Thialysine is oxidatively deaminated by snake venom L-aminoacid oxidase at alkaline pH. The oxygen consumption curves show a characteristic diphasic course: the quick uptake of half a mole of oxygen per mole of substrate, in aggreement with a typical oxidative deamination, is followed by a slow extra oxygen consumption. The first product of the reaction is the corresponding alpha-oxo-epsilon-amino acid, which spontaneously cyclizes to the internal Schiff base 5-6-dihydro-delta 3,1,4-thiazin-3-carboxylic acid (TZCA). This latter has been identified by its UV absorption spectrum, by some chemical reactions, by paper chromatography, and by the production of cystamine and glyoxylic acid after prolonged oxidation of thialysine followed by acid hydrolysis. The possibility of an alpha-beta elimination reaction giving rise to cysteamine from thialysine, coupled to the oxidative deamination, has been excluded.
Oxidative deamination of thialysine by snake venom L-aminoacid oxidase. / Cini, Chiara; C., Foppoli; C. D., Marco. - In: ITALIAN JOURNAL OF BIOCHEMISTRY. - ISSN 0021-2938. - STAMPA. - 27(1978), pp. 305-320.
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|Titolo:||Oxidative deamination of thialysine by snake venom L-aminoacid oxidase.|
|Data di pubblicazione:||1978|
|Citazione:||Oxidative deamination of thialysine by snake venom L-aminoacid oxidase. / Cini, Chiara; C., Foppoli; C. D., Marco. - In: ITALIAN JOURNAL OF BIOCHEMISTRY. - ISSN 0021-2938. - STAMPA. - 27(1978), pp. 305-320.|
|Appartiene alla tipologia:||01a Articolo in rivista|