Aug 30, 1976

Oxidation of S-e-carboxymethyl-selenocysteine by L-aminoacid oxidase and by D-aspartate oxidase

Molecular and Cellular Biochemistry
C De MarcoS Dernini

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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References

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Citations

Mentioned in this Paper

D-Amino Acid Dehydrogenase
Snake Venoms
Selenium
Enzymes, antithrombotic
Sulfur
Kidney
Oxidation
D-Aspartate oxidase
Blood Ammonia Measurement
Ammonia Inhalants

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