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PROSITE documentation PDOC00422 [for PROSITE entry PS00480]

Citrate synthase signature





Description

Citrate synthase (EC 2.3.3.1) (CS) is the tricarboxylic acid cycle enzyme that catalyzes the synthesis of citrate from oxaloacetate and acetyl-CoA in an aldol condensation. CS can directly form a carbon-carbon bond in the absence of metal ion cofactors.

In prokaryotes, citrate synthase is composed of six identical subunits. In eukaryotes, there are two isozymes of citrate synthase: one is found in the mitochondrial matrix, the second is cytoplasmic. Both seem to be dimers of identical chains.

There are a number of regions of sequence similarity between prokaryotic and eukaryotic citrate synthases. One of the best conserved contains a histidine which is one of three residues shown [1] to be involved in the catalytic mechanism of the vertebrate mitochondrial enzyme. We used this region as a signature pattern.

Last update:

April 2006 / Pattern revised.

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Technical section

PROSITE method (with tools and information) covered by this documentation:

CITRATE_SYNTHASE, PS00480; Citrate synthase signature  (PATTERN)


Reference

1AuthorsKarpusas M. Branchaud B. Remington S.J.
TitleProposed mechanism for the condensation reaction of citrate synthase: 1.9-A structure of the ternary complex with oxaloacetate and carboxymethyl coenzyme A.
SourceBiochemistry 29:2213-2219(1990).
PubMed ID2337600



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