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- W2038443856 abstract "In addition to the main transaminase reaction, the pyridoxal 5′-phosphate-dependent enzyme human liver peroxisomal alanine:glyoxylate aminotransferase (AGT) is able to catalyze the α,β-elimination of β-chloro-l-alanine with a catalytic efficiency similar to that of the physiological transaminase reaction with l-alanine. On the other hand, during the reaction of AGT with l-cysteine, changes in the coenzyme forms and analysis of the products reveal the occurrence of both β-elimination and half-transamination of l-cysteine together with the pyruvate transamination. A mechanism in which a ketimine species is the common intermediate of half-transamination and β-elimination of l-cysteine is proposed. l-cysteine partitions between these two reactions with a ratio of ~ 2.5. Rapid scanning stopped-flow and quench flow experiments permit the identification of reaction intermediates and the measurements of the kinetic parameters of l-cysteine half-transamination. The kcat of this reaction is 200- or 60-fold lower than that of l-alanine and l-serine, respectively. Conversely, l-cysteine binds to AGT with a binding affinity 30- and 200-fold higher than that of l-alanine and l-serine, respectively. This appears to be consistent with the calculated interaction energies of the l-cysteine, l-alanine and l-serine docked at the active site of AGT." @default.
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- W2038443856 date "2008-09-01" @default.
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- W2038443856 title "Reactions of human liver peroxisomal alanine:glyoxylate aminotransferase with β-chloro-L-alanine and L-cysteine: Spectroscopic and kinetic analysis" @default.
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- W2038443856 doi "https://doi.org/10.1016/j.bbapap.2008.04.013" @default.
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