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 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 | 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 | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | Q99497 | - |
- |
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 | Comment | Organism |
---|---|---|
DJ-1 | - |
Homo sapiens |
PARK7 | - |
Homo sapiens |
Parkinsonism-associated protein | - |
Homo sapiens |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
22 | - |
assay at | Homo sapiens |
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 Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
assay at | Homo sapiens |
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 |