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Literature summary extracted from
- Investigation of metal binding and activation of Escherichia coli glyoxalase I: kinetic, thermodynamic and mutagenesis studies (2004), Biochem. J., 377, 309-316.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 4.4.1.5 | expression in Escherichia coli | Escherichia coli |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 4.4.1.5 | H5Q | active in the presence of both Ni2+ and Zn2+ | Escherichia coli |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 4.4.1.5 | 0.0089 | - |
glutathione-methylglyoxal hemithioacetal | in the presence of Cd2+ | Escherichia coli |  |
| 4.4.1.5 | 0.01 | - |
glutathione-methylglyoxal hemithioacetal | in the presence of Mn2+ | Escherichia coli | |
| 4.4.1.5 | 0.01 | - |
glutathione-methylglyoxal hemithioacetal | in the presence of Fe2+ | Escherichia coli | |
| 4.4.1.5 | 0.012 | - |
glutathione-methylglyoxal hemithioacetal | in the presence of Co+ | Escherichia coli | |
| 4.4.1.5 | 0.027 | - |
glutathione-methylglyoxal hemithioacetal | in the presence of Ni2+ | Escherichia coli | |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.4.1.5 | Cd2+ | 6% of activity with Ni2+ | Escherichia coli | |
| 4.4.1.5 | Co2+ | 31% of activity with Ni2+ | Escherichia coli | |
| 4.4.1.5 | Fe2+ | 16% of activity with Ni2+ | Escherichia coli | |
| 4.4.1.5 | Mn2+ | 18% of activity with Ni2+ | Escherichia coli | |
| 4.4.1.5 | additional information | no activity with Zn2+ | Escherichia coli | |
| 4.4.1.5 | Ni2+ | required for activity | Escherichia coli | |
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 | Escherichia coli | 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 | Escherichia coli | - |
- |
- |
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 | Escherichia coli | (R)-S-lactoylglutathione | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 4.4.1.5 | GLXI | - |
Escherichia coli |
| 4.4.1.5 | glyoxalase I | - |
Escherichia coli |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 4.4.1.5 | 1.5 | - |
glutathione-methylglyoxal hemithioacetal | in the presence of Fe2+ | Escherichia coli | |
| 4.4.1.5 | 8 | - |
glutathione-methylglyoxal hemithioacetal | in the presence of Mn2+ | Escherichia coli | |
| 4.4.1.5 | 21.4 | - |
glutathione-methylglyoxal hemithioacetal | in the presence of Cd2+ | Escherichia coli | |
| 4.4.1.5 | 55.7 | - |
glutathione-methylglyoxal hemithioacetal | in the presence of Fe2+ | Escherichia coli | |
| 4.4.1.5 | 60.2 | - |
glutathione-methylglyoxal hemithioacetal | in the presence of Mn2+ | Escherichia coli | |
| 4.4.1.5 | 106 | - |
glutathione-methylglyoxal hemithioacetal | in the presence of Co+ | Escherichia coli | |
| 4.4.1.5 | 338 | - |
glutathione-methylglyoxal hemithioacetal | in the presence of Ni2+ | Escherichia coli | |
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