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Information on EC 3.5.1.124 - protein deglycase and Organism(s) Homo sapiens and UniProt Accession Q99497

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EC Tree
     3 Hydrolases
         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
             3.5.1 In linear amides
                3.5.1.124 protein deglycase
IUBMB 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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This record set is specific for:
Homo sapiens
UNIPROT: Q99497
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Word Map
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The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
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an Nomega-(1-hydroxy-2-oxopropyl)-[protein]-L-arginine
+
H2O
=
a [protein]-L-arginine
+
lactate
an Nomega-(1-hydroxy-2-oxopropyl)-[protein]-L-arginine
+
=
+
an N6-(1-hydroxy-2-oxopropyl)-[protein]-L-lysine
+
H2O
=
a [protein]-L-lysine
+
lactate
an N6-(1-hydroxy-2-oxopropyl)-[protein]-L-lysine
+
=
a [protein]-L-lysine
+
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
+
=
a [protein]-L-cysteine
+
Synonyms
glyoxalase, park7, dj-1 protein, deglycase, protein deglycase, parkinsonism-associated protein dj-1, dj-1 deglycase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
DJ-1 deglycase
-
glutathione-independent glyoxalase
-
Maillard deglycase
-
Parkinsonism-associated protein
-
Parkinsonism-associated protein DJ-1
-
DJ-1 protein
-
-
-
-
PARK7
-
-
-
-
yajL
-
-
-
-
yhbO
-
-
-
-
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].
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
an S-(1-hydroxy-2-oxopropyl)-[aspartate aminotransferase]-L-lysine + H2O
a [aspartate aminotransferase]-L-lysine + (R)-lactate
show the reaction diagram
-
-
-
?
an S-(1-hydroxy-2-oxopropyl)-[fructose-1,6-biphosphate aldolase]-L-arginine + H2O
a [fructose-1,6-biphosphate aldolase]-L-arginine + (R)-lactate
show the reaction diagram
-
-
-
?
an S-(1-hydroxy-2-oxopropyl)-[fructose-1,6-biphosphate aldolase]-L-lysine + H2O
a [fructose-1,6-biphosphate aldolase]-L-lysine + (R)-lactate
show the reaction diagram
-
-
-
?
an S-(1-hydroxy-2-oxopropyl)-[protein]-L-arginine + H2O
a [protein]-L-arginine + (R)-lactate
show the reaction diagram
an S-(1-hydroxy-2-oxopropyl)-[protein]-L-cysteine + H2O
a [protein]-L-cysteine + (R)-lactate
show the reaction diagram
an S-(1-hydroxy-2-oxopropyl)-[protein]-L-lysine + H2O
a [protein]-L-lysine + (R)-lactate
show the reaction diagram
an S-(1-hydroxy-2-oxopropyl)-[protein]-N-acetyl-L-arginine + H2O
a [protein]-L-arginine + (R)-lactate
show the reaction diagram
-
-
-
?
an S-(1-hydroxy-2-oxopropyl)-[protein]-N-acetyl-L-cysteine + H2O
a [protein]-L-cysteine + (R)-lactate
show the reaction diagram
-
-
-
?
an S-(1-hydroxy-2-oxopropyl)-[protein]-N-acetyl-L-lysine + H2O
a [protein]-L-lysine + (R)-lactate
show the reaction diagram
-
-
-
?
N6-(1-hydroxy-2-oxopropyl)-N2-acetyl-L-lysine + H2O
N-acetyl-L-lysine + (R)-lactate
show the reaction diagram
-
-
-
?
N6-(1-hydroxy-2-oxopropyl)-[alpha-synuclein]-L-lysine + H2O
[alpha-synuclein]-L-lysine + lactate
show the reaction diagram
-
-
-
?
Nomega-(1-hydroxy-2-oxopropyl)-Nalpha-acetyl-L-arginine + H2O
Nalpha-acetyl-L-arginine + (R)-lactate
show the reaction diagram
-
-
-
?
S-(1-hydroxy-2-oxopropyl)-N-acetyl-L-cysteine + H2O
N-acetyl-L-cysteine + (R)-lactate
show the reaction diagram
S-(1-hydroxy-2-oxopropyl)-[bovine serum albumin]-N-acetyl-L-cysteine + H2O
[bovine serum albumin]-L-cysteine + (R)-lactate
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
an S-(1-hydroxy-2-oxopropyl)-[protein]-L-arginine + H2O
a [protein]-L-arginine + (R)-lactate
show the reaction diagram
an S-(1-hydroxy-2-oxopropyl)-[protein]-L-cysteine + H2O
a [protein]-L-cysteine + (R)-lactate
show the reaction diagram
an S-(1-hydroxy-2-oxopropyl)-[protein]-L-lysine + H2O
a [protein]-L-lysine + (R)-lactate
show the reaction diagram
additional information
?
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.35
N6-(1-hydroxy-2-oxopropyl)-N2-acetyl-L-lysine
pH 7.0, 22°C
0.44
Nomega-(1-hydroxy-2-oxopropyl)-Nalpha-acetyl-L-arginine
pH 7.0, 22°C
0.32
S-(1-hydroxy-2-oxopropyl)-N-acetyl-L-cysteine
pH 7.0, 22°C
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.28
N6-(1-hydroxy-2-oxopropyl)-N2-acetyl-L-lysine
pH 7.0, 22°C
0.27
Nomega-(1-hydroxy-2-oxopropyl)-Nalpha-acetyl-L-arginine
pH 7.0, 22°C
0.42
S-(1-hydroxy-2-oxopropyl)-N-acetyl-L-cysteine
pH 7.0, 22°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
assay at
30
assay at
55
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55 - 95
enzyme activity is reduced by 74% for DJ-1 at 70°C, DJ-1 is inactive at 95°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PARK7_HUMAN
189
0
19891
Swiss-Prot
other Location (Reliability: 2)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C106S
site-directed mutagenesis, inactive mutant
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant soluble and active enzyme from Escherichia coli by anion exchange and hydroxy apatite chromatography followed by dialysis
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
recombinant expression in Escherichia coli from pET21a-DJ-1 plasmid
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team