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Literature summary for 3.5.1.124 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 3.5.1.124

Protein Variants

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

Natural Substrates/ Products (Substrates)

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

Organism

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

Reaction

Reaction Comment Organism Reaction ID
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)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
an S-(1-hydroxy-2-oxopropyl)-[bovine serum albumin]-L-amino acid + H2O
-
 Escherichia coli a [bovine serum albumin]-L-amino acid + (R)-lactate
-
 ?
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
-
 ?
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
-
 ?
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
-
 ?
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
-
 ?
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
-
 ?
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
-
 ?
an S-(1-hydroxy-2-oxopropyl)-[protein]-L-arginine + H2O
-
 Escherichia coli a [protein]-L-arginine + (R)-lactate
-
 ?
an S-(1-hydroxy-2-oxopropyl)-[protein]-L-cysteine + H2O
-
 Escherichia coli a [protein]-L-cysteine + (R)-lactate
-
 ?
an S-(1-hydroxy-2-oxopropyl)-[protein]-L-lysine + H2O
-
 Escherichia coli a [protein]-L-lysine + (R)-lactate
-
 ?
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 ?
-
 ?

Synonyms

Synonyms Comment Organism
deglycase
-
 Escherichia coli
More cf. EC 4.2.1.130 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

pH Optimum

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

General Information

General Information Comment Organism
evolution enzyme YajL belongs to the PfpI/Hsp31/DJ-1 superfamily Escherichia coli
evolution enzyme YhbO belongs to the PfpI/Hsp31/DJ-1 superfamily Escherichia coli
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
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
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
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