Malate synthase

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In enzymology, a malate synthase (EC 2.3.3.9) is an enzyme that catalyzes the chemical reaction

acetyl-CoA + H2O + glyoxylate \rightleftharpoons (S)-malate + CoA

The 3 substrates of this enzyme are acetyl-CoA, H2O, and glyoxylate, whereas its two products are (S)-malate and CoA.

This enzyme belongs to the family of transferases, specifically those acyltransferases that convert acyl groups into alkyl groups on transfer. The systematic name of this enzyme class is acetyl-CoA:glyoxylate C-acetyltransferase (thioester-hydrolysing, carboxymethyl-forming). Other names in common use include L-malate glyoxylate-lyase (CoA-acetylating), glyoxylate transacetylase, glyoxylate transacetase, glyoxylic transacetase, malate condensing enzyme, malate synthetase, malic synthetase, and malic-condensing enzyme. This enzyme participates in pyruvate metabolism and glyoxylate and dicarboxylate metabolism.

Contents

[edit] Structural studies

As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 1P7T, 1Y8B, 2GQ3, and 2JQX.

[edit] References

[edit] External links

The CAS registry number for this enzyme class is 9013-48-3.

[edit] Gene Ontology (GO) codes

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