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The use of natural and unnatural amino acid substrates to define the substrate specificity differences of Escherichia coli aspartate and tyrosine aminotransferases.

The tyrosine (eTATase) and aspartate (eAATase) aminotransferases of Escherichia coli transaminate diacarboxylic amino acids with similar rate constants. However, eTATase exhibits approximately 10(2)-10(4)-fold higher second-order rate constants for the transamination of aromatic amino acids than doe...

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Autors principals: Onuffer, J. J., Ton, B. T., Klement, I., Kirsch, J. F.
Format: Artigo
Idioma:Inglês
Publicat: Cold Spring Harbor Laboratory Press 1995
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Accés en línia:https://ncbi.nlm.nih.gov/pmc/articles/PMC2143219/
https://ncbi.nlm.nih.gov/pubmed/8528072
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