Malate synthase

Function

Malate synthase (MS) catalyzes the reversible conversion of acetyl-CoA, glyoxylate and water to (S)-malate and CoA. MS participates in pyruvate, glyoxylate and dicarboxylate metabolism. There are 2 isozymes of MS. MS G is formed during growth on glycolate^[1] and MS A which metabolizes glyoxylate formed in the dissimilation of acetate.

Structural highlights

. The ternary complex contains malate, acetyl-CoA and Mg+2 ion^[2].

. Water molecules are shown as red spheres.

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3d structures of malate synthase

Malate synthase 3D structures

Structure of malate synthase G complex with CoA, malate, Hepes and Mg+2 ion (green) (PDB entry 2gq3)

Drag the structure with the mouse to rotate

ReferencesReferences

↑ Anstrom DM, Kallio K, Remington SJ. Structure of the Escherichia coli malate synthase G:pyruvate:acetyl-coenzyme A abortive ternary complex at 1.95 A resolution. Protein Sci. 2003 Sep;12(9):1822-32. PMID:12930982
↑ Anstrom DM, Remington SJ. The product complex of M. tuberculosis malate synthase revisited. Protein Sci. 2006 Aug;15(8):2002-7. PMID:16877713 doi:15/8/2002

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Michal Harel, Alexander Berchansky, Joel L. Sussman, Karsten Theis

[1] Anstrom DM, Kallio K, Remington SJ. Structure of the Escherichia coli malate synthase G:pyruvate:acetyl-coenzyme A abortive ternary complex at 1.95 A resolution. Protein Sci. 2003 Sep;12(9):1822-32. PMID:12930982

[2] Anstrom DM, Remington SJ. The product complex of M. tuberculosis malate synthase revisited. Protein Sci. 2006 Aug;15(8):2002-7. PMID:16877713 doi:15/8/2002

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