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Literature summary for 4.2.1.130 extracted from
- Hsp31 of Escherichia coli K-12 is glyoxalase III (2011), Mol. Microbiol., 81, 926-936.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene hchA | Escherichia coli |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| C185A | mutation almost completely abolishes glyoxalase activity | Escherichia coli |
| E77A | mutation almost completely abolishes glyoxalase activity | Escherichia coli |
| H184A | kcat/KM is 3.6fold lower compared to the wild-type value | Escherichia coli |
| H186A | mutant enzyme shows approximately 17% remaining activity | Escherichia coli |
| additional information | mutagenesis studies based on evaluation of conserved catalytic residues reveals that the Cys185 and Glu77 are essential for catalysis, whereas His186 is less crucial for enzymatic function, although it participates in the catalytic process | Escherichia coli |
| additional information | generation of a hchA-deficient strain from Escherichia coli strain MG1655 | Escherichia coli |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Cu2+ | maximal inhibition below 0.025 mM | Escherichia coli |  |
| EDTA | an extensive dialysis of Hsp31 with 10 mM EDTA does not significantly decrease the glyoxalase III activity of more than 30% | Escherichia coli | |
| Fe3+ | - |
Escherichia coli | |
| additional information | the effects of some metal ions might be due to a change in oxidation state of enzyme | Escherichia coli | |
| Ni2+ | inhibits slightly | Escherichia coli | |
| Zn2+ | maximal inhibition above 0.3 mM, 10% inhibition at 0.025 mM, more than 50% inhibition at 0.1 mM | Escherichia coli | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | Michaelis-Menten kinetics | Escherichia coli | |
| 0.19 | - |
methylglyoxal | pH 7.5, temperature not specified in the publication, mutant enzyme H184A | Escherichia coli | |
| 1.43 | - |
methylglyoxal | pH 7.5, temperature not specified in the publication, wild-type enzyme | Escherichia coli | |
| 156.9 | - |
2-oxopropanal | pH 7.5, 37°C | Escherichia coli | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Fe2+ | activates | Escherichia coli | |
| Fe2+ | enhances activity | Escherichia coli | |
| Mg2+ | activates slightly | Escherichia coli | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 2-oxopropanal + H2O | Escherichia coli | i.e. methylglyoxal | (R)-lactate | - |
? | |
| methylglyoxal + H2O | Escherichia coli | Hsp31 efficiently detoxifies exogenously added methylglyoxal | (R)-lactate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
| Escherichia coli | P31658 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Escherichia coli |
| native enzyme 27.6fold by ammonium sulfate fractionation, heat treatment, gel filtration chromatography, anion exchange chromatography, and hydrophobic interaction chromatography on n-butyl sepharose resin | Escherichia coli |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 0.254 | - |
pH 7.5, temperature not specified in the publication | Escherichia coli |
| 0.254 | - |
purified native enzyme, pH 7.5, 37°C | Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 2-oxopropanal + H2O | i.e. methylglyoxal | Escherichia coli | (R)-lactate | - |
? | |
| methylglyoxal + H2O | - |
Escherichia coli | (R)-lactate | - |
? | |
| methylglyoxal + H2O | Hsp31 efficiently detoxifies exogenously added methylglyoxal | Escherichia coli | (R)-lactate | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| glyoxalase III | - |
Escherichia coli |
| hchA | - |
Escherichia coli |
| Hsp31 | - |
Escherichia coli |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 35 | 40 | - |
Escherichia coli |
| 37 | - |
- |
Escherichia coli |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 10 | 50 | activity range, profile overview | Escherichia coli |
| 25 | 50 | 25°C: about 55% of maximal activity, 50°C: about 75% of maximal activity | Escherichia coli |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.095 | - |
methylglyoxal | pH 7.5, temperature not specified in the publication, mutant enzyme H184A | Escherichia coli | |
| 1.43 | - |
2-oxopropanal | pH 7.5, 37°C | Escherichia coli | |
| 2.61 | - |
methylglyoxal | pH 7.5, temperature not specified in the publication, wild-type enzyme | Escherichia coli | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 6 | 8 | - |
Escherichia coli |
| 7.5 | - |
assay at | Escherichia coli |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 4 | 10 | activity range, profile overview | Escherichia coli |
| 5 | 9 | pH 5.0: about 45% of maximal activity, pH 9.0: about 45% of maximal activity | Escherichia coli |
Expression
| Organism | Comment | Expression |
|---|---|---|
| Escherichia coli | the enzyme is heat-inducible | up |
General Information
| General Information | Comment | Organism |
|---|---|---|
| malfunction | the stationary-phase Escherichia coli cells becomes more susceptible to methylglyoxal when hchA is deleted | Escherichia coli |
| malfunction | glyoxalase activity is completely abolished in the gene hchA-deficient strain. Stationary-phase Escherichia coli cells become more susceptible to methylgloxal when gene hchA is deleted, which can be complemented by an expression of plasmid-encoded hch. Accumulation of intracellular methylglyoxal in hchA-deficient strains | Escherichia coli |
| additional information | Hsp31 has a putative catalytic triad consisting of Asp214, His186, and Cys185. The nucleophilic cysteine Cys185 and adjacent glutamic acid Glu77 residues are critical in enzyme catalysis, forming the core of the active site | Escherichia coli |
| physiological function | glutathione-dependent glyoxalase pathway, i.e. glyoxalase I/II, is the most important route for the in vivo detoxification of methylglyoxal. Glyoxalase III may play a critical role in conditions with limiting carbon source. The enzyme may play an important role in protecting stationary-phase cells against carbonyl toxicity | Escherichia coli |
| physiological function | enzyme Hsp31 is a heat-inducible molecular chaperone. Hsp31 also displays glyoxalase activity that catalyses the conversion of methylglyoxal to D-lactate without an additional cofactor | Escherichia coli |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.5 | - |
methylglyoxal | pH 7.5, temperature not specified in the publication, mutant enzyme H184A | Escherichia coli | |
| 1.8 | - |
methylglyoxal | pH 7.5, temperature not specified in the publication, wild-type enzyme | Escherichia coli | |
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