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

Acta Biochim Pol. 1993;40(3):421-8.


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.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aspergillus nidulans / enzymology*
  • Carbon-Oxygen Lyases*
  • Chromatography, Gel
  • Cysteine Synthase
  • Fungal Proteins / physiology*
  • Lyases / antagonists & inhibitors
  • Lyases / isolation & purification
  • Lyases / physiology*
  • Molecular Weight
  • Multienzyme Complexes*
  • Mutation / genetics
  • Saccharomyces cerevisiae / enzymology
  • Saccharomyces cerevisiae Proteins*


  • Fungal Proteins
  • Multienzyme Complexes
  • Saccharomyces cerevisiae Proteins
  • Cysteine Synthase
  • MET17 protein, S cerevisiae
  • O-acetylhomoserine (thiol)-lyase
  • Lyases
  • Carbon-Oxygen Lyases