Purification and characterization of mitochondrial cysteine aminotransferase from rat liver.
Cysteine aminotransferase has been purified over 300-fold from rat liver mitochondria. Transamination between L-cysteine and 2-oxoglutarate, and the reverse reaction, were observed to be catalyzed by the purified enzyme but inhibited by L-aspartate. The enzyme also catalyzed transamination of alanine, 3-sulfinic acid, aspartic acid, and cysteic acid. A new reaction assay method was devised, contributing an indication that mitochondrial cysteine aminotransferase is identical to mitochondrial aspartate aminotransferase. The latter apparently catalyzed 3 transamination reactions in the cysteine degradation process within mitochondria.
D000818:Animals; D001219:Aspartate Aminotransferases / Q000032:analysis / Q000378:metabolism; D002848:Chromatography, DEAE-Cellulose; D003545:Cysteine / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D007525:Isoelectric Focusing; D008297:Male; D008930:Mitochondria, Liver / Q000201:enzymology*; D051381:Rats; D000637:Transaminases / Q000032:analysis / Q000302:isolation & purification*
D000637:Transaminases; D001219:Aspartate Aminotransferases; C019968:cysteine aminotransferase; D003545:Cysteine