3.5.1.124 an S-(1-hydroxy-2-oxopropyl)-[aspartate aminotransferase]-L-arginine + H2O - Escherichia coli a [aspartate aminotransferase]-L-arginine + (R)-lactate - ? 439119 3.5.1.124 an S-(1-hydroxy-2-oxopropyl)-[aspartate aminotransferase]-L-lysine + H2O - Homo sapiens a [aspartate aminotransferase]-L-lysine + (R)-lactate - ? 439120 3.5.1.124 an S-(1-hydroxy-2-oxopropyl)-[aspartate aminotransferase]-L-lysine + H2O - Escherichia coli a [aspartate aminotransferase]-L-lysine + (R)-lactate - ? 439120 3.5.1.124 an S-(1-hydroxy-2-oxopropyl)-[bovine serum albumin]-L-amino acid + H2O - Escherichia coli a [bovine serum albumin]-L-amino acid + (R)-lactate - ? 439121 3.5.1.124 an S-(1-hydroxy-2-oxopropyl)-[bovine serum albumin]-L-lysine + H2O - Escherichia coli a [bovine serum albumin]-L-lysine + (R)-lactate - ? 439122 3.5.1.124 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 - ? 439123 3.5.1.124 an S-(1-hydroxy-2-oxopropyl)-[fructose-1,6-biphosphate aldolase]-L-arginine + H2O - Escherichia coli a [fructose-1,6-biphosphate aldolase]-L-arginine + (R)-lactate - ? 439123 3.5.1.124 an S-(1-hydroxy-2-oxopropyl)-[fructose-1,6-biphosphate aldolase]-L-arginine + H2O 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 Escherichia coli a [fructose-1,6-biphosphate aldolase]-L-arginine + (R)-lactate - ? 439123 3.5.1.124 an S-(1-hydroxy-2-oxopropyl)-[fructose-1,6-biphosphate aldolase]-L-arginine + H2O 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 Escherichia coli a [fructose-1,6-biphosphate aldolase]-L-arginine + (R)-lactate - ? 439123 3.5.1.124 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 - ? 439124 3.5.1.124 an S-(1-hydroxy-2-oxopropyl)-[fructose-1,6-biphosphate aldolase]-L-lysine + H2O - Escherichia coli a [fructose-1,6-biphosphate aldolase]-L-lysine + (R)-lactate - ? 439124 3.5.1.124 an S-(1-hydroxy-2-oxopropyl)-[fructose-1,6-biphosphate aldolase]-L-lysine + H2O 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 Escherichia coli a [fructose-1,6-biphosphate aldolase]-L-lysine + (R)-lactate - ? 439124 3.5.1.124 an S-(1-hydroxy-2-oxopropyl)-[fructose-1,6-biphosphate aldolase]-L-lysine + H2O 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 Escherichia coli a [fructose-1,6-biphosphate aldolase]-L-lysine + (R)-lactate - ? 439124 3.5.1.124 an S-(1-hydroxy-2-oxopropyl)-[glyceraldehyde-3-phosphate dehydrogenase]-L-cysteine + H2O 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 Escherichia coli a [glyceraldehyde-3-phosphate dehydrogenase]-L-cysteine + (R)-lactate - ? 439125 3.5.1.124 an S-(1-hydroxy-2-oxopropyl)-[glyceraldehyde-3-phosphate dehydrogenase]-L-cysteine + H2O 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 Escherichia coli a [glyceraldehyde-3-phosphate dehydrogenase]-L-cysteine + (R)-lactate - ? 439125 3.5.1.124 an S-(1-hydroxy-2-oxopropyl)-[protein]-L-arginine + H2O - Pyrococcus furiosus a [protein]-L-arginine + (R)-lactate - ? 438189 3.5.1.124 an S-(1-hydroxy-2-oxopropyl)-[protein]-L-arginine + H2O - Homo sapiens a [protein]-L-arginine + (R)-lactate - ? 438189 3.5.1.124 an S-(1-hydroxy-2-oxopropyl)-[protein]-L-arginine + H2O - Escherichia coli a [protein]-L-arginine + (R)-lactate - ? 438189 3.5.1.124 an S-(1-hydroxy-2-oxopropyl)-[protein]-L-cysteine + H2O - Pyrococcus furiosus a [protein]-L-cysteine + (R)-lactate - ? 438190 3.5.1.124 an S-(1-hydroxy-2-oxopropyl)-[protein]-L-cysteine + H2O - Homo sapiens a [protein]-L-cysteine + (R)-lactate - ? 438190 3.5.1.124 an S-(1-hydroxy-2-oxopropyl)-[protein]-L-cysteine + H2O - Escherichia coli a [protein]-L-cysteine + (R)-lactate - ? 438190 3.5.1.124 an S-(1-hydroxy-2-oxopropyl)-[protein]-L-lysine + H2O - Pyrococcus furiosus a [protein]-L-lysine + (R)-lactate - ? 438191 3.5.1.124 an S-(1-hydroxy-2-oxopropyl)-[protein]-L-lysine + H2O - Homo sapiens a [protein]-L-lysine + (R)-lactate - ? 438191 3.5.1.124 an S-(1-hydroxy-2-oxopropyl)-[protein]-L-lysine + H2O - Escherichia coli a [protein]-L-lysine + (R)-lactate - ? 438191 3.5.1.124 an S-(1-hydroxy-2-oxopropyl)-[protein]-N-acetyl-L-arginine + H2O - Homo sapiens a [protein]-L-arginine + (R)-lactate - ? 439126 3.5.1.124 an S-(1-hydroxy-2-oxopropyl)-[protein]-N-acetyl-L-cysteine + H2O - Homo sapiens a [protein]-L-cysteine + (R)-lactate - ? 439127 3.5.1.124 an S-(1-hydroxy-2-oxopropyl)-[protein]-N-acetyl-L-lysine + H2O - Homo sapiens a [protein]-L-lysine + (R)-lactate - ? 439128 3.5.1.124 methylglyoxal + H2O - Vibrio cholerae (R)-lactate - ? 415682 3.5.1.124 methylglyoxal + H2O the enzyme also shows aminopeptidase activity and protease activity Vibrio cholerae (R)-lactate - ? 415682 3.5.1.124 methylglyoxal + H2O - Vibrio cholerae O395 (R)-lactate - ? 415682 3.5.1.124 methylglyoxal + H2O the enzyme also shows aminopeptidase activity and protease activity Vibrio cholerae O395 (R)-lactate - ? 415682 3.5.1.124 additional information glyoxalase activity of DJ-1 reflects its deglycase activity Homo sapiens ? - ? 89 3.5.1.124 additional information hemithioacetal degradation Homo sapiens ? - ? 89 3.5.1.124 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 ? - ? 89 3.5.1.124 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 Drosophila melanogaster ? - ? 89 3.5.1.124 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 Escherichia coli ? - ? 89 3.5.1.124 additional information the enzyme DJ-1 also shows glyoxalase III activity, cf. EC 4.2.1.130, which is representative of its deglycase activity Homo sapiens ? - ? 89 3.5.1.124 additional information the enzyme DJ-1 also shows glyoxalase III activity, cf. EC 4.2.1.130, which is representative of its deglycase activity Escherichia coli ? - ? 89 3.5.1.124 N6-(1-hydroxy-2-oxopropyl)-N2-acetyl-L-lysine + H2O - Homo sapiens N-acetyl-L-lysine + (R)-lactate - ? 439875 3.5.1.124 N6-(1-hydroxy-2-oxopropyl)-[alpha-synuclein]-L-lysine + H2O - Homo sapiens [alpha-synuclein]-L-lysine + lactate - ? 450388 3.5.1.124 Nomega-(1-hydroxy-2-oxopropyl)-Nalpha-acetyl-L-arginine + H2O - Homo sapiens Nalpha-acetyl-L-arginine + (R)-lactate - ? 439873 3.5.1.124 S-(1-hydroxy-2-oxopropyl)-N-acetyl-L-cysteine + H2O - Homo sapiens N-acetyl-L-cysteine + (R)-lactate - ? 439874 3.5.1.124 S-(1-hydroxy-2-oxopropyl)-N-acetyl-L-cysteine + H2O - Escherichia coli N-acetyl-L-cysteine + (R)-lactate - ? 439874 3.5.1.124 S-(1-hydroxy-2-oxopropyl)-N-acetyl-L-cysteine + H2O 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 Homo sapiens N-acetyl-L-cysteine + (R)-lactate - ? 439874 3.5.1.124 S-(1-hydroxy-2-oxopropyl)-[bovine serum albumin]-N-acetyl-L-cysteine + H2O - Homo sapiens [bovine serum albumin]-L-cysteine + (R)-lactate - ? 439876