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Literature summary extracted from

  • Subedi, K.P.; Choi, D.; Kim, I.; Min, B.; Park, C.
    Hsp31 of Escherichia coli K-12 is glyoxalase III (2011), Mol. Microbiol., 81, 926-936.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.2.1.130 gene hchA Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
4.2.1.130 C185A mutation almost completely abolishes glyoxalase activity Escherichia coli
4.2.1.130 E77A mutation almost completely abolishes glyoxalase activity Escherichia coli
4.2.1.130 H184A kcat/KM is 3.6fold lower compared to the wild-type value Escherichia coli
4.2.1.130 H186A mutant enzyme shows approximately 17% remaining activity Escherichia coli
4.2.1.130 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
4.2.1.130 additional information generation of a hchA-deficient strain from Escherichia coli strain MG1655 Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.2.1.130 Cu2+ maximal inhibition below 0.025 mM Escherichia coli
4.2.1.130 EDTA an extensive dialysis of Hsp31 with 10 mM EDTA does not significantly decrease the glyoxalase III activity of more than 30% Escherichia coli
4.2.1.130 Fe3+
-
Escherichia coli
4.2.1.130 additional information the effects of some metal ions might be due to a change in oxidation state of enzyme Escherichia coli
4.2.1.130 Ni2+ inhibits slightly Escherichia coli
4.2.1.130 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.2.1.130 additional information
-
additional information Michaelis-Menten kinetics Escherichia coli
4.2.1.130 0.19
-
methylglyoxal pH 7.5, temperature not specified in the publication, mutant enzyme H184A Escherichia coli
4.2.1.130 1.43
-
methylglyoxal pH 7.5, temperature not specified in the publication, wild-type enzyme Escherichia coli
4.2.1.130 156.9
-
2-oxopropanal pH 7.5, 37°C Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.2.1.130 Fe2+ activates Escherichia coli
4.2.1.130 Fe2+ enhances activity Escherichia coli
4.2.1.130 Mg2+ activates slightly Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.2.1.130 2-oxopropanal + H2O Escherichia coli i.e. methylglyoxal (R)-lactate
-
?
4.2.1.130 methylglyoxal + H2O Escherichia coli Hsp31 efficiently detoxifies exogenously added methylglyoxal (R)-lactate
-
?

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.130 Escherichia coli
-
-
-
4.2.1.130 Escherichia coli P31658
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.2.1.130
-
Escherichia coli
4.2.1.130 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]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.2.1.130 0.254
-
pH 7.5, temperature not specified in the publication Escherichia coli
4.2.1.130 0.254
-
purified native enzyme, pH 7.5, 37°C Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.130 2-oxopropanal + H2O i.e. methylglyoxal Escherichia coli (R)-lactate
-
?
4.2.1.130 methylglyoxal + H2O
-
Escherichia coli (R)-lactate
-
?
4.2.1.130 methylglyoxal + H2O Hsp31 efficiently detoxifies exogenously added methylglyoxal Escherichia coli (R)-lactate
-
?

Synonyms

EC Number Synonyms Comment Organism
4.2.1.130 glyoxalase III
-
Escherichia coli
4.2.1.130 hchA
-
Escherichia coli
4.2.1.130 Hsp31
-
Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.2.1.130 35 40
-
Escherichia coli
4.2.1.130 37
-
-
Escherichia coli

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
4.2.1.130 10 50 activity range, profile overview Escherichia coli
4.2.1.130 25 50 25°C: about 55% of maximal activity, 50°C: about 75% of maximal activity Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.2.1.130 0.095
-
methylglyoxal pH 7.5, temperature not specified in the publication, mutant enzyme H184A Escherichia coli
4.2.1.130 1.43
-
2-oxopropanal pH 7.5, 37°C Escherichia coli
4.2.1.130 2.61
-
methylglyoxal pH 7.5, temperature not specified in the publication, wild-type enzyme Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.2.1.130 6 8
-
Escherichia coli
4.2.1.130 7.5
-
assay at Escherichia coli

pH Range

EC Number pH Minimum pH Maximum Comment Organism
4.2.1.130 4 10 activity range, profile overview Escherichia coli
4.2.1.130 5 9 pH 5.0: about 45% of maximal activity, pH 9.0: about 45% of maximal activity Escherichia coli

Expression

EC Number Organism Comment Expression
4.2.1.130 Escherichia coli the enzyme is heat-inducible up

General Information

EC Number General Information Comment Organism
4.2.1.130 malfunction the stationary-phase Escherichia coli cells becomes more susceptible to methylglyoxal when hchA is deleted Escherichia coli
4.2.1.130 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
4.2.1.130 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
4.2.1.130 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
4.2.1.130 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]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
4.2.1.130 0.5
-
methylglyoxal pH 7.5, temperature not specified in the publication, mutant enzyme H184A Escherichia coli
4.2.1.130 1.8
-
methylglyoxal pH 7.5, temperature not specified in the publication, wild-type enzyme Escherichia coli