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.
Publication types
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Research Support, U.S. Gov't, P.H.S.
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Review
MeSH terms
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Anti-Bacterial Agents / chemistry
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Anti-Bacterial Agents / pharmacology
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Bacterial Proteins / chemistry
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Bacterial Proteins / metabolism*
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Binding Sites
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Carbon-Sulfur Lyases
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Catalysis
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Ferrous Compounds / chemistry
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Ferrous Compounds / metabolism
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Homocysteine / analogs & derivatives*
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Homocysteine / chemistry
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Homocysteine / metabolism*
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Hydrolases / chemistry
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Hydrolases / metabolism*
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Models, Molecular
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Oxidation-Reduction
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Pentanes / chemistry
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Pentanes / metabolism
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Substrate Specificity
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Sulfides / chemistry
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Sulfides / metabolism
Substances
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4,5-dihydroxy-2,3-pentanedione
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Anti-Bacterial Agents
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Bacterial Proteins
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Ferrous Compounds
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Pentanes
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S-ribosyl-L-homocysteine
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Sulfides
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Homocysteine
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Hydrolases
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homocysteinase
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Carbon-Sulfur Lyases
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LuxS protein, Bacteria