Open AccessOxidative Deamination of Sulfinyl, Sulfonyl and Thiosulfonyl Amino Acids by D‐Aspartate Oxidase
Author(s) -
Marco Carlo,
Rinaldi Augusto
Publication year - 1972
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1972.tb19708.x
Subject(s) - oxidative deamination , sulfur , chemistry , amino acid , deamination , radical , enzyme , oxidase test , oxidative phosphorylation , sulfonyl , alanine , stereochemistry , biochemistry , medicinal chemistry , organic chemistry , alkyl
C 3 and C 4 α‐amino acids bearing an —SO 2 H, —SO 2 SH or —SO 3 H ω‐group are oxidatively deaminated by partially purified D‐aspartate oxidase preparations obtained from beef, pig or rabbit kidney. From the C 3 sulfur‐containing amino acids the partially oxidized sulfur radicals (—SO 2 H, —SO 2 SH) are split off during the reaction, originating pyruvate. When a fully oxidized sulfur radical (—SO 3 H) is present, sulfopyruvic acid is obtained. The C 4 sulfur‐containing amino acids all give rise to the corresponding sulfur‐containing ketoacids. The K m and V values observed with the three different enzyme preparations for all the compounds under study are reported. The present results and some observations already known suggest that the substitution of a partially or fully oxidized sulfur radical for the ω‐carboxyl group does not greatly affect the specificity of enzymes acting on dicarboxylic amino acids.