3.5.1.124: protein deglycase
This is an abbreviated version!
For detailed information about protein deglycase, go to the full flat file.
Word Map on EC 3.5.1.124
-
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
- 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
Reaction
Synonyms
deglycase, DJ-1, DJ-1 deglycase, DJ-1 protein, glutathione-independent glyoxalase, glyoxalase, glyoxylase III, hchA, Hsp31, Maillard deglycase, More, PARK7, Parkinsonism-associated protein, Parkinsonism-associated protein DJ-1, PfpI, yajL, yhbO
ECTree
3.5.1.124 protein deglycaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 3.5.1.124 - protein deglycase
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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
-
-
?
