D
IPR011607

Methylglyoxal synthase-like domain

InterPro entry
Short nameMGS-like_dom
Overlapping
homologous
superfamilies
 
domain relationships

Description

Methylglyoxal synthase (MGS,
4.2.3.3
), which catalyses 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
[6, 4]
.

The main core of the MGS-like domain, a modified 'Rossmann' fold, is characterised by a five stranded parallel β-sheet flanked on either side by three and five α-helices, respectively
[3, 5]
. MGS-like domains share a conserved phosphate binding site
[1, 2]
.

References

1.Structure classification-based assessment of CASP3 predictions for the fold recognition targets. Murzin AG. Proteins Suppl 3, 88-103, (1999). View articlePMID: 10526357

2.Characterization of AICAR transformylase/IMP cyclohydrolase (ATIC) from Staphylococcus lugdunensis. Verma P, Kar B, Varshney R, Roy P, Sharma AK. FEBS J. 284, 4233-4261, (2017). PMID: 29063699

3.Structural insights into the human and avian IMP cyclohydrolase mechanism via crystal structures with the bound XMP inhibitor. Wolan DW, Cheong CG, Greasley SE, Wilson IA. Biochemistry 43, 1171-83, (2004). View articlePMID: 14756553

4.Characterization of methylglyoxal synthase from Clostridium acetobutylicum ATCC 824 and its use in the formation of 1, 2-propanediol. Huang K, Rudolph FB, Bennett GN. Appl. Environ. Microbiol. 65, 3244-7, (1999). PMID: 10388730

5.The structure of carbamoyl phosphate synthetase determined to 2.1 A resolution. Thoden JB, Raushel FM, Benning MM, Rayment I, Holden HM. Acta Crystallogr. D Biol. Crystallogr. 55, 8-24, (1999). View articlePMID: 10089390

6.Transmitting the allosteric signal in methylglyoxal synthase. Falahati H, Pazhang M, Zareian S, Ghaemi N, Rofougaran R, Hofer A, Rezaie AR, Khajeh K. Protein Eng. Des. Sel. 26, 445-52, (2013). PMID: 23592737

Cross References

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