Malate synthase (EC: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. Malate synthase has a TIM beta/alpha-barrel fold [1].
Malate synthase is a protein of 530 to 570 amino acids whose sequence is highly conserved across species [2]. The signature pattern for this entry is to a very conserved region in the central section of the enzyme.
Howard BR, Endrizzi JA, Remington SJ.
Crystal structure of Escherichia coli malate synthase G complexed with magnesium and glyoxylate at 2.0 A resolution: mechanistic implications.
Biochemistry 39 3156-68 2000
[PubMed: 10715138] http://dx.doi.org/10.1021/bi992519h