Decarboxylases involved in polyamine biosynthesis and their inactivation by nitric oxide

Rebecca A. Hillary, Anthony E. Pegg

Research output: Contribution to journalArticlepeer-review

51 Scopus citations

Abstract

Polyamines are ubiquitous cellular components that are involved in normal and neoplastic growth. Polyamine biosynthesis is very highly regulated in mammalian cells by the activities of two key decarboxylases acting on ornithine and S-adenosylmethionine. Recent studies, which include crystallographic analysis of the recombinant human proteins, have provided a detailed knowledge of their structure and function. Ornithine decarboxylase is a PLP-requiring decarboxylase, whereas S-adenosylmethionine decarboxylase (AdoMetDC) contains a covalently bound pyruvate prosthetic group. Both enzymes have a key cysteine residue, which is involved in protonation of the Schiff base intermediate C α to form the product. These residues, Cys360 in ornithine decarboxylase (ODC) and Cys82 in AdoMetDC, react readily with nitric oxide (NO), which is therefore a potent inactivator of polyamine synthesis. The inactivation of these enzymes may mediate some of the antiproliferative actions of NO.

Original languageEnglish (US)
Pages (from-to)161-166
Number of pages6
JournalBiochimica et Biophysica Acta - Proteins and Proteomics
Volume1647
Issue number1-2
DOIs
StatePublished - Apr 11 2003

All Science Journal Classification (ASJC) codes

  • Analytical Chemistry
  • Biophysics
  • Biochemistry
  • Molecular Biology

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