L-lanthionine oxidation by snake venom L-amino acid oxidase.
L-Lanthionine is oxidized by snake venom L-amino acid oxidase with the release of one mole of ammonia per mole of lanthionine. Spectrophotometric, chromatographic, and analytical properties are all consistent with the identification of the mono-keto derivative of lanthionine as the first enzymatic product of the reaction. This then cyclizes into a dihydrothiazine dicarboxylic acid which is further subject to spontaneous changes. Authentic samples 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.
D000409:Alanine / Q000031:analogs & derivatives* / Q000378:metabolism; D000594:Amino Acid Oxidoreductases / Q000378:metabolism*; D000818:Animals; D003435:Crotalid Venoms; D050830:L-Amino Acid Oxidase; D009682:Magnetic Resonance Spectroscopy; D013058:Mass Spectrometry; D010084:Oxidation-Reduction; D012911:Snakes; D013440:Sulfides
D003435:Crotalid Venoms; D013440:Sulfides; D000594:Amino Acid Oxidoreductases; D050830:L-Amino Acid Oxidase; C001520:lanthionine; D000409:Alanine