InterPro domain: IPR011607

Methylglyoxal synthase (MGS, EC 4.2.3.3), which catalyzes the conversion of dihydroxyacetone phosphate (DHAP) to methylglyoxal (MG) and inorganic phosphate, has been found in many organisms, including enteric bacteria, some gram-positive bacteria, a number of archaebacteria, several yeast species and goat liver [ 1 , 2 ].

The main core of the MGS-like domain, a modified 'Rossmann' fold, is characterised by a five stranded parallel beta-sheet flanked on either side by three and five alpha-helices, respectively [ 3 , 4 ]. MGS-like domains share a conserved phosphate binding site [ 5 , 6 ].

1. Transmitting the allosteric signal in methylglyoxal synthase. Protein Eng. Des. Sel. 26, 445-52
2. Characterization of methylglyoxal synthase from Clostridium acetobutylicum ATCC 824 and its use in the formation of 1, 2-propanediol. Appl. Environ. Microbiol. 65, 3244-7
3. Structural insights into the human and avian IMP cyclohydrolase mechanism via crystal structures with the bound XMP inhibitor. Biochemistry 43, 1171-83
4. The structure of carbamoyl phosphate synthetase determined to 2.1 A resolution. Acta Crystallogr. D Biol. Crystallogr. 55, 8-24
5. Structure classification-based assessment of CASP3 predictions for the fold recognition targets. Proteins Suppl 3, 88-103
6. Characterization of AICAR transformylase/IMP cyclohydrolase (ATIC) from Staphylococcus lugdunensis. FEBS J. 284, 4233-4261