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Literature summary extracted from
- Molecular enzymology of the glyoxalase system (2008), Drug Metabol. Drug Interact., 23, 13-27.
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.4.1.5 | additional information | glyoxalase I is highly overexpressed in highly invasive tumors in comparison to tumors with low malignant potential | Mus musculus |
Application
| EC Number | Application | Comment | Organism |
|---|---|---|---|
| 3.1.2.6 | drug development | cancer therapy, inhibitors of the glyoxalase system would be expected to suppress the growth of cancer cells and could find clinical use as anticancer drug | Mus musculus |
| 4.4.1.5 | drug development | cancer therapy, inhibitors of the glyoxalase system would be expected to suppress the growth of cancer cells and could find clinical use as anticancer drug | Mus musculus |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.1.2.6 | transcription factor p63 | upregulation of glyoxalase II | Mus musculus | |
| 3.1.2.6 | transcription factor p73 | upregulation of glyoxalase II | Mus musculus | |
| 4.4.1.5 | S-(4-bromophenyl)glutathione | glyoxalase I | Mus musculus |  |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 3.1.2.6 | cytosol | - |
Mus musculus | 5829 | - |
| 3.1.2.6 | mitochondrion | - |
Mus musculus | 5739 | - |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.1.2.6 | Fe2+ | catalytic process of glyoxalase II involves a water moleule activated by a binuclear metal center containing one zinc atom plus a second bivalent metal ion which could be a zinc or an iron | Mus musculus | |
| 3.1.2.6 | Zn2+ | essential role in catalytic mechanism | Mus musculus | |
| 4.4.1.5 | additional information | a wide range of bivalent metal ions can substitute for zinc in glyoxalase I from mammalian sources, and several of them afford enzyme activities of similar magnitude to the zinc-containing glyoxalase I | Mus musculus | |
| 4.4.1.5 | Zn2+ | essential role in catalytic mechanism | Mus musculus | |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.1.2.6 | additional information | Mus musculus | catalytic process involves a water molecule activated by a binuclear metal center containing one zinc atom plus a second bivalent metal ion which could be a zinc or an iron | ? | - |
? | |
| 3.1.2.6 | additional information | Mus musculus | glyoxalase system containing glyoxalase I and II catalyzes the conversion of 2-oxoaldehydes into their corresponding 2-hydroxyacids | ? | - |
? | |
| 3.1.2.6 | S-(2-hydroxyacyl)glutathione + H2O | Mus musculus | second step in the glyoxalase system | glutathione + a 2-hydroxycarboxylate anion | regeneration of glutathione for the first step in the glyoxalase system | ir | |
| 3.1.2.6 | S-D-lactoylglutathione + H2O | Mus musculus | - |
D-lactate + glutathione | - |
? | |
| 4.4.1.5 | methylglyoxal + glutathione | Mus musculus | first step in the glyoxalase system | (R)-S-lactoylglutathione | - |
r | |
| 4.4.1.5 | additional information | Mus musculus | glyoxalase system containing glyoxalase I and II catalyzes the conversion of 2-oxoaldehydes into their corresponding 2-hydroxyacids | ? | - |
? | |
| 4.4.1.5 | additional information | Mus musculus | major cellular function of glycolase I is the inactivation of methylglyoxal, a toxic by-product of the triose phosphate isomerase reaction of glycolysis | ? | - |
? | |
| 4.4.1.5 | additional information | Mus musculus | reaction involves abstraction of a proton from carbon 1 and reinsertion of the proton at carbon 2. Proton transfer takes place with limited proton exchange with the surrounding medium, and a hydride transfer is involved. In the absence of substrate or product, the metal is coordinated with 2 water molecules in addition to the side chains of Gln33 and Glu99 in the same subunit and His126 and Glu172 from the neighbouring subunit. During the catalytic process the water molecule are displaced by the incoming substrate. Glu172 serves as the acid-base in the catalytic mechanism. | ? | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.1.2.6 | Mus musculus | - |
- |
- |
| 4.4.1.5 | Mus musculus | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.1.2.6 | by affinity chromatography | Mus musculus |
| 4.4.1.5 | by affinity chromatography | Mus musculus |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.1.2.6 | additional information | catalytic process involves a water molecule activated by a binuclear metal center containing one zinc atom plus a second bivalent metal ion which could be a zinc or an iron | Mus musculus | ? | - |
? | |
| 3.1.2.6 | additional information | glyoxalase system containing glyoxalase I and II catalyzes the conversion of 2-oxoaldehydes into their corresponding 2-hydroxyacids | Mus musculus | ? | - |
? | |
| 3.1.2.6 | S-(2-hydroxyacyl)glutathione + H2O | second step in the glyoxalase system | Mus musculus | glutathione + a 2-hydroxycarboxylate anion | regeneration of glutathione for the first step in the glyoxalase system | ir | |
| 3.1.2.6 | S-D-lactoylglutathione + H2O | - |
Mus musculus | D-lactate + glutathione | - |
? | |
| 4.4.1.5 | methylglyoxal + glutathione | first step in the glyoxalase system | Mus musculus | (R)-S-lactoylglutathione | - |
r | |
| 4.4.1.5 | additional information | glyoxalase system containing glyoxalase I and II catalyzes the conversion of 2-oxoaldehydes into their corresponding 2-hydroxyacids | Mus musculus | ? | - |
? | |
| 4.4.1.5 | additional information | major cellular function of glycolase I is the inactivation of methylglyoxal, a toxic by-product of the triose phosphate isomerase reaction of glycolysis | Mus musculus | ? | - |
? | |
| 4.4.1.5 | additional information | reaction involves abstraction of a proton from carbon 1 and reinsertion of the proton at carbon 2. Proton transfer takes place with limited proton exchange with the surrounding medium, and a hydride transfer is involved. In the absence of substrate or product, the metal is coordinated with 2 water molecules in addition to the side chains of Gln33 and Glu99 in the same subunit and His126 and Glu172 from the neighbouring subunit. During the catalytic process the water molecule are displaced by the incoming substrate. Glu172 serves as the acid-base in the catalytic mechanism. | Mus musculus | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.1.2.6 | monomer | mammalian glyoxalase II | Mus musculus |
| 4.4.1.5 | homodimer | mammalian glyoxalase I is composed of two equal subunits which both harbor an acitve site | Mus musculus |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.1.2.6 | glyoxalase II | - |
Mus musculus |
| 4.4.1.5 | glyoxalase I | - |
Mus musculus |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.4.1.5 | glutathione | - |
Mus musculus | |
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