Disease relevance of YGR012W

• The accumulation of functionally active spinach CSase in E. coli was also demonstrated by immunoblotting and assaying enzymatic activity [1].

High impact information on YGR012W

• Cysteine synthase (CSase) [O-acetyl-L-serine acetate-lyase (adding hydrogen sulfide), EC 4.2.99.8] catalyzes the formation of L-cysteine, the key step in sulfur assimilation in plants, from O-acetyl-L-serine and hydrogen sulfide [1].
• The results are consistent with the absence of heme in the closely related enzymes O-acetylserine sulfhydrylase, threonine deaminase, and tryptophan synthase [2].
• Low-molecular-weight O-acetylserine sulfhydrylase and serine sulfhydrylase of Saccharomyces cerevisiae are the same protein [3].
• Studies with crude preparations obtained from a cysteine auxotroph of Saccharomyces cerevisiae showed that O-acetylserine sulfhydrylase could be separated from O-acetylhomoserine sulfhydrylase by chromatography on a DEAE-cellulose column and centrifugation in a sucrose density gradient [4].

Associations of YGR012W with chemical compounds

• We report here the isolation and characterization of cDNA clones encoding cysteine synthase from spinach (Spinacia oleracea L.). Internal peptide sequences were obtained from V8 protease-digested fragments of purified CSase [1].

References