Methylglyoxal synthase

Of these, two antiparallel beta sheets and one alpha helix are located in a subdomain where the N-terminus and C-terminus are in close juxtaposition.

Within the wide V-groove, there are twelve hydrogen bonds and six salt bridges between the monomers in the presence of phosphate binding.

At the peak interfaces, ten hydrogen bonds and no salt bridges connect the monomers regardless of phosphate binding.

[5] The active site contains many conserved residues for function (Asp, His, Thr) and structure (Gly, Pro).

The C-3 of DHAP is oxidized to an aldehyde, while C-1, which bears the phosphate ester, is dephosphorylated and reduced to a methyl group.

[5] Additionally, phosphate binding causes rotation of threonine residues that close the active site.

[14] Transmittance of the allosteric signal is determined to pass through Arg97 and Val101 because none of these are located in the active site, yet mutations at these residues negates any inhibitory effect of phosphate binding.

[14] The induction of salt-bridge formation between Asp10 and Arg140 is an additional inter-subunit signal transmission pathway for organisms that retain the last 10 amino acids of the monomer peptide.

[4] It has activity levels similar to that of glyceraldehyde-3-phosphate dehydrogenase from glycolysis, suggesting an interplay between the two enzymes in the breakdown of triose phosphates.

For fuel ethanol production, complete metabolism of complex combinations of sugars in E. coli by synthetic biocatalysts is necessary.

[16] This suggests that MGS production of methylglyoxal plays a role in controlling expression of sugar-specific transporters and catabolic genes in native E.coli.

[17] For biotechnological and synthetic applications, phosphate binding helps to stabilize and protect the enzyme against cold- and heat-induced denaturation.

[9] His-His interaction via the insertion of one histidine residue between Arg22 and His23 is also known to confer greater thermostability by increasing its half-life 4.6-fold.