DESULFURATION OF L-CYSTEINE THROUGH TRANSAMINATION AND TRANS-SULFURATION IN RAT-LIVER
- 1 January 1977
- journal article
- research article
- Vol. 9 (3) , 241-246
Abstract
Desulfuration of L-cysteine by rat liver via a pathway of transamination followed by transsulfuration was studied using cyanide as a sulfur acceptor. More than a 5-fold increase in formation of thiocyanate from L-cysteine and cyanide was observed in the presence of 2-oxoglutarate and pyruvate. L-Cysteine aminotransferase and 3-mercaptopyruvate sulfurtransferase activities in the same preparations were also determined. It was concluded that L-cysteine was desulfurated through transamination and transsulfuration of the resulting 3-mercaptopyruvate, and that the rate-limiting step appears to be the transamination reaction.This publication has 6 references indexed in Scilit:
- TRANSAMINATION OF L-CYSTEINE IN RAT-LIVER MITOCHONDRIA1977
- METABOLISM OF MITOCHONDRIAL PROTEINS .I. DISTRIBUTION AND CHARACTERIZATION OF ISOZYMES OF ALANINE AMINO-TRANSFERASE IN RAT LIVER1965
- MECHANISM OF DESULPHHYDRATION OF CYSTEINE1962
- CRYSTALLINE ENZYME THAT CLEAVES HOMOSERINE AND CYSTATHIONINE .3. COENZYME RESOLUTION, ACTIVATORS, AND INHIBITORS1959
- ENZYMATIC DESULFURATION OF BETA-MERCAPTOPYRUVATE TO PYRUVATE1954
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951