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Literature summary 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
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.4.1.5 | 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)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.4.1.5 | glutathione-methylglyoxal hemithioacetal | Homo sapiens | glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione | (R)-S-lactoylglutathione | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.4.1.5 | Homo sapiens | - |
- |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.4.1.5 | glutathione-methylglyoxal hemithioacetal | glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione | Homo sapiens | (R)-S-lactoylglutathione | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 4.4.1.5 | glyoxalase I | - |
Homo sapiens |
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Release 2023.1 (January 2023)
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