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Literature summary for 3.5.1.124 extracted from

  • Mihoub, M.; Abdallah, J.; Gontero, B.; Dairou, J.; Richarme, G.
    The DJ-1 superfamily member Hsp31 repairs proteins from glycation by methylglyoxal and glyoxal (2015), Biochem. Biophys. Res. Commun., 463, 1305-1310.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene hchA 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 P31658
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
an S-(1-hydroxy-2-oxopropyl)-[aspartate aminotransferase]-L-arginine + H2O
-
Escherichia coli a [aspartate aminotransferase]-L-arginine + (R)-lactate
-
?
an S-(1-hydroxy-2-oxopropyl)-[aspartate aminotransferase]-L-lysine + H2O
-
Escherichia coli a [aspartate aminotransferase]-L-lysine + (R)-lactate
-
?
an S-(1-hydroxy-2-oxopropyl)-[bovine serum albumin]-L-lysine + H2O
-
Escherichia coli a [bovine serum albumin]-L-lysine + (R)-lactate
-
?
an S-(1-hydroxy-2-oxopropyl)-[fructose-1,6-biphosphate aldolase]-L-arginine + H2O
-
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
-
Escherichia coli a [fructose-1,6-biphosphate aldolase]-L-lysine + (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 DJ-1 also shows glyoxalase III activity, cf. EC 4.2.1.130, which is representative of its deglycase activity Escherichia coli ?
-
?
S-(1-hydroxy-2-oxopropyl)-N-acetyl-L-cysteine + H2O
-
Escherichia coli N-acetyl-L-cysteine + (R)-lactate
-
?

Synonyms

Synonyms Comment Organism
glutathione-independent glyoxalase
-
Escherichia coli
glyoxalase
-
Escherichia coli
hchA
-
Escherichia coli
Hsp31
-
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 Hsp31 is a member of the PfpI/Hsp31/DJ-1 superfamily whose members possess a conserved exposed cysteine involved in environmental stress resistance Escherichia coli
malfunction bacterial extracts from a hchA mutant display increased glycation levels and the apparent glyoxylase activity of Hsp31 reflects its deglycase activity Escherichia coli
physiological function Hsp31 is reported to function as a chaperone, an aminopeptidase, and a glutathione-independent glyoxylase. Enzyme Hsp31 repairs proteins from glycation by methylglyoxal and glyoxal, it repairs glycated serum albumin, glyceraldehyde-3-phosphate dehydrogenase, fructose biphosphate aldolase, and aspartate aminotransferase. Since glycation with methylglyoxal and glyoxal inactivates the enzymes partially or completely, the protein deglycase HSp31 functionally protects the enzymes. To execute its deglycase activity, Hsp31 recruits its previously reported functions: 1. chaperone activity to interact with nonnative glycated proteins and gain access to partially buried glycated sites, 2. glyoxalase 1 activity to interact with glycated substrates and convert hemithioacetals into thioesters, and aminocarbinols into amides, 3. reactive cysteine 185 to attack carbonyl groups of thioesters and amides, 4. glyoxalase 2 activity to cut thioesters for cysteine deglycation, and 5. amidase/peptidase activity to cut amide bonds for lysine/arginine deglycation. The requirement of these apparently disparate functions of Hsp31 for deglycation strongly suggests that deglycation is its primary function Escherichia coli