IPR011076
Malate synthase superfamily
InterPro entry
Short name | Malate_synth_sf |
Overlapping entries |
Description
Malate synthase (MS) (
2.3.3.9) catalyses the aldol condensation of glyoxylate with acetyl-CoA to form malate as part of the second step of the glyoxylate bypass and an alternative to the tricarboxylic acid cycle in bacteria, fungi and plants. There have been identified two isoforms, A and G (MSA and MSG, respectively) that differ in size and is attributed to an inserted α/β domain in MSG that may have regulatory function
[2, 3]. MSA and MSG consist of an N-terminal α-helical clasp domain, a central TIM-barrel domain and a C-terminal helical plug domain. In malate synthases, the TIM β/α-barrel fold and the C-terminal helical domain are well conserved and the cleft between them forms the active site
[2, 3, 1].
References
1.Crystal structure of Escherichia coli malate synthase G complexed with magnesium and glyoxylate at 2.0 A resolution: mechanistic implications. Howard BR, Endrizzi JA, Remington SJ. Biochemistry 39, 3156-68, (2000). View articlePMID: 10715138
2.Atomic resolution structures of Escherichia coli and Bacillus anthracis malate synthase A: comparison with isoform G and implications for structure-based drug discovery. Lohman JR, Olson AC, Remington SJ. Protein Sci. 17, 1935-45, (2008). View articlePMID: 18714089
3.Structure of the Escherichia coli malate synthase G:pyruvate:acetyl-coenzyme A abortive ternary complex at 1.95 A resolution. Anstrom DM, Kallio K, Remington SJ. Protein Sci. 12, 1822-32, (2003). View articlePMID: 12930982
GO terms
Cross References
Contributing Member Database Entry
- SUPERFAMILY:SSF51645