The Enzyme Database

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EC 2.3.3.9     
Accepted name: malate synthase
Reaction: acetyl-CoA + glyoxylate + H2O = (S)-malate + CoA
For diagram of the glyoxylate cycle, click here
Other name(s): L-malate glyoxylate-lyase (CoA-acetylating); glyoxylate transacetylase; glyoxylate transacetase; glyoxylic transacetase; malate condensing enzyme; malate synthetase; malic synthetase; malic-condensing enzyme; acetyl-CoA:glyoxylate C-acetyltransferase (thioester-hydrolysing, carboxymethyl-forming)
Systematic name: acetyl-CoA:glyoxylate C-acetyltransferase [(S)-malate-forming]
Comments: 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.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9013-48-3
References:
1.  Dixon, G.H., Kornberg, H.L. and Lund, P. Purification and properties of malate synthetase. Biochim. Biophys. Acta 41 (1960) 217–233. [PMID: 13816984]
2.  Molina, I., Pellicer, M.T., Badia, J., Aguilar, J. and Baldoma, L. Molecular characterization of Escherichia coli malate synthase G. Differentiation with the malate synthase A isoenzyme. Eur. J. Biochem. 224 (1994) 541–548. [PMID: 7925370]
3.  Anstrom, D.M., Kallio, K. and Remington, S.J. Structure of the Escherichia coli malate synthase G:pyruvate:acetyl-coenzyme A abortive ternary complex at 1.95 Å resolution. Protein Sci. 12 (2003) 1822–1832. [PMID: 12930982]
4.  Smith, C.V., Huang, C.C., Miczak, A., Russell, D.G., Sacchettini, J.C. and Honer zu Bentrup, K. Biochemical and structural studies of malate synthase from Mycobacterium tuberculosis. J. Biol. Chem. 278 (2003) 1735–1743. [PMID: 12393860]
[EC 2.3.3.9 created 1961 as EC 4.1.3.2, transferred 2002 to EC 2.3.3.9]
 
 


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