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Literature summary for 4.2.1.130 extracted from

  • Abdallah, J.; Mihoub, M.; Gautier, V.; Richarme, G.
    The DJ-1 superfamily members YhbO and YajL from Escherichia coli repair proteins from glycation by methylglyoxal and glyoxal (2016), Biochem. Biophys. Res. Commun., 470, 282-286.
    View publication on PubMed
Search for more literature for 4.2.1.130

Activating Compound

Activating Compound Comment Organism Structure
bovine serum albumin activates the glyoxalase activity of the enzyme with methylglyoxal and glyoxal Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
2,4-Dinitrophenylhydrazine inactivation; inactivation Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P45470 MG1655
-
Escherichia coli Q46948 MG1655
-

Substrates and Products (Substrate)

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

Synonyms Comment Organism
More cf. EC 3.5.1.124 Escherichia coli
yajL
-
 Escherichia coli
yhbO
-
 Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
22
-
 assay at Escherichia coli

Turnover Number [1/s]

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

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
 assay at Escherichia coli

General Information

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