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).
CATALYTIC METAL(S)
| Metal/Site Information | |||||
| Residue in MACiE* | Atom in MACiE* | Residue Type in MACiE | Physiological Metal |
Site Type |
Function(s) |
| MG 3001 A | MG | magnesium | divalent cation | mononuclear | Coordinates substrate Increases electrophilicity Electrostatic stabiliser |
*It refers to the MACiE reference pdb: 1d8c
| Metal/s Properties in Resting State | ||||||
| MG 3001 A | Resting state enzyme (-) | |||||
| Oxidation State | 2 | |||||
| Coordination Geometry | octahedral | |||||
| Coordination Number | 6 | |||||
| Notes | - | |||||
| References |
| -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 |