The enzyme catalyzes the condensation of glyoxylate and acetyl-coenzyme A and hydrolysis of the intermediate to yiel malate and coenzyme A. It uses a divalent metal ion to perform the reaction (PMID10715138).
|Residue in MACiE*||Atom in MACiE*||Residue Type in MACiE||Physiological
|MG 3001 A||MG||magnesium||divalent cation||mononuclear|| Coordinates substrate|
*It refers to the MACiE reference pdb: 1d8c
|Metal/s Properties in Resting State|
|MG 3001 A||Resting state enzyme (-)|
|-Smith CV, Huang CC, Miczak A, Russell DG, Sacchettini JC, Höner zu Bentrup K|
Biochemical and structural studies of malate synthase from Mycobacterium tuberculosis.
J Biol Chem. 2003 Jan 17;278(3):1735-43. Epub 2002 Oct 21.(MEDLINE:12393860)
|-Howard BR, Endrizzi JA, Remington SJ|
Crystal structure of Escherichia coli malate synthase G complexed with magnesium and glyoxylate at 2.0 A resolution: mechanistic implications.
Biochemistry. 2000 Mar 21;39(11):3156-68.(MEDLINE:10715138)
|- Some information have been also deduced from the MACiE mechanism model|