Skip to main content
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1981 Aug;147(2):688–690. doi: 10.1128/jb.147.2.688-690.1981

Low-Molecular-Weight O-Acetylserine Sulfhydrylase and Serine Sulfhydrylase of Saccharomyces cerevisiae Are the Same Protein

Shuzo Yamagata 1
PMCID: PMC216093  PMID: 7021536

Abstract

Low-molecular-weight O-acetyl-l-serine sulfhydrylase was purified from a cysteine auxotroph of Saccharomyces cerevisiae and was demonstrated to be identical with l-serine sulfhydrylase.

Full text

PDF
688

Images in this article

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Becker M. A., Tomkins G. M. Pleiotrophy in a cysteine-requiring mutant of Samonella typhimurium resulting from altered protein-protein interaction. J Biol Chem. 1969 Nov 10;244(21):6023–6030. [PubMed] [Google Scholar]
  2. Braunstein A. E., Goryachenkova E. V., Tolosa E. A., Willhardt I. H., Yefremova L. L. Specificity and some other properties of liver serine sulphhydrase: evidence for its identity with cystathionine -synthase. Biochim Biophys Acta. 1971 Jul 21;242(1):247–260. doi: 10.1016/0005-2744(71)90105-7. [DOI] [PubMed] [Google Scholar]
  3. Hulanicka M. D., Hallquist S. G., Kredich N. M., Mojica-A T. Regulation of O-acetylserine sulfhydrylase B by L-cysteine in Salmonella typhimurium. J Bacteriol. 1979 Oct;140(1):141–146. doi: 10.1128/jb.140.1.141-146.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  5. Paszewski A., Grabski J. On sulfhydrylation of O-acetylserine and O-acetylhomoserine in homocysteine synthesis in yeast. Acta Biochim Pol. 1976;23(4):321–324. [PubMed] [Google Scholar]
  6. SCHLOSSMANN K., LYNEN F. Biosynthese des Cysteins aus Serin und Schwefelwasserstoff. Biochem Z. 1957;328(7):591–594. [PubMed] [Google Scholar]
  7. Vesterberg O., Svensson H. Isoelectric fractionation, analysis, and characterization of ampholytes in natural pH gradients. IV. Further studies on the resolving power in connection with separation of myoglobins. Acta Chem Scand. 1966;20(3):820–834. doi: 10.3891/acta.chem.scand.20-0820. [DOI] [PubMed] [Google Scholar]
  8. Weber K., Osborn M. The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J Biol Chem. 1969 Aug 25;244(16):4406–4412. [PubMed] [Google Scholar]
  9. Wiebers J. L., Garner H. R. Acyl derivatives of homoserine as substrates for homocysteine synthesis in Neurospora crassa, yeast, and Escherichia coli. J Biol Chem. 1967 Dec 10;242(23):5644–5649. [PubMed] [Google Scholar]
  10. Yamagata S. Occurrence of low molecular weight O-acetylserine sulfhydrylase in the yeast Saccharomyces cerevisiae. J Biochem. 1980 Nov;88(5):1419–1423. doi: 10.1093/oxfordjournals.jbchem.a133111. [DOI] [PubMed] [Google Scholar]
  11. Yamagata S., Takeshima K., Naiki N. Evidence for the identity of O-acetylserine sulfhydrylase with O-acetylhomoserine sulfhydrylase in yeast. J Biochem. 1974 Jun;75(6):1221–1229. doi: 10.1093/oxfordjournals.jbchem.a130505. [DOI] [PubMed] [Google Scholar]
  12. Yamagata S., Takeshima K., Naiki N. O-acetylserine and O-acetylhomoserine sulfhydrylase of yeast; studies with methionine auxotrophs. J Biochem. 1975 May;77(5):1029–1036. doi: 10.1093/oxfordjournals.jbchem.a130803. [DOI] [PubMed] [Google Scholar]

Articles from Journal of Bacteriology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES