L-LANTHIONINE OXIDATION BY SNAKE-VENOM L-AMINO-ACID OXIDASE

  • 1 January 1982
    • journal article
    • research article
    • Vol. 14  (3) , 193-199
Abstract
L-Lanthionine is oxidized by snake venom L-amino acid oxidase with the release of 1 mol ammonia/mol lanthionine. Spectrophotometric, chromatographic, and analytical properties are all consistent with the identification of the mono-keto derivative of lanthionine as the 1st enzymatic product of the reaction. This then cyclizes into a dihydrothiazine dicarboxylic acid which is further subject to spontaneous changes. Authentic smaples of the thiazine derivative have been prepared by interacting L-cysteine with bromopyruvic acid. The properties of the synthetic product are described and compared with those exhibited by the enzymatic product.

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