|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
|Reactions Classified By Substrate → Small-Molecule Reactions|
EC Number: 220.127.116.11
Supersedes EC number: 18.104.22.168
The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the direction in which it was curated.
Most BioCyc compounds have been protonated to a reference pH value of 7.3. Please see the PGDB Concepts Guide for more information.
Mass balance status: Balanced.
Enzyme Commission Primary Name: malate synthase
Enzyme Commission Synonyms: L-malate glyoxylate-lyase (CoA-acetylating), glyoxylate transacetylase, glyoxylate transacetase, glyoxylic transacetase, malate condensing enzyme, malate synthetase, malic synthetase, malic-condensing enzyme
Enzyme Commission Summary:
The enzyme catalyses the irreversible condensation of acetyl-CoA with glyoxylate to form (S)-malate. Among other functions, the enzyme participates in the glyoxylate cycle, a modified version of the TCA cycle that bypasses steps that lead to a loss of CO2.
Anstrom03: Anstrom DM, Kallio K, Remington SJ (2003). "Structure of the Escherichia coli malate synthase G:pyruvate:acetyl-coenzyme A abortive ternary complex at 1.95 A resolution." Protein Sci 12(9);1822-32. PMID: 12930982
Molina94: Molina I, Pellicer MT, Badia J, Aguilar J, Baldoma L (1994). "Molecular characterization of Escherichia coli malate synthase G. Differentiation with the malate synthase A isoenzyme." Eur J Biochem 1994;224(2);541-8. PMID: 7925370
Smith03: Smith CV, Huang CC, Miczak A, Russell DG, Sacchettini JC, Honer zu Bentrup K (2003). "Biochemical and structural studies of malate synthase from Mycobacterium tuberculosis." J Biol Chem 278(3);1735-43. PMID: 12393860
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