A nucleosidase required for in vivo function of the S-adenosyl-L-methionine radical enzyme, biotin synthase

Eunjoo Choi-Rhee, John E. Cronan

Research output: Contribution to journalArticlepeer-review

Abstract

Biotin synthase is an S-adenosyl-L-methionine (SAM) radical enzyme that inserts sulfur into dethiobiotin to produce biotin. The reaction proceeds through 5′-deoxyadenosyl radical intermediates that become reduced during the sulfur insertion step to give another product of the reaction, 5′-deoxyadenosine. We report that Escherichia coli strains lacking the 5′-methylthioadenosine/S-adenosylhomocysteine nucleosidase encoded by the pfs gene are deficient in biotin synthase activity due to accumulation of 5′-deoxyadenosine, a new substrate of the pfs-encoded nucleosidase. Physiological experiments indicate that lipoic acid synthase, another SAM radical enzyme, is also inhibited by 5′-deoxyadenosine accumulation.

Original languageEnglish (US)
Pages (from-to)589-593
Number of pages5
JournalChemistry and Biology
Volume12
Issue number5
DOIs
StatePublished - May 2005

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Pharmacology
  • Drug Discovery
  • Clinical Biochemistry

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