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Branched-chain amino acid transferase is poten tially attractive for making novel L-amino acids from ketoacids. To assay the enzyme meaningfully and compare activity with different ketoacid we developed an assay measuring hte production of oxoglutarate (common to all the reactions). This allowed a detailed kinetic study showing ping-pong kinetics for a range of different ketoacid substrates. The constant maximum rate shows that the rate limitation is in the glutamate-poxoglutarate half-reaction not in the handling of the various ketoacids. Thi has important and obvious implications for improvement by protein engineering.

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This page is a summary of: The specificity and kinetic mechanism of branched‐chain amino acid aminotransferase from Escherichia coli studied with a new improved coupled assay procedure and the enzyme's potential for biocatalysis, FEBS Journal, December 2013, Wiley,
DOI: 10.1111/febs.12609.
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