Abstract
A fluorescent derivative of lysine-258 isolated from the active site of aspartate aminotransferase modified by treatment of the apoenzyme with pyridoxal 5'-sulfate has been characterized as a substituted 2H-pyrrolo[3,4-c]pyridine. Similar pyrrolopyridines are produced in up to 20% yield by reaction of pyridoxal sulfate with simple alkylamines or with amino acids including lysine. The latter forms two products, one of which is identical with that isolated from the enzyme. The pyrrolopyridine derived from ethylamine has been characterized by proton and 13C NMR, ultraviolet-visible, and mass spectroscopy and by its chemical reactions.
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