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Publication Detail

Title: Enzymatic reaction of beta-N-methylaminoalanine with L-amino acid oxidase.

Authors: Hashmi, M; Anders, M W

Published In Biochim Biophys Acta, (1991 May 24)

Abstract: The reaction of beta-N-methylaminoalanine (BMAA) with L-amino acid oxidase (L-AAO) in the presence of catalase yields ammonia and beta-N-methylaminopyruvate, which was trapped as its 2,4-dinitrophenylhydrazone, as products. Incubation of BMAA with L-AAO in the presence of semicarbazide led to the formation of a semicarbazone, indicating intermediate iminium ion formation; when potassium cyanide (5 mM) was added, semicarbazone formation was blocked. The formation of beta-N-methylaminopyruvate was decreased by omission of catalase and was reduced in the presence of hydrogen peroxide (100 mM). These results indicate that BMAA is converted by L-AAO to the corresponding alpha-imino acid, which undergoes hydrolysis to beta-N-methylaminopyruvate. The alpha-keto acid is readily oxidized to N-methylglycine by hydrogen peroxide.

PubMed ID: 2043677 Exiting the NIEHS site

MeSH Terms: No MeSH terms associated with this publication

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