Reaction participants Show >> << Hide
- Name help_outline dihydroxyacetone phosphate Identifier CHEBI:57642 (Beilstein: 4428349) help_outline Charge -2 Formula C3H5O6P InChIKeyhelp_outline GNGACRATGGDKBX-UHFFFAOYSA-L SMILEShelp_outline C(CO)(COP([O-])(=O)[O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 41 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline methylglyoxal Identifier CHEBI:17158 (Beilstein: 906750; CAS: 78-98-8) help_outline Charge 0 Formula C3H4O2 InChIKeyhelp_outline AIJULSRZWUXGPQ-UHFFFAOYSA-N SMILEShelp_outline [H]C(=O)C(C)=O 2D coordinates Mol file for the small molecule Search links Involved in 25 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline phosphate Identifier CHEBI:43474 Charge -2 Formula HO4P InChIKeyhelp_outline NBIIXXVUZAFLBC-UHFFFAOYSA-L SMILEShelp_outline OP([O-])([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 992 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:17937 | RHEA:17938 | RHEA:17939 | RHEA:17940 | |
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Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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The regulation of Escherichia coli methylglyoxal synthase; a new control site in glycolysis?
Hopper D.J., Cooper R.A.
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Isolation of methylglyoxal synthase from goat liver.
Ray S., Ray M.
An enzyme fraction which specifically catalyzes the formation of methylglyoxal from dihydroxyacetone phosphate has been isolated and partially purified from goat liver. The enzyme fraction appears to be substantially free from glyoxalase I, reduced glutathione, and triosephosphate isomerase. Appro ... >> More
An enzyme fraction which specifically catalyzes the formation of methylglyoxal from dihydroxyacetone phosphate has been isolated and partially purified from goat liver. The enzyme fraction appears to be substantially free from glyoxalase I, reduced glutathione, and triosephosphate isomerase. Approximately equimolar quantities of methylglyoxal and inorganic phosphate were obtained from dihydroxyacetone phosphate. Formation of methylglyoxal was confirmed by colorimetric and enzymatic estimations as well as by paper chromatography and its spectrum. Glyceraldehyde-3-phosphate, fructose 1,6-bisphosphate, dihydroxyacetone, and glyceraldehyde, failed to act as substrates. The enzyme is inhibited by some phosphorylated compounds and inorganic phosphates. << Less
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The formation and catabolism of methylglyoxal during glycolysis in Escherichia coli.
Cooper R.A., Anderson A.