3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 4.2.3.3
BRENDA Enzyme Link: BRENDA 4.2.3.3
KEGG Enzyme Link: KEGG4.2.3.3
BioCyc Enzyme Link: BioCyc 4.2.3.3
ExPASy Enzyme Link: ExPASy4.2.3.3
EC2PDB Enzyme Link: EC2PDB 4.2.3.3
ExplorEnz Enzyme Link: ExplorEnz 4.2.3.3
PRIAM enzyme-specific profiles Link: PRIAM 4.2.3.3
IntEnz Enzyme Link: IntEnz 4.2.3.3
MEDLINE Enzyme Link: MEDLINE 4.2.3.3
MSA:

4.2.3.3;

Phylogenetic Tree:

4.2.3.3;

Uniprot:
M-CSA:
RHEA:17937 dihydroxyacetone phosphate = methylglyoxal + phosphate
RULE(radius=1) [*:1]-[O;H0;+0:2]-[CH2;+0:3]-[*:4]-[CH2;+0:5]-[OH;+0:6]>>[*:1]-[OH;+0:2].[CH3;+0:3]-[*:4]-[CH;+0:5]=[O;H0;+0:6]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Isolation of methylglyoxal synthase from goat liver.Ray S, Ray M1981 Jun 257240200
The regulation of Escherichia coli methylglyoxal synthase; a new control site in glycolysis?Hopper DJ, Cooper RA1971 Mar 1611945670
The formation and catabolism of methylglyoxal during glycolysis in Escherichia coli.Cooper RA, Anderson A1970 Dec 1111945504