzyme. J. Mol. Biol. 238: 615-625, 1994.
    • (1994) J. Mol. Biol. , vol.238 , pp. 615-625
    • Cameron, A.D.1    Roper, D.I.2    Moreton, K.M.3    Muirhead, H.4    Holbrook, J.J.5    Wigley, D.B.6
  • 20
    • 0024299122 scopus 로고
    • The use of a genetically engineered tryptophan to identify the movement of a domain of B. stearothermophilus lactate dehydrogenase with the process which limits the steady-state turnover of the enzyme
    • Waldman, A.D.B., Hart, K.W., Clarke, A.R., Wigley, D.B., Barstow, D.A., Atkinson, T., Chia, W.N., Holbrook, J.J. The use of a genetically engineered tryptophan to identify the movement of a domain of B. stearothermophilus lactate dehydrogenase with the process which limits the steady-state turnover of the enzyme. Biochem. Biophys. Res. Commun. 150:752-759, 1988.
    • (1988) Biochem. Biophys. Res. Commun. , vol.150 , pp. 752-759
    • Waldman, A.D.B.1    Hart, K.W.2    Clarke, A.R.3    Wigley, D.B.4    Barstow, D.A.5    Atkinson, T.6    Chia, W.N.7    Holbrook, J.J.8
  • 21
    • 0025777309 scopus 로고
    • Analysis of protein loop closure: 2 types of hinges produce one motion in lactate-dehydrogenase
    • Gerstein, M., Chothia, C. Analysis of protein loop closure: 2 types of hinges produce one motion in lactate-dehydrogenase. J. Mol. Biol. 220:133-149, 1991.
    • (1991) J. Mol. Biol. , vol.220 , pp. 133-149
    • Gerstein, M.1    Chothia, C.2
  • 26
    • 0023188994 scopus 로고
    • Amino acid sequence of the L-lactate dehydrogenase of Bacillus caldotenax deduced from the nucleotide sequence of the cloned gene
    • Barstow, D.A., Murphy, J.P., Sharman, A.F., Clarke, A.R., Holbrook, J.J., Atkinson, T. Amino acid sequence of the L-lactate dehydrogenase of Bacillus caldotenax deduced from the nucleotide sequence of the cloned gene. Eur. J. Biochem. 165:581-586, 1987.
    • (1987) Eur. J. Biochem. , vol.165 , pp. 581-586
    • Barstow, D.A.1    Murphy, J.P.2    Sharman, A.F.3    Clarke, A.R.4    Holbrook, J.J.5    Atkinson, T.6
  • 27
    • 1842404687 scopus 로고    scopus 로고
    • GRAFIT. 3.00 .Leatherbarrow RJ. Erithacus Software Ltd. Staines UK: 1989
    • GRAFIT. 3.00 .Leatherbarrow RJ. Erithacus Software Ltd. Staines UK: 1989.
  • 28
    • 0030916534 scopus 로고    scopus 로고
    • Helix bending in alamethicin: Molecular Dynamics simulations and amide hydrogen exchange in methanol
    • Gibbs, N., Sessions, R.B., Williams, P.B., Dempsey, C.E. Helix bending in alamethicin: Molecular Dynamics simulations and amide hydrogen exchange in methanol. Biophys. J. 72:2490-2495, 1997.
    • (1997) Biophys. J. , vol.72 , pp. 2490-2495
    • Gibbs, N.1    Sessions, R.B.2    Williams, P.B.3    Dempsey, C.E.4
  • 29
    • 0013237284 scopus 로고
    • Conformational flexibility of manxane revealed by adiabatic mapping, normal mode analysis and molecular dynamics
    • Sessions, R.B., Osguthorpe, D.J., Dauber-Osguthorpe, P. Conformational flexibility of manxane revealed by adiabatic mapping, normal mode analysis and molecular dynamics. J. Phys. Chem. 99:9034-9044, 1995.
    • (1995) J. Phys. Chem. , vol.99 , pp. 9034-9044
    • Sessions, R.B.1    Osguthorpe, D.J.2    Dauber-Osguthorpe, P.3
  • 30
    • 1842335648 scopus 로고    scopus 로고
    • Doctoral thesis. University of Bristol, U.K.
    • Dafforn, T.R. Doctoral thesis. University of Bristol, U.K. 1996.
    • (1996)
    • Dafforn, T.R.1
  • 31
    • 1842336222 scopus 로고
    • A Raman spectroscopic study of pyruvate bound to lactate dehydrogenase and its R109Q and D168N Mutants
    • Deng, H., Zheng, J., Burgner, J., Clarke, A.R., Holbrook, J.J., Callender, R. A Raman spectroscopic study of pyruvate bound to lactate dehydrogenase and its R109Q and D168N Mutants. Biophys. J. 57:41, 1990.
    • (1990) Biophys. J. , vol.57 , pp. 41
    • Deng, H.1    Zheng, J.2    Burgner, J.3    Clarke, A.R.4    Holbrook, J.J.5    Callender, R.6
  • 32
    • 0023657928 scopus 로고
    • The geometries of interacting arginine-carboxyls in proteins
    • Singh, J., Thornton, J.M., Snarey, M., Campbell, S.F. The geometries of interacting arginine-carboxyls in proteins. FEBS Lett. 224:161-171, 1987.
    • (1987) FEBS Lett. , vol.224 , pp. 161-171
    • Singh, J.1    Thornton, J.M.2    Snarey, M.3    Campbell, S.F.4
  • 33
    • 0028301445 scopus 로고
    • Amino/aromatic interactions in proteins: Is the evidence stacked against hydrogen-bonding
    • Mitchell, J.B.O., Nandi, C.L., Mcdonald, I.K., Thornton, J.M., Price, S.L. Amino/aromatic interactions in proteins: is the evidence stacked against hydrogen-bonding. J. Mol. Biol. 239:315-331, 1994.
    • (1994) J. Mol. Biol. , vol.239 , pp. 315-331
    • Mitchell, J.B.O.1    Nandi, C.L.2    Mcdonald, I.K.3    Thornton, J.M.4    Price, S.L.5
  • 34
    • 0027308754 scopus 로고
    • Atomic environments of arginine side-chains in proteins
    • Nandi, C.L., Singh, J., Thornton, J.M. Atomic environments of arginine side-chains in proteins. Protein Eng. 6:247-259, 1993.
    • (1993) Protein Eng. , vol.6 , pp. 247-259
    • Nandi, C.L.1    Singh, J.2    Thornton, J.M.3
  • 35
    • 1842337368 scopus 로고
    • Doctoral thesis. University of Bristol, U.K.
    • Hawrani, A.S. El, Doctoral thesis. University of Bristol, U.K., 1995.
    • (1995)
    • El Hawrani, A.S.1


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