Mechanism of action of S-ribosylhomocysteinase (LuxS).

Dehua Pei, Jinge Zhu

Journal: Current opinion in chemical biology 2005;8(5):492-7

PMID: 15450491

Full Text on Elsevier Science View on PubMed

Abstract

S-Ribosylhomocysteinase (LuxS) cleaves the thioether bond in S-ribosylhomocysteine to produce homocysteine and 4,5-dihydroxy-2,3-pentanedione. This reaction serves the dual purposes of detoxification of S-adenosylhomocysteine and production of type 2 quorum sensing molecule. Recent research has shown that LuxS uses Fe(2+) to catalyze an internal redox reaction, shifting the ribose carbonyl group from its C1 to C3 position. Subsequent beta-elimination completes this highly unusual reaction. LuxS and other enzymes on the same pathway may provide a novel class of antibacterial drug targets.

Address: Department of Chemistry and Ohio State Biochemistry Program, The Ohio State University, 100 West 18th Avenue, Columbus, Ohio 43210, USA. [email protected]

DOI: 10.1016/j.cbpa.2004.08.003

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MeSH Terms: Anti-Bacterial Agents, Bacterial Proteins, Binding Sites, Carbon-Sulfur Lyases, Catalysis, Ferrous Compounds, Homocysteine, Hydrolases, Models, Molecular, Oxidation-Reduction, Pentanes, Substrate Specificity, Sulfides