Inhibition of Saccharomyces cerevisiae phosphomannose isomerase by the NO-donor S-nitroso-acetyl-penicillamine

L. Salvati, M. Mattu, F. Tiberi, F. Polticelli, P. Ascenzi

Research output: Contribution to journalArticlepeer-review


Phosphomannose isomerase (PMI; EC. is an essential metalloenzyme in the early steps of the protein glycosylation pathway in both prokaryotes and eukaryotes. The Cys150 residue (according to Candida albicans PMI numbering) is conserved in the active centre of mammalian and yeast PMI, but not in bacterial species where it is replaced by Asn. Here, the dose- and time-dependent inhibitory effect of the NO-donor S-nitroso-acetyl-penicillamine on the Saccharomyces cerevisiae PMI catalytic activity is reported. The analysis of the X-ray crystal structure of C. albicans PMI and of the molecular model of S. cerevisiae PMI provides a rationale for the low reactivity of Cys150 towards alkylating and nitrosylating agents.

Original languageEnglish
Pages (from-to)287-292
Number of pages6
JournalJournal of Enzyme Inhibition
Issue number3
Publication statusPublished - 2001


  • Enzyme inhibition
  • Nitric oxide
  • Phosphomannose isomerase
  • S-nitroso-acetyl-penicillamine
  • Saccharomyces cerevisiae
  • Yeast

ASJC Scopus subject areas

  • Molecular Medicine
  • Biochemistry


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