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Information on EC 3.5.1.124 - protein deglycase
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EC Tree
3.5.1.124 protein deglycaseIUBMB Comments
The enzyme, previously thought to be a glyoxalase, acts on glycated L-arginine, L-lysine, and L-cysteine residues within proteins that have been attacked and modified by glyoxal or 2-oxopropanal. The attack forms hemithioacetal in the case of cysteines and aminocarbinols in the case of arginines and lysines. The enzyme repairs the amino acids, releasing glycolate or lactate (70-80% (S)-lactate and 20-30% (R)-lactate), depending on whether the attacking agent was glyoxal or 2-oxopropanal, respectively [3,4].
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Word Map
- 3.5.1.124
- methylglyoxal
- gsh
-
detoxify
- neurodegenerative
- d-lactate
-
dicarbonyls
- ascorbate
- dismutase
- seedlings
-
dopaminergic
- chlorophyll
-
neuroprotective
-
non-enzymatic
- alzheimer
-
early-onset
- mellitus
- malondialdehyde
-
substantia
-
mg-induced
- dehydroascorbate
- pink1
-
endproducts
- lipoxygenase
- rage
- monodehydroascorbate
-
ascorbate-glutathione
-
d-lactic
- mdhar
-
glutathione-dependent
- hemithioacetal
- s-d-lactoylglutathione
-
sh-sy5y
-
pd-related
- properdin
- phytochelatins
-
atp13a2
- diagnostics
- alpha-synuclein
-
pd-associated
-
anti-glycation
-
gsh-dependent
-
asa-gsh
- trypanothione
- drug development
- aminoguanidine
-
methylglyoxal-induced
-
deglycation
-
hyperglycaemia
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
an Nomega-(1-hydroxy-2-oxopropyl)-[protein]-L-arginine
+
=
+
an N6-(1-hydroxy-2-oxopropyl)-[protein]-L-lysine
+
=
a [protein]-L-lysine
+
an S-(1-hydroxy-2-oxopropyl)-[protein]-L-cysteine
+
=
a [protein]-L-cysteine
+
Synonyms
glyoxalase, park7, dj-1 protein, deglycase, protein deglycase, parkinsonism-associated protein dj-1, dj-1 deglycase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
deglycase
DJ-1
DJ-1 protein
-
-
-
-
glutathione-independent glyoxalase
glyoxylase III
-
-
incorrect
-
Hsp31
Maillard deglycase
PARK7
yajL
yhbO
additional information
PARK7
-
-
-
-
yajL
-
-
-
-
yhbO
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
an Nomega-(1-hydroxy-2-oxopropyl)-[protein]-L-arginine + H2O = a [protein]-L-arginine + lactate
(1)
-
-
-
an S-(1-hydroxy-2-oxopropyl)-[protein]-L-cysteine + H2O = a [protein]-L-cysteine + (R)-lactate
(3)
-
-
-
an N6-(1-hydroxy-2-oxopropyl)-[protein]-L-lysine + H2O = a [protein]-L-lysine + lactate
(2)
-
-
-
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
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SYSTEMATIC NAME
IUBMB Comments
a [protein]-L-amino acid-1-hydroxypropan-2-one hydrolase [(R)-lactate-forming]
The enzyme, previously thought to be a glyoxalase, acts on glycated L-arginine, L-lysine, and L-cysteine residues within proteins that have been attacked and modified by glyoxal or 2-oxopropanal. The attack forms hemithioacetal in the case of cysteines and aminocarbinols in the case of arginines and lysines. The enzyme repairs the amino acids, releasing glycolate or lactate (70-80% (S)-lactate and 20-30% (R)-lactate), depending on whether the attacking agent was glyoxal or 2-oxopropanal, respectively [3,4].
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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-amino acid + H2O
a [bovine serum albumin]-L-amino acid + (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)-[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]-N-acetyl-L-arginine + H2O
a [protein]-L-arginine + (R)-lactate
-
-
-
?
an S-(1-hydroxy-2-oxopropyl)-[protein]-N-acetyl-L-cysteine + H2O
a [protein]-L-cysteine + (R)-lactate
-
-
-
?
an S-(1-hydroxy-2-oxopropyl)-[protein]-N-acetyl-L-lysine + H2O
a [protein]-L-lysine + (R)-lactate
-
-
-
?
N6-(1-hydroxy-2-oxopropyl)-N2-acetyl-L-lysine + H2O
N-acetyl-L-lysine + (R)-lactate
-
-
-
?
N6-(1-hydroxy-2-oxopropyl)-[alpha-synuclein]-L-lysine + H2O
[alpha-synuclein]-L-lysine + lactate
-
-
-
?
Nomega-(1-hydroxy-2-oxopropyl)-Nalpha-acetyl-L-arginine + H2O
Nalpha-acetyl-L-arginine + (R)-lactate
-
-
-
?
S-(1-hydroxy-2-oxopropyl)-[bovine serum albumin]-N-acetyl-L-cysteine + H2O
[bovine serum albumin]-L-cysteine + (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)-[aspartate aminotransferase]-L-lysine + H2O
a [aspartate aminotransferase]-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-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-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)-[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)-[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
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-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-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-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-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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
methylglyoxal + H2O
(R)-lactate
the enzyme also shows aminopeptidase activity and protease activity
-
-
?
methylglyoxal + H2O
(R)-lactate
the enzyme also shows aminopeptidase activity and protease activity
-
-
?
S-(1-hydroxy-2-oxopropyl)-N-acetyl-L-cysteine + H2O
N-acetyl-L-cysteine + (R)-lactate
-
-
-
?
S-(1-hydroxy-2-oxopropyl)-N-acetyl-L-cysteine + H2O
N-acetyl-L-cysteine + (R)-lactate
-
-
-
?
S-(1-hydroxy-2-oxopropyl)-N-acetyl-L-cysteine + H2O
N-acetyl-L-cysteine + (R)-lactate
after spontaneous hemithioacetal formation, hemithioacetal degradation results in the quantitative formation of D-lactate via migration catalyzed by DJ-1 and thioester hydrolysis by DJ-1
-
-
?
additional information
?
-
-
neither His-tagged hDJ-1, nor untagged hDJ-1 show any deglycase activity in vitro, cysteine deglycase activity of enzyme DJ-1 is due to a buffer artifact, which can be attributed to TRIS buffer
-
-
?
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
-
-
?
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
?
-
glyoxalase activity of DJ-1 reflects its deglycase activity
-
-
?
additional information
?
-
-
glyoxalase activity of DJ-1 reflects its deglycase activity
-
-
?
additional information
?
-
DJ-1, by displacing the imidazolidine-aminocarbinol equilibrium, allows indirect degradation of imidazolidine intermediates before they convert into irreversible advanced glycation end products, such as N-(5-hydro-5-methyl-4-imidazolon-2-yl)ornithine (MG-H1). In contrast with its ability to prevent Schiff base formation, DJ-1 does not degrade Schiff bases, DJ-1 is unable to deglycate Schiff bases. The enzyme DJ-1 prevents glycation of Arg22, Lys28, Lys42, Arg43, Lys111, Cys202, Lys208, Lys230, Lys243, Arg259, Cys290, Lys318, Lys330, Arg331, Cys339, and Lys342 in rabbit muscle fructose-1,6-biphosphate aldolase. Residues Lys42, Arg43, and Lys230 are located in the active site, with Lys42 and Arg43 being involved in substrate binding (mutation of Arg43 results in 14fold decrease in activity) and Lys230 forming a Schiff base with the substrate (mutation of Lys230 results in complete loss of activity)
-
-
?
additional information
?
-
-
DJ-1, by displacing the imidazolidine-aminocarbinol equilibrium, allows indirect degradation of imidazolidine intermediates before they convert into irreversible advanced glycation end products, such as N-(5-hydro-5-methyl-4-imidazolon-2-yl)ornithine (MG-H1). In contrast with its ability to prevent Schiff base formation, DJ-1 does not degrade Schiff bases, DJ-1 is unable to deglycate Schiff bases. The enzyme DJ-1 prevents glycation of Arg22, Lys28, Lys42, Arg43, Lys111, Cys202, Lys208, Lys230, Lys243, Arg259, Cys290, Lys318, Lys330, Arg331, Cys339, and Lys342 in rabbit muscle fructose-1,6-biphosphate aldolase. Residues Lys42, Arg43, and Lys230 are located in the active site, with Lys42 and Arg43 being involved in substrate binding (mutation of Arg43 results in 14fold decrease in activity) and Lys230 forming a Schiff base with the substrate (mutation of Lys230 results in complete loss of activity)
-
-
?
additional information
?
-
the enzyme DJ-1 also shows glyoxalase III activity, cf. EC 4.2.1.130, which is representative of its deglycase activity
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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-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-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-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
-
-
-
?
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
?
-
glyoxalase activity of DJ-1 reflects its deglycase activity
-
-
?
additional information
?
-
-
glyoxalase activity of DJ-1 reflects its deglycase activity
-
-
?
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.44
Nomega-(1-hydroxy-2-oxopropyl)-Nalpha-acetyl-L-arginine
pH 7.0, 22°C
additional information
additional information
biphasic kinetics for aminocarbinol degradation, overview
-
additional information
additional information
-
biphasic kinetics for aminocarbinol degradation, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.27
Nomega-(1-hydroxy-2-oxopropyl)-Nalpha-acetyl-L-arginine
pH 7.0, 22°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
70
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
55 - 95
55 - 95
enzyme activity is reduced by 72% for YhbO 70°C, YhbO is inactive at 95°C
55 - 95
enzyme activity is reduced by 74% for DJ-1 at 70°C, DJ-1 is inactive at 95°C
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
physiological function
evolution
enzyme YajL belongs to the PfpI/Hsp31/DJ-1 superfamily
evolution
enzyme YhbO belongs to the PfpI/Hsp31/DJ-1 superfamily
evolution
Hsp31 is a member of the PfpI/Hsp31/DJ-1 superfamily whose members possess a conserved exposed cysteine involved in environmental stress resistance
evolution
the enzyme PfpI belongs to the PfpI/Hsp31/DJ-1 superfamily
malfunction
bacterial extracts from a hchA mutant display increased glycation levels and the apparent glyoxylase activity of Hsp31 reflects its deglycase activity
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
malfunction
-
methylglyoxal causes formation of advanced glycation end-products on proteins, one of which is Nepsilon-carboxymethyllysine (CEL), which can be detected by immunoblotting whole cell lysates. Control S2 cells show little to no increase in CEL adducts when treated with 1 mM methylglyoxal. They are capable of efficiently detoxifying methylglyoxal. Knockdown of glyoxalase Glo1 causes a detectable impairment of methylglyoxal detoxification activity in vivo, since CEL adducts are clearly increased upon treatment with 1 mM methylglyoxal. In contrast, DJ-1 knockdown causes no detectable increase in CEL adducts compared with control cells, and combined knockdown of DJ-1beta and Glo1 shows no additional phenotype compared with Glo1 knockdown alone
malfunction
protein glycation levels are 2 to 10fold increased in deglycase-depleted cells, and deglycase mutants display up to 500fold loss of viability in methylglyoxal or glucose-containing media. Both DJ-1- and glyoxalase-deficient cells display 4-fold increases in protein glycation levels, especially in unstressed cells
malfunction
reduced DJ-1 activity due to mutations or oxidative stress may lead to the accumulation of glycated alpha-synuclein and its aggregates
physiological function
deglycases play important roles in protecting cells against electrophile and carbonyl stress. Deglycases prevent acrylamide formation, likely by degrading Maillard adducts responsible for its formation, they prevent glycation by depleting methylglyoxal pools
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
physiological function
protein glycation is a nonenzymatic covalent reaction between proteins and carbonyl groups resulting in protein denaturation. Enzyme DJ-1 is a protein deglycase that repairs proteins from glycation by glyoxals, which constitutes most glycation damage. DJ-1-associated Parkinsonism results from excessive protein glycation and DJ-1 is a major antiglycation and anti-aging protein. Residue Cys106 is the nucleophile crucial for the deglycase activity of DJ-1. The enzyme DJ-1 prevents glycation of Arg22, Lys28, Lys42, Arg43, Lys111, Cys202, Lys208, Lys230, Lys243, Arg259, Cys290, Lys318, Lys330, Arg331, Cys339, and Lys342 in rabbit muscle fructose-1,6-biphosphate aldolase. Residues Lys42, Arg43, and Lys230 are located in the active site, with Lys42 and Arg43 being involved in substrate binding (mutation of Arg43 results in 14fold decrease in activity) and Lys230 forming a Schiff base with the substrate (mutation of Lys230 results in complete loss of activity). Aspartate aminotransferase activity is decreased by 20-90% by 1-5 mM methylglyoxal at 37°C, addition of 0.002 mM DJ-1, 30 min after the addition of methylglyoxal, rapidly restores (in 2 min) up to 90-100% of aspartate aminotransferase activity following 1-2 mM methylglyoxal stress and up to 60% after 5 mM methylglyoxal stress. DJ-1 affords full protection against glycation by 2 mM methylglyoxal
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 72% by PfpI
physiological function
the enzyme prevents acrylamide formation in vivo, acrylamide formation in the glyoxal/asparagine mixture is reduced by 78% by YhbO
physiological function
the enzyme prevents acrylamide formation in vivo, acrylamide formation in the glyoxal/asparagine mixture is reduced by 98% by DJ-1
physiological function
-
using both DJ-1 knockdown in Drosophila cells in culture, and DJ-1beta knock-out flies, no contribution of DJ-1 to survival to methylglyoxal challenge or to accumulation of methylglyoxal protein adducts can be detected
physiological function
by degrading Maillard adducts formed between carbonyls and thiols or amino groups, the DJ-1 family Maillard deglycases prevent the formation of the advanced glycation end products (AGEs) that arise from Maillard adducts after dehydrations, oxidations and rearrangements. Since glycation is involved in ageing, cancer, atherosclerosis and cataracts, as well as post-diabetic, neurovegetatives and renal and autoimmune diseases, the DJ-1 deglycases are likely to play an important role in preventing these diseases. These deglycases, especially those from thermophilic organisms, may also be used to prevent the formation of dietary AGEs during food processing, sterilization and storage. They prevent acrylamide formation in food, likely by degrading the asparagine/glyoxal Maillard adducts responsible for its formation. Since Maillard adducts are the substrates of the DJ-1 family deglycases
physiological function
the deglycase activity of DJ-1 mitigates alpha-synuclein glycation and aggregation in dopaminergic cells
Show AA Sequence and Transmembrane Helices (2224 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
dimer
VcHsp31 acquires two (type-I and type-II) dimeric forms. Type-I dimer is similar to EcHsp31 where two VcHsp31 monomers associate in eclipsed manner through several intersubunit hydrogen bonds involving their P-domains. Type-II dimer is a dimeric organization, where some of the intersubunit hydrogen bonds are abrogated and each monomer swings out in the opposite directions centering at their P-domains, like twisting of wet cloth. Normal mode analysis (NMA) of type-I dimer shows similar movement of the individual monomers. Upon swinging, a dimeric surface of 400 A2, mostly hydrophobic in nature, is uncovered which might bind partially unfolded protein substrates. It is proposed that, in solution, VcHsp31 remains as an equilibrium mixture of both the dimers. With increase in temperature, transformation to type-II form having more exposed hydrophobic surface, occurs progressively accounting for the temperature dependent increase of chaperone activity of VcHsp31
dimer
-
VcHsp31 acquires two (type-I and type-II) dimeric forms. Type-I dimer is similar to EcHsp31 where two VcHsp31 monomers associate in eclipsed manner through several intersubunit hydrogen bonds involving their P-domains. Type-II dimer is a dimeric organization, where some of the intersubunit hydrogen bonds are abrogated and each monomer swings out in the opposite directions centering at their P-domains, like twisting of wet cloth. Normal mode analysis (NMA) of type-I dimer shows similar movement of the individual monomers. Upon swinging, a dimeric surface of 400 A2, mostly hydrophobic in nature, is uncovered which might bind partially unfolded protein substrates. It is proposed that, in solution, VcHsp31 remains as an equilibrium mixture of both the dimers. With increase in temperature, transformation to type-II form having more exposed hydrophobic surface, occurs progressively accounting for the temperature dependent increase of chaperone activity of VcHsp31
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals of VcHsp31 and its mutants are grown by hanging drop vapor diffusion method at different temperatures, from 18°C-25°C
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C46S
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
C53S
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
H158A
reduced amidopeptidase activity, glyoxalase activity is 53% compared to wild-type enzyme
Y224A
H158A
-
reduced amidopeptidase activity, glyoxalase activity is 53% compared to wild-type enzyme
-
additional information
additional information
-
construction of DJ-1 knockdown in Drosophila cells in culture, and DJ-1beta knock-out flies. DJ-1beta knockdown does not affect the response of S2 cells to methylglyoxal challenge
additional information
construction of yhbO/yajL and yhbO/yajL/hchA mutants displaying high amounts of glycated proteins
additional information
construction of yhbO/yajL and yhbO/yajL/hchA mutants displaying high amounts of glycated proteins
additional information
-
construction of yhbO/yajL and yhbO/yajL/hchA mutants displaying high amounts of glycated proteins
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant soluble and active enzyme from Escherichia coli by anion exchange and hydroxy apatite chromatography followed by dialysis
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloned in pET28a+ vector, overexpressed in Escherichia coli BL21 (DE3) cells as N-terminus 6×His tagged fusion protein
DJ-1 gene is subcloned from pLenti6-DJ-1-V5-WT plasmid into the pRetroX-Tight-Puro Advanced vector. The confirmed clone is transfected into HEK-293 cells
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
stress-inducible enzyme
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
secreted DJ-1 levels in serum and DJ-1-binding compounds will be a diagnostic biomarker and therapeutic drug for neurodegenerative diseases
drug development
secreted DJ-1 levels in serum and DJ-1-binding compounds will be a diagnostic biomarker and therapeutic drug for neurodegenerative diseases
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Richarme, G.; Dairou, J.
Parkinsonism-associated protein DJ-1 is a bona fide deglycase
Biochem. Biophys. Res. Commun.
483
387-391
2017
Homo sapiens (Q99497)
brenda
Richarme, G.; Mihoub, M.; Dairou, J.; Bui, L.C.; Leger, T.; Lamouri, A.
Parkinsonism-associated protein DJ-1/Park7 is a major protein deglycase that repairs methylglyoxal- and glyoxal-glycated cysteine, arginine, and lysine residues
J. Biol. Chem.
290
1885-1897
2015
Homo sapiens (Q99497), Homo sapiens
brenda
Pfaff, D.H.; Fleming, T.; Nawroth, P.; Teleman, A.A.
Evidence against a role for the Parkinsonism-associated protein DJ-1 in methylglyoxal detoxification
J. Biol. Chem.
292
685-690
2017
Drosophila melanogaster
brenda
Mihoub, M.; Abdallah, J.; Richarme, G.
Protein repair from glycation by glyoxals by the DJ-1 family Maillard deglycases
Adv. Exp. Med. Biol.
1037
133-147
2017
Homo sapiens (Q99497)
brenda
Sharma, N.; Rao, S.P.; Kalivendi, S.V.
The deglycase activity of DJ-1 mitigates alpha-synuclein glycation and aggregation in dopaminergic cells Role of oxidative stress mediated downregulation of DJ-1 in Parkinsons disease
Free Radic. Biol. Med.
135
28-37
2019
Homo sapiens (Q99497)
brenda
Das, S.; Roy Chowdhury, S.; Dey, S.; Sen, U.
Structural and biochemical studies on Vibrio cholerae Hsp31 reveals a novel dimeric form and glutathione-independent glyoxalase activity
PLoS ONE
12
e0172629
2017
Vibrio cholerae (A0A0H3AFW5), Vibrio cholerae O395 (A0A0H3AFW5)
brenda
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