| EC |
2.3.3.9 |
| Accepted name: |
malate synthase |
| Reaction: |
acetyl-CoA + glyoxylate + H2O = (S)-malate + CoA |
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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, Gene, 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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [PMID: 12393860] |
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| [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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