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pubmed-article:7556224pubmed:abstractTextThe electron distribution in the coenzyme-substrate adduct of aspartate aminotransferase was changed by replacing active-site Arg386 with alanine and introducing a new arginine residue nearby. [Y225R, R386A]Aspartate aminotransferase decarboxylates L-aspartate to L-alanine (kcat = 0.04 s-1), while its transaminase activity towards dicarboxylic amino acids is decreased by three orders of magnitude (kcat = 0.19 s-1). Molecular-dynamics simulations based on the crystal structure of the mutant enzyme suggest that a new hydrogen bond to the imine N atom of the pyridoxal-5'-phosphate- aspartate adduct and an altered electrostatic potential around its beta-carboxylate group underlie the 650,000-fold increase in the ratio of beta-decarboxylase/transaminase activity.lld:pubmed
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pubmed-article:7556224pubmed:articleTitleChanging the reaction specificity of a pyridoxal-5'-phosphate-dependent enzyme.lld:pubmed
pubmed-article:7556224pubmed:affiliationBiochemisches Institut, Universität Zürich, Switzerland.lld:pubmed
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