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Literature summary 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

Activating Compound

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

Protein Variants

EC Number Protein Variants Comment Organism
3.5.1.124 additional information construction of yhbO/yajL and yhbO/yajL/hchA mutants displaying high amounts of glycated proteins Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.2.1.130 2,4-Dinitrophenylhydrazine inactivation; inactivation Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.5.1.124 an S-(1-hydroxy-2-oxopropyl)-[protein]-L-arginine + H2O Escherichia coli
-
 a [protein]-L-arginine + (R)-lactate
-
 ?
3.5.1.124 an S-(1-hydroxy-2-oxopropyl)-[protein]-L-cysteine + H2O Escherichia coli
-
 a [protein]-L-cysteine + (R)-lactate
-
 ?
3.5.1.124 an S-(1-hydroxy-2-oxopropyl)-[protein]-L-lysine + H2O Escherichia coli
-
 a [protein]-L-lysine + (R)-lactate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.124 Escherichia coli P45470 MG1655
-
3.5.1.124 Escherichia coli Q46948 MG1655
-
4.2.1.130 Escherichia coli P45470 MG1655
-
4.2.1.130 Escherichia coli Q46948 MG1655
-

Reaction

EC Number Reaction Comment Organism Reaction ID
3.5.1.124 an N6-(1-hydroxy-2-oxopropyl)-[protein]-L-lysine + H2O = a [protein]-L-lysine + lactate reaction mechanism via spontaneous aminocarbinol formation, H migration catalyzed by deglycase, and amidolysis by deglycase. The mechnaism is similar for L-cysteine and L-arginine deglycation Escherichia coli
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.124 an S-(1-hydroxy-2-oxopropyl)-[bovine serum albumin]-L-amino acid + H2O
-
 Escherichia coli a [bovine serum albumin]-L-amino acid + (R)-lactate
-
 ?
3.5.1.124 an S-(1-hydroxy-2-oxopropyl)-[fructose-1,6-biphosphate aldolase]-L-arginine + H2O fructose-1,6-biphosphate aldolase activity only decreases to 99%, 86% or 97%, respectively, of its initial activity, suggesting that YajL efficiently deglycates FBP as glycation occurs Escherichia coli a [fructose-1,6-biphosphate aldolase]-L-arginine + (R)-lactate
-
 ?
3.5.1.124 an S-(1-hydroxy-2-oxopropyl)-[fructose-1,6-biphosphate aldolase]-L-arginine + H2O fructose-1,6-biphosphate aldolase activity only decreases to 99%, 86% or 97%, respectively, of its initial activity, suggesting that YhbO efficiently deglycates FBP as glycation occurs Escherichia coli a [fructose-1,6-biphosphate aldolase]-L-arginine + (R)-lactate
-
 ?
3.5.1.124 an S-(1-hydroxy-2-oxopropyl)-[fructose-1,6-biphosphate aldolase]-L-lysine + H2O fructose-1,6-biphosphate aldolase activity only decreases to 99%, 86% or 97%, respectively, of its initial activity, suggesting that YajL efficiently deglycates FBP as glycation occurs Escherichia coli a [fructose-1,6-biphosphate aldolase]-L-lysine + (R)-lactate
-
 ?
3.5.1.124 an S-(1-hydroxy-2-oxopropyl)-[fructose-1,6-biphosphate aldolase]-L-lysine + H2O fructose-1,6-biphosphate aldolase activity only decreases to 99%, 86% or 97%, respectively, of its initial activity, suggesting that YhbO efficiently deglycates FBP as glycation occurs Escherichia coli a [fructose-1,6-biphosphate aldolase]-L-lysine + (R)-lactate
-
 ?
3.5.1.124 an S-(1-hydroxy-2-oxopropyl)-[glyceraldehyde-3-phosphate dehydrogenase]-L-cysteine + H2O glyceraldehyde-3-phosphate dehydrogenase activity decreases to 40% in absence of a deglycase, while in the presence of YajL, glyceraldehyde-3-phosphate dehydrogenase remains 100% active, suggesting that YajL deglycates GAPDH as glycation occurs Escherichia coli a [glyceraldehyde-3-phosphate dehydrogenase]-L-cysteine + (R)-lactate
-
 ?
3.5.1.124 an S-(1-hydroxy-2-oxopropyl)-[glyceraldehyde-3-phosphate dehydrogenase]-L-cysteine + H2O glyceraldehyde-3-phosphate dehydrogenase activity decreases to 40% in absence of a deglycase, while in the presence of YhbO, glyceraldehyde-3-phosphate dehydrogenase decreases only to 80% of its initial activity, suggesting that YhbO deglycates GAPDH as glycation occurs Escherichia coli a [glyceraldehyde-3-phosphate dehydrogenase]-L-cysteine + (R)-lactate
-
 ?
3.5.1.124 an S-(1-hydroxy-2-oxopropyl)-[protein]-L-arginine + H2O
-
 Escherichia coli a [protein]-L-arginine + (R)-lactate
-
 ?
3.5.1.124 an S-(1-hydroxy-2-oxopropyl)-[protein]-L-cysteine + H2O
-
 Escherichia coli a [protein]-L-cysteine + (R)-lactate
-
 ?
3.5.1.124 an S-(1-hydroxy-2-oxopropyl)-[protein]-L-lysine + H2O
-
 Escherichia coli a [protein]-L-lysine + (R)-lactate
-
 ?
3.5.1.124 additional information the enzyme also shows GSH-independent activity of glyoxylase III, EC 4.2.1.130. The apparent glyoxalase activity of YhbO, EC 4.2.1.130, reflects its deglycase activity Escherichia coli ?
-
 ?
4.2.1.130 2-oxoethanal + H2O i.e. glyoxal Escherichia coli acetate
-
 ?
4.2.1.130 2-oxopropanal + H2O i.e. methylglyoxal Escherichia coli (R)-lactate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.5.1.124 deglycase
-
 Escherichia coli
3.5.1.124 More cf. EC 4.2.1.130 Escherichia coli
3.5.1.124 yajL
-
 Escherichia coli
3.5.1.124 yhbO
-
 Escherichia coli
4.2.1.130 More cf. EC 3.5.1.124 Escherichia coli
4.2.1.130 yajL
-
 Escherichia coli
4.2.1.130 yhbO
-
 Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.5.1.124 22
-
 assay at Escherichia coli
4.2.1.130 22
-
 assay at 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 0.08
-
 2-oxopropanal pH 7.0, 22°C Escherichia coli
4.2.1.130 0.15
-
 2-oxoethanal pH 7.0, 22°C Escherichia coli
4.2.1.130 0.29
-
 2-oxopropanal pH 7.0, 22°C Escherichia coli
4.2.1.130 0.42
-
 2-oxoethanal pH 7.0, 22°C Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5.1.124 7
-
 assay at Escherichia coli
4.2.1.130 7
-
 assay at Escherichia coli

General Information

EC Number General Information Comment Organism
3.5.1.124 evolution enzyme YajL belongs to the PfpI/Hsp31/DJ-1 superfamily Escherichia coli
3.5.1.124 evolution enzyme YhbO belongs to the PfpI/Hsp31/DJ-1 superfamily Escherichia coli
3.5.1.124 malfunction bacterial extracts from deglycase mutants display increased glycation levels, whereas deglycase overexpression decreases protein glycation. yajL mutants display decreased viability in methylglyoxal- or glucose-containing media Escherichia coli
3.5.1.124 malfunction bacterial extracts from deglycase mutants display increased glycation levels, whereas deglycase overexpression decreases protein glycation. yhbO mutants display decreased viability in methylglyoxal- or glucose-containing media Escherichia coli
3.5.1.124 physiological function the enzyme is involved in protection against environmental stresses, it protect scells against protein glycation. It repairs glyoxal- and methylglyoxal-glycated proteins. YajL repairs glycated serum albumin, collagen, glyceraldehyde-3-phosphate dehydrogenase, and fructose biphosphate aldolase Escherichia coli
3.5.1.124 physiological function the enzyme is involved in protection against environmental stresses, it protects cells against protein glycation. It repairs glyoxal- and methylglyoxal-glycated proteins. YhbO repairs glycated serum albumin, collagen, glyceraldehyde-3-phosphate dehydrogenase, and fructose biphosphate aldolase. Overexpression of YhbO (from the pBAD-yhbO plasmid) in a wild-type strain overexpressing the YeaG kinase (from pET-21ayeaG) decreases protein aggregation from 7% to 2%, and decreases protein glycation by approximately 60% Escherichia coli
4.2.1.130 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
4.2.1.130 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