Activating Compound | Comment | Organism | Structure |
---|---|---|---|
bovine serum albumin | activates the glyoxalase activity of the enzyme with methylglyoxal and glyoxal | Escherichia coli |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
2,4-Dinitrophenylhydrazine | inactivation; inactivation | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P45470 | MG1655 | - |
Escherichia coli | Q46948 | MG1655 | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2-oxoethanal + H2O | i.e. glyoxal | Escherichia coli | acetate | - |
? | |
2-oxopropanal + H2O | i.e. methylglyoxal | Escherichia coli | (R)-lactate | - |
? |
Synonyms | Comment | Organism |
---|---|---|
More | cf. EC 3.5.1.124 | Escherichia coli |
yajL | - |
Escherichia coli |
yhbO | - |
Escherichia coli |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
22 | - |
assay at | Escherichia coli |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.08 | - |
2-oxopropanal | pH 7.0, 22°C | Escherichia coli | |
0.15 | - |
2-oxoethanal | pH 7.0, 22°C | Escherichia coli | |
0.29 | - |
2-oxopropanal | pH 7.0, 22°C | Escherichia coli | |
0.42 | - |
2-oxoethanal | pH 7.0, 22°C | Escherichia coli |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
assay at | Escherichia coli |
General Information | Comment | Organism |
---|---|---|
physiological function | the apparent glyoxalase activities of DJ-1 and Hsp31 reflect their deglycase activities. YhbO also displays apparent glyoxalase activities which reflect their deglycase activities, EC 3.5.1.124. The kinetics of methylglyoxal degradation by YhbO display a lag, which is likely required for spontaneous formation of the substrate, glycated YhbO. The stimulation by bovine serum albumin of the degradation of methylglyoxal and glyoxal by the deglycases is consistent with their substrates being glycated proteins (glycated YhbO, YajL or BSA) instead of glyoxals, in accordance with YhbO being a protein deglycase rather than a glyoxalase | Escherichia coli |
physiological function | the apparent glyoxalase activities of DJ-1 and Hsp31 reflect their deglycase activities. YhbO also displays apparent glyoxalase activities which reflect their deglycase activities, EC 3.5.1.124. The stimulation by bovine serum albumin of the degradation of methylglyoxaland glyoxal by the deglycases is consistent with their substrates being glycated proteins (glycated YhbO, YajL or BSA) instead of glyoxals, in accordance with YajL being a protein deglycase rather than a glyoxalase | Escherichia coli |