Sulfur amino acid metabolism in Schizosaccharomyces pombe: occurrence of two O-acetylhomoserine sulfhydrylases and the lack of the reverse transsulfuration pathway.
The fission yeast Schizosaccharomyces pombe has a unique organization of sulfur amino acid metabolism: it has two distinct O-acetylhomoserine sulfhydrylases (homocysteine synthases). Similar to Enterobacteriaceae, S. pombe lacks cystathionine beta-synthase and cystathionine gamma-lyase-the enzymes of the reverse transsulfuration pathway, by which methionine is readily metabolized to cysteine-a likely effector in the sulfur metabolite repression system. Consequently no repression of sulfate assimilation is observed when methionine is added to the growth medium.
Brzywczy
J
J
Institute of Biochemistry and Biophysics, Warszawa, Poland.
Paszewski
A
A
D000603:Amino Acids, Sulfur / Q000378:metabolism*; D019757:Carbon-Oxygen Lyases; D003547:Cysteine Synthase; D008190:Lyases / Q000378:metabolism*; D009097:Multienzyme Complexes; D029701:Saccharomyces cerevisiae Proteins; D012568:Schizosaccharomyces / Q000201:enzymology / Q000254:growth & development / Q000378:metabolism*
D000603:Amino Acids, Sulfur; D009097:Multienzyme Complexes; D029701:Saccharomyces cerevisiae Proteins; D003547:Cysteine Synthase; C103381:MET17 protein, S cerevisiae; C018725:O-acetylhomoserine (thiol)-lyase; D008190:Lyases; D019757:Carbon-Oxygen Lyases