Abstract
The synthesis of citrate from acetyl-coenzyme A and oxaloacetate is catalyzed in most organisms by a Si-citrate synthase, which is Si-face stereospecific with respect to C-2 of oxaloacetate. However, in Clostridium kluyveri and some other strictly anaerobic bacteria, the reaction is catalyzed by a Re-citrate synthase, whose primary structure has remained elusive. We report here that Re-citrate synthase from C. kluyveri is the product of a gene predicted to encode isopropylmalate synthase. C. kluyveri is also shown to contain a gene for Si-citrate synthase, which explains why cell extracts of the organism always exhibit some Si-citrate synthase activity.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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2-Isopropylmalate Synthase / genetics*
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2-Isopropylmalate Synthase / metabolism
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Citrate (si)-Synthase / genetics*
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Citrate (si)-Synthase / metabolism
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Citrates / chemistry
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Citrates / metabolism
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Clostridium kluyveri / enzymology
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Clostridium kluyveri / genetics*
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Clostridium kluyveri / metabolism
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Genome, Bacterial
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Molecular Structure
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Oxaloacetic Acid / chemistry
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Oxaloacetic Acid / metabolism
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Oxo-Acid-Lyases / genetics*
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Oxo-Acid-Lyases / metabolism
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Phylogeny*
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Stereoisomerism
Substances
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Citrates
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Oxaloacetic Acid
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Citrate (si)-Synthase
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2-Isopropylmalate Synthase
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homocitrate synthase
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Oxo-Acid-Lyases