Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
an S-(1-hydroxy-2-oxopropyl)-[aspartate aminotransferase]-L-arginine + H2O
a [aspartate aminotransferase]-L-arginine + (R)-lactate
-
-
-
?
an S-(1-hydroxy-2-oxopropyl)-[aspartate aminotransferase]-L-lysine + H2O
a [aspartate aminotransferase]-L-lysine + (R)-lactate
-
-
-
?
an S-(1-hydroxy-2-oxopropyl)-[bovine serum albumin]-L-lysine + H2O
a [bovine serum albumin]-L-lysine + (R)-lactate
-
-
-
?
an S-(1-hydroxy-2-oxopropyl)-[fructose-1,6-biphosphate aldolase]-L-arginine + H2O
a [fructose-1,6-biphosphate aldolase]-L-arginine + (R)-lactate
-
-
-
?
an S-(1-hydroxy-2-oxopropyl)-[fructose-1,6-biphosphate aldolase]-L-lysine + H2O
a [fructose-1,6-biphosphate aldolase]-L-lysine + (R)-lactate
-
-
-
?
an S-(1-hydroxy-2-oxopropyl)-[protein]-L-arginine + H2O
a [protein]-L-arginine + (R)-lactate
-
-
-
?
an S-(1-hydroxy-2-oxopropyl)-[protein]-L-cysteine + H2O
a [protein]-L-cysteine + (R)-lactate
-
-
-
?
an S-(1-hydroxy-2-oxopropyl)-[protein]-L-lysine + H2O
a [protein]-L-lysine + (R)-lactate
-
-
-
?
S-(1-hydroxy-2-oxopropyl)-N-acetyl-L-cysteine + H2O
N-acetyl-L-cysteine + (R)-lactate
-
-
-
?
an S-(1-hydroxy-2-oxopropyl)-[bovine serum albumin]-L-amino acid + H2O
a [bovine serum albumin]-L-amino acid + (R)-lactate
-
-
-
?
an S-(1-hydroxy-2-oxopropyl)-[fructose-1,6-biphosphate aldolase]-L-arginine + H2O
a [fructose-1,6-biphosphate aldolase]-L-arginine + (R)-lactate
an S-(1-hydroxy-2-oxopropyl)-[fructose-1,6-biphosphate aldolase]-L-lysine + H2O
a [fructose-1,6-biphosphate aldolase]-L-lysine + (R)-lactate
an S-(1-hydroxy-2-oxopropyl)-[glyceraldehyde-3-phosphate dehydrogenase]-L-cysteine + H2O
a [glyceraldehyde-3-phosphate dehydrogenase]-L-cysteine + (R)-lactate
an S-(1-hydroxy-2-oxopropyl)-[protein]-L-arginine + H2O
a [protein]-L-arginine + (R)-lactate
an S-(1-hydroxy-2-oxopropyl)-[protein]-L-cysteine + H2O
a [protein]-L-cysteine + (R)-lactate
an S-(1-hydroxy-2-oxopropyl)-[protein]-L-lysine + H2O
a [protein]-L-lysine + (R)-lactate
additional information
?
-
an S-(1-hydroxy-2-oxopropyl)-[fructose-1,6-biphosphate aldolase]-L-arginine + H2O
a [fructose-1,6-biphosphate aldolase]-L-arginine + (R)-lactate
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
-
-
?
an S-(1-hydroxy-2-oxopropyl)-[fructose-1,6-biphosphate aldolase]-L-arginine + H2O
a [fructose-1,6-biphosphate aldolase]-L-arginine + (R)-lactate
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
-
-
?
an S-(1-hydroxy-2-oxopropyl)-[fructose-1,6-biphosphate aldolase]-L-lysine + H2O
a [fructose-1,6-biphosphate aldolase]-L-lysine + (R)-lactate
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
-
-
?
an S-(1-hydroxy-2-oxopropyl)-[fructose-1,6-biphosphate aldolase]-L-lysine + H2O
a [fructose-1,6-biphosphate aldolase]-L-lysine + (R)-lactate
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
-
-
?
an S-(1-hydroxy-2-oxopropyl)-[glyceraldehyde-3-phosphate dehydrogenase]-L-cysteine + H2O
a [glyceraldehyde-3-phosphate dehydrogenase]-L-cysteine + (R)-lactate
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
-
-
?
an S-(1-hydroxy-2-oxopropyl)-[glyceraldehyde-3-phosphate dehydrogenase]-L-cysteine + H2O
a [glyceraldehyde-3-phosphate dehydrogenase]-L-cysteine + (R)-lactate
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
-
-
?
an S-(1-hydroxy-2-oxopropyl)-[protein]-L-arginine + H2O
a [protein]-L-arginine + (R)-lactate
-
-
-
?
an S-(1-hydroxy-2-oxopropyl)-[protein]-L-arginine + H2O
a [protein]-L-arginine + (R)-lactate
-
-
-
?
an S-(1-hydroxy-2-oxopropyl)-[protein]-L-cysteine + H2O
a [protein]-L-cysteine + (R)-lactate
-
-
-
?
an S-(1-hydroxy-2-oxopropyl)-[protein]-L-cysteine + H2O
a [protein]-L-cysteine + (R)-lactate
-
-
-
?
an S-(1-hydroxy-2-oxopropyl)-[protein]-L-lysine + H2O
a [protein]-L-lysine + (R)-lactate
-
-
-
?
an S-(1-hydroxy-2-oxopropyl)-[protein]-L-lysine + H2O
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
evolution
Hsp31 is a member of the PfpI/Hsp31/DJ-1 superfamily whose members possess a conserved exposed cysteine involved in environmental stress resistance
malfunction
bacterial extracts from a hchA mutant display increased glycation levels and the apparent glyoxylase activity of Hsp31 reflects its deglycase activity
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
evolution
enzyme YajL belongs to the PfpI/Hsp31/DJ-1 superfamily
evolution
enzyme YhbO belongs to the PfpI/Hsp31/DJ-1 superfamily
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
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
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
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%
physiological function
the enzyme prevents acrylamide formation in vivo, acrylamide formation in the glyoxal/asparagine mixture is reduced by 78% by YhbO
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Mihoub, M.; Abdallah, J.; Gontero, B.; Dairou, J.; Richarme, G.
The DJ-1 superfamily member Hsp31 repairs proteins from glycation by methylglyoxal and glyoxal
Biochem. Biophys. Res. Commun.
463
1305-1310
2015
Escherichia coli (P31658)
brenda
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
Biochem. Biophys. Res. Commun.
470
282-286
2016
Escherichia coli (P45470), Escherichia coli (Q46948), Escherichia coli
brenda
Richarme, G.; Marguet, E.; Forterre, P.; Ishino, S.; Ishino, Y.
DJ-1 family Maillard deglycases prevent acrylamide formation
Biochem. Biophys. Res. Commun.
478
1111-1116
2016
Escherichia coli (P45470), Pyrococcus furiosus (Q51732), Pyrococcus furiosus, Homo sapiens (Q99497)
brenda