Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.5.1.124 extracted from

  • 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 (2015), J. Biol. Chem., 290, 1885-1897.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.5.1.124

Protein Variants

Protein Variants Comment Organism
C106S site-directed mutagenesis, inactive mutant Homo sapiens
C46S site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme Homo sapiens
C53S site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information biphasic kinetics for aminocarbinol degradation, overview Homo sapiens
0.32
-
 S-(1-hydroxy-2-oxopropyl)-N-acetyl-L-cysteine pH 7.0, 22°C Homo sapiens
0.35
-
 N6-(1-hydroxy-2-oxopropyl)-N2-acetyl-L-lysine pH 7.0, 22°C Homo sapiens
0.44
-
 Nomega-(1-hydroxy-2-oxopropyl)-Nalpha-acetyl-L-arginine pH 7.0, 22°C Homo sapiens

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 Homo sapiens
-
 a [protein]-L-arginine + (R)-lactate
-
 ?
an S-(1-hydroxy-2-oxopropyl)-[protein]-L-cysteine + H2O Homo sapiens
-
 a [protein]-L-cysteine + (R)-lactate
-
 ?
an S-(1-hydroxy-2-oxopropyl)-[protein]-L-lysine + H2O Homo sapiens
-
 a [protein]-L-lysine + (R)-lactate
-
 ?
additional information Homo sapiens glyoxalase activity of DJ-1 reflects its deglycase activity ?
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens Q99497
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
an S-(1-hydroxy-2-oxopropyl)-[aspartate aminotransferase]-L-lysine + H2O
-
 Homo sapiens a [aspartate aminotransferase]-L-lysine + (R)-lactate
-
 ?
an S-(1-hydroxy-2-oxopropyl)-[fructose-1,6-biphosphate aldolase]-L-arginine + H2O
-
 Homo sapiens a [fructose-1,6-biphosphate aldolase]-L-arginine + (R)-lactate
-
 ?
an S-(1-hydroxy-2-oxopropyl)-[fructose-1,6-biphosphate aldolase]-L-lysine + H2O
-
 Homo sapiens a [fructose-1,6-biphosphate aldolase]-L-lysine + (R)-lactate
-
 ?
an S-(1-hydroxy-2-oxopropyl)-[protein]-L-arginine + H2O
-
 Homo sapiens a [protein]-L-arginine + (R)-lactate
-
 ?
an S-(1-hydroxy-2-oxopropyl)-[protein]-L-cysteine + H2O
-
 Homo sapiens a [protein]-L-cysteine + (R)-lactate
-
 ?
an S-(1-hydroxy-2-oxopropyl)-[protein]-L-lysine + H2O
-
 Homo sapiens a [protein]-L-lysine + (R)-lactate
-
 ?
an S-(1-hydroxy-2-oxopropyl)-[protein]-N-acetyl-L-arginine + H2O
-
 Homo sapiens a [protein]-L-arginine + (R)-lactate
-
 ?
an S-(1-hydroxy-2-oxopropyl)-[protein]-N-acetyl-L-cysteine + H2O
-
 Homo sapiens a [protein]-L-cysteine + (R)-lactate
-
 ?
an S-(1-hydroxy-2-oxopropyl)-[protein]-N-acetyl-L-lysine + H2O
-
 Homo sapiens a [protein]-L-lysine + (R)-lactate
-
 ?
additional information glyoxalase activity of DJ-1 reflects its deglycase activity Homo sapiens ?
-
 ?
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) Homo sapiens ?
-
 ?
N6-(1-hydroxy-2-oxopropyl)-N2-acetyl-L-lysine + H2O
-
 Homo sapiens N-acetyl-L-lysine + (R)-lactate
-
 ?
Nomega-(1-hydroxy-2-oxopropyl)-Nalpha-acetyl-L-arginine + H2O
-
 Homo sapiens Nalpha-acetyl-L-arginine + (R)-lactate
-
 ?
S-(1-hydroxy-2-oxopropyl)-N-acetyl-L-cysteine + H2O
-
 Homo sapiens N-acetyl-L-cysteine + (R)-lactate
-
 ?
S-(1-hydroxy-2-oxopropyl)-[bovine serum albumin]-N-acetyl-L-cysteine + H2O
-
 Homo sapiens [bovine serum albumin]-L-cysteine + (R)-lactate
-
 ?

Synonyms

Synonyms Comment Organism
DJ-1
-
 Homo sapiens
PARK7
-
 Homo sapiens
Parkinsonism-associated protein
-
 Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
22
-
 assay at Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.27
-
 Nomega-(1-hydroxy-2-oxopropyl)-Nalpha-acetyl-L-arginine pH 7.0, 22°C Homo sapiens
0.28
-
 N6-(1-hydroxy-2-oxopropyl)-N2-acetyl-L-lysine pH 7.0, 22°C Homo sapiens
0.42
-
 S-(1-hydroxy-2-oxopropyl)-N-acetyl-L-cysteine pH 7.0, 22°C Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
 assay at Homo sapiens

General Information

General Information Comment Organism
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 Homo sapiens