L-lanthionine oxidation by snake venom L-amino acid oxidase.

Physiological chemistry and physics Pub Date : 1982-01-01
G Ricci, G Federici, G Lucente, M Achilli, D Cavallini
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引用次数: 0

Abstract

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.

蛇毒l -氨基酸氧化酶氧化l -硫氨酸。
l -硫氨酸被蛇毒l -氨基酸氧化酶氧化,每摩尔硫氨酸释放1摩尔氨。分光光度法、色谱法和分析性质都与确定硫代氨酸的单酮衍生物为该反应的第一个酶促产物相一致。然后环化成二氢噻嗪二羧酸,这进一步受到自发变化的影响。通过l -半胱氨酸与溴丙酮酸相互作用制备了噻吩衍生物的真实样品。描述了合成产物的性质,并与酶促产物的性质进行了比较。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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