InterPro domain: IPR044856

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 alpha/beta domain in MSG that may have regulatory function 1 . In malate synthases, the TIM beta/alpha-barrel fold, containing the active site, and the C-terminal domain are well conserved [ 2 , 2 ].

This superfamily represents the alpha-helical C-terminal domain of malate synthases that caps the active site [ 3 ].

1. Atomic resolution structures of Escherichia coli and Bacillus anthracis malate synthase A: comparison with isoform G and implications for structure-based drug discovery. Protein Sci. 17, 1935-45
2. Crystal structure of Escherichia coli malate synthase G complexed with magnesium and glyoxylate at 2.0 A resolution: mechanistic implications. Biochemistry 39, 3156-68