Abstract
Amiclenomycin, a natural product containing the 1-amino cyclohexa-2,5-diene moiety is an inhibitor of 7;8-diaminopelargonic acid aminotransferase, a pyridoxal phosphate (PLP) dependent enzyme involved in biotin biosynthesis. The postulated mechanism implies the aromatisation of the Schiff base formed between PLP and amiclenomycin. Aromatic adducts have been obtained by heating PLP with amiclenomycin and other related 1-amino cyclohexa-2,5-dienes. They were fully characterized by UV–visible and ESI mass spectrometry and provide standards for identification of the enzyme-derived products.
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