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1993 | 40 | 3 |

Tytuł artykułu

Comparative studies on O-acetylhomoserine sulfhydrylase: physiological role and characterization of the Aspergillus nidulans enzyme

Warianty tytułu

Języki publikacji

EN

Abstrakty

O-acetylhomoserine sulfhydrylase (OAH SHLase) from Aspergillus nidulans is an oligomeric protein with a broad substrate specificity with regard to sulfhydryl compounds. As its Saccharomyces cerevisiae counterpart the enzyme also reacts with O-acetylserine and is inhibited by carbonyl reagents but not by antiserum raised against the yeast enzyme. In contrast to Saccharomyces cerevisiae the enzyme is not essential for Aspergillus nidulans as indicated by the completely prototrophic phenotype of OAH SHLase-negative mutants. Its major physiological role in Aspergillus nidulans seems to be recycling of the thiomethyl group of methylthio- adenosine but it is also a constituent of the alternative pathway of cysteine synthesis.

Wydawca

-

Rocznik

Tom

40

Numer

3

Opis fizyczny

p.421-428,fig.

Twórcy

autor
  • Polish Academy of Sciences, ul.Pawinskiego 5A, 020-106 Warszawa, Poland
autor
autor

Bibliografia

  • 1. Yamagata, S. (1989) Roles of O-acetyl-L-homo- serine sulfhydrylases in microorganisms. Biochimie 71,1125 - 1143.
  • 2. Paszewski, A. & Grabski, J. (1974) Regulation of S-amino acids biosynthesis in Aspergillus nidul­ans. Mol. Gen. Genet. 132,307 - 320.
  • 3. Paszewski, A. & Grabski, J. (1975) Enzymatic lesions in methionine mutants of Aspergillus nidulans: role and regulation of an alternative pathway for cysteine and methionine synthesis. , ]. Bacteriol. 124,893 - 904.
  • 4. Treichler, H.J., Liersch, M. & Nüesch, J. (1978) Genetics and Biochemistry of Cephalosporin Biosynthesis; in Antibiotics and Other Secondary Metabolites; Biosynthesis and Production (Hutter R., Leisinger, T. & Nüesch, J., eds.) pp. 177 -199, 5th FEMS Symposium, Academic Press Inc., London.
  • 5. Yamagata, S. (1971) Homocysteine synthesis in yeast. Partial purification and properties of O-acetylhomoserine sulfhydrylase. J. Biochem. 70,1035 -1045.
  • 6. Yamagata, S. (1976) O-Acetylserine and O-acetylhomoserine sulfhydrylase of yeast; subunit structure. J. Biochem. 80,787 - 797.
  • 7. Yamagata, S. & Takeshima, K. (1976) O-Acetyl- serine and O-acetylhomoserine sulfhydrylase of yeast; Further purification and characterization as a pyridoxal enzyme. J. Biochem. 80, 777 - 785.
  • 8. Yamagata, S., Takeshima, K. & Naiki, N. (1974) Evidence for the identity of O-acetylserine sulf­hydrylase with O-acetylhomoserine sulfhy­drylase in yeast. /. Biochem. 75,1221 - 1229.
  • 9. Kerjan, P., Cherest, H. & Surdin-Kerjan, Y. (1986) Nucleotide sequence of the Saccharomyces cerevisiae MET25 gene. Nuc. Acids Res. 14,7861 - 7871.
  • 10. Yamagata, S., Paszewski, A. & Lewandowska, I. (1990) Purification and properties of O-acetyl-L- -homoserine sulfhydrylase from Aspergillus nidulans. J. Gen. Appl. Microbiol. 36,137 -141.
  • 11. Bradford, M.M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72,248 - 254.
  • 12. Paszewski, A. & Grabski, J. (1973) Studies on P-cystathionase and O-acetylhomoserine sulf­hydrylase as the enzymes of alternative methio­nine biosynthetic pathways in Aspergillus nidulans. Acta Biochim. Polon. 20,159 -168.
  • 13. Kredich, N.M. & Tomkins, G.M. (1966) The enzymatic synthesis of L-cysteine in Escherichia coli and Salmonella typhimurium. }. Biol. Chem. 241,4955 - 4965.
  • 14. Wiebers, J.L. & Garner, H.R. (1967) Acyl derivatives of homoserine as substrates for homocysteine synthesis in Neurospora crassa, yeast, and Escherichia coli. J. Biol. Chem. 242,5644 -5649.
  • 15. Wong, F.F. (1971) The use of chloroplatinic acid as a chromatographic spray for sulfur com­pounds. J. Chromatogr. 59,448 - 451.
  • 16. Guranowski, A. & Paszewski, A. (1982) Meta­bolism of 5-methylthioadenosine in Aspergillus nidulans. Biochim. Biophys. Acta 717, 289 - 294.
  • 17. Yamagata, S. (1984) O-Acetylhomoserine sulf­hydrylase of the fission yeast Schizosaccha- romyces pombe: Partial purification, characte­rization, and its probable role in homocysteine biosynthesis. ]. Biochem. 96,1511 - 1523.

Typ dokumentu

Bibliografia

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Identyfikator YADDA

bwmeta1.element.agro-article-9c921939-ce8c-4b71-82fe-fc67043527bf
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