SULFUR AMINO-ACID-METABOLISM IN SCHIZOSACCHAROMYCES-POMBE - OCCURRENCE OF 2 O-ACETYLHOMOSERINE SULFHYDRYLASES AND THE LACK OF THE REVERSE TRANSSULFURATION PATHWAY
J. Brzywczy et A. Paszewski, SULFUR AMINO-ACID-METABOLISM IN SCHIZOSACCHAROMYCES-POMBE - OCCURRENCE OF 2 O-ACETYLHOMOSERINE SULFHYDRYLASES AND THE LACK OF THE REVERSE TRANSSULFURATION PATHWAY, FEMS microbiology letters, 121(2), 1994, pp. 171-174
The fission yeast Schizosaccharomyces pombe has a unique organization
of sulfur amino acid metabolism: it has two distinct O-acetylhomoserin
e sulfhydrylases (homocysteine synthases). Similar to Enterobacteriace
ae, 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 grow
th medium.