General Stability | Organism |
---|---|
DTT and either sucrose or mannitol are required for stability | Escherichia coli |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
4-hydroxymercuribenzoate | inactivates the enzyme, reversible by dithiothreitol and other thiol-group-containing compounds | Escherichia coli | |
5,5'-dithiobis-(2-nitrobenzoate) | 0.4 mM, 15 min, complete inactivation. 5 mM DTT restores activity almost completely | Escherichia coli | |
Borate | boric acid/borate buffer is moderately inhibitory | Escherichia coli | |
DTNB | - |
Escherichia coli | |
additional information | glutathione analogues, which are inhibitors of glyoxalase I, do not inhibit glyoxalase III, but the enzyme is sensitive to thiol-blocking reagents; S-methylglutathione and S-octylglutathione, even at concentrations of 20 mM and 0.25 mM respectively, have no inhibitory effect on Escherichia coli glyoxalase III | Escherichia coli | |
N-ethylmaleimide | 0.4 mM, 15 min, complete inactivation. 5 mM DTT restores activity almost completely | Escherichia coli | |
NEM | - |
Escherichia coli | |
p-hydroxymercuribenzoate | 0.4 mM, 15 min, complete inactivation. 5 mM DTT restores activity almost completely | Escherichia coli |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
40000 | - |
2 * 40000, SDS-PAGE | Escherichia coli |
41000 | - |
- |
Escherichia coli |
82000 | - |
gel filtration | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
2-oxopropanal + H2O | Escherichia coli | - |
(R)-lactate | - |
ir |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Escherichia coli | P31658 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Escherichia coli |
native enzyme 725fold by ammonium sulfate fractionation, heat treatment, gel filtration, anion exchange chromatography, and affinity chromatography on a 4-hydroxymercuribenzoate-bound resin | Escherichia coli |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
additional information | glyoxalase III activity is present in all three media in almost equal amounts ranging from 0.033 to 0.054 unit/mg of protein | Escherichia coli | - |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
0.033 | 0.054 | crude enzyme extracts, pH 8.0, 37°C | Escherichia coli |
37 | - |
pH 8.0, 37°C | Escherichia coli |
Storage Stability | Organism |
---|---|
-15°C, 1 mM DTT and 10% sucrose, almost completely stable | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2-oxopropanal + H2O | - |
Escherichia coli | (R)-lactate | - |
ir | |
2-oxopropanal + H2O | stereospcific recation | Escherichia coli | (R)-lactate | - |
ir | |
methylglyoxal + H2O | glyoxalase III does not catalyse the reverse reaction. Glyoxalase III cannot catalyse either the formation or the breakdown of S-D-lactoylglutathione | Escherichia coli | (R)-lactate | - |
ir | |
additional information | purified glyoxalase III can catalyse the conversion of methylglyoxal into S-D-lactoylglutathione in the presence of GSH or S-D-lactoylglutathione into D-lactate, cf. EC 4.4.1.5 | Escherichia coli | ? | - |
? | |
phenylglyoxal + H2O | - |
Escherichia coli | ? | - |
ir | |
phenylglyoxal + H2O | the rate with phenylglyoxal is about 15% of that with methylglyoxal | Escherichia coli | ? | - |
ir |
Subunits | Comment | Organism |
---|---|---|
dimer | 2 * 40000, SDS-PAGE | Escherichia coli |
dimer | 2 * 41000, about, SDS-PAGE | Escherichia coli |
Synonyms | Comment | Organism |
---|---|---|
glyoxalase III | - |
Escherichia coli |
glyoxylase III | - |
Escherichia coli |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Escherichia coli |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6 | 8 | no sharp optimum | Escherichia coli |
8 | - |
assay at | Escherichia coli |
8 | - |
glyoxalase III is active over a wide range of pH with no sharp pH optimum | Escherichia coli |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
5 | 10 | pH 5.0: sharp decrease in reaction rate below, pH 10.0: activity 20-25% lower than the rate at physiological pH | Escherichia coli |
5 | 10 | glyoxalase III is active over a wide range of pH with no sharp pH optimum, sharp decrease in reaction rate occurs below pH 5.0, 20.25% of maximal activity at pH 10.0 | Escherichia coli |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
additional information | no requirement for glutathione, GSH | Escherichia coli |