Oxidation of S-e-carboxymethyl-selenocysteine by L-aminoacid oxidase and by D-aspartate oxidase.
Mol Cell Biochem
; 12(2): 89-92, 1976 Aug 30.
Article
en En
| MEDLINE
| ID: mdl-8703
ABSTRACT
Se-Carboxymethyl-DL-selnocysteine (CMSeC) has been prepared in a pure crystalline form from selenocysteine and monochloracetic acid. It has been shown that CMSeC is a substrate for the L-aminoacid oxidase form snake venom and for the D-aspartate oxidase from beef kidney. Oxygen consumption and ammonia production indicate that only the L or the D form of CMSeC ar acted upon respectively by one or the other of the above enzymes. No noticeable differences were shown in the oxidation rate of CMSeC and S-carboxymethylcysteine, an indication that the substitution of a selenium for a sulfur atom in the molecule does not greatly affect the substrate specificity of the two enzymes. Data have been obtained suggesting that the product of the oxidative deamination of CMSeC Is Se-carboxymethyl-selenopyruvic acid.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Cisteína
/
D-Aminoácido Oxidasa
/
Aminoácido Oxidorreductasas
Límite:
Animals
Idioma:
En
Revista:
Mol Cell Biochem
Año:
1976
Tipo del documento:
Article