On the factors controlling the structural specificity and stereospecificity of the L-lactate dehydrogenase from Bacillus stearothermophilus: effects of Gln102.fwdarw.Arg and Arg171... von Kallwass, Helmut K. W, Hogan, James K, Macfarlane, Emma L. A, Martichonok, Valeri, Parris, Wendy, Kay, Cyril M, Gold, Marvin, Jones, J. Bryan

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Threonine 246 at the active site of the L-lactate dehydrogenase of Bacillus stearothermophilus is important for catalysis but not for substrate binding von Sakowicz, Roman, Kallwass, Helmut K. W, Parris, Wendy, Kay, Cyril M, Jones, J. Bryan, Gold, Marvin

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Effects of Gln102Arg and Cys97Gly mutations on the structural specificity and stereospecificity of the L-lactate dehydrogenase from Bacillus stearothermophilus von Kallwass, Helmut K. W, Luyten, Marcel A, Parris, Wendy, Gold, Marvin, Kay, Cyril M, Jones, J. Bryan

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Site-specific immobilization of an L-lactate dehydrogenase via an engineered surface cysteine residue von KALLWASS, H. K. W, PARRIS, W, MACFARLANE, E. L. A, GOLD, M, JONES, J. B

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Potential of R-2-Hydroxyisocaproate dehydrogenase from Lactobacillus casei for stereospecific reductions von Kallwass, Helmut K.W.

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Single amino acid substitutions can further increase the stability of a thermophilic L-lactate dehydrogenase von Kallwass, Helmut K.W., Surewicz, Witold K., Parris, Wendy, Macfarlane, Emma L.A., Luyten, Marcel A., Kay, Cyril M., Gold, Marvin, Jones, J.Bryan

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Crystallization and preliminary X-ray diffraction studies of two mutants of lactate dehydrogenase from Bacillus stearothermophilus von Huang, Kui, Kodandapani, R., Kallwass, Helmut, Hogan, James K., Parris, Wendy, Friesen, James D., Gold, Marvin, Jones, J. Bryan, James, Michael N. G.

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