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Literature summary for 4.4.1.5 extracted from
- Active site structure and mechanism of human glyoxalase I-an ab initio theoretical study (2001), J. Am. Chem. Soc., 123, 6973-6982.
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Zn2+ | metal center of the active site zinc complex plays a direct catalytical role by binding the substrate and stabilizing the proposed enediolate reaction intermediate, one Zn2+-ion per active site | Homo sapiens |  |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| glutathione-methylglyoxal hemithioacetal | Homo sapiens | glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione | (R)-S-lactoylglutathione | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| glutathione-methylglyoxal hemithioacetal | glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione | Homo sapiens | (R)-S-lactoylglutathione | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| glyoxalase I | - |
Homo sapiens |
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