EC Number | Cloned (Comment) | Organism |
---|---|---|
4.2.1.130 | gene PARK7, sequence comparisons | Homo sapiens |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
4.2.1.130 | purified enzyme DJ-1d covalently bound to glyoxylate, X-ray diffraction structure determinatin and analysis at 1.60 A resolution, PDB ID 4OGF, and analysis of structure PDB ID 1P5F | Homo sapiens |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
4.2.1.130 | glyceraldehyde | about 60% inhibition at 10 mM | Homo sapiens | |
4.2.1.130 | glycolaldehyde | about 60% inhibition at 10 mM | Homo sapiens | |
4.2.1.130 | glyoxylate | determmination of an enzyme crystal structure with the inhibitor bound to the active Cys residue of the enzyme as a hemithioacetal, detailed binding structure analysis, overview | Homo sapiens | |
4.2.1.130 | additional information | poor or no inhibition by acrolein, acetaldehyde, propionaldehyde, butyraldehyde, valeraldehyde, acetol, 2,3-butanedione, dihydroxyacetone, 1,2-propanediol, and oxalic acid | Homo sapiens |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
4.2.1.130 | additional information | - |
additional information | cooperative mechanism, Eadie-Hofstee plots for hDJ-1 indicate mono- and bi-phasic curves, which are analyzed by using the Hill equation and gives a coefficient (n) of 1.0. KInetics, overview | Homo sapiens | |
4.2.1.130 | 13 | - |
Phenylglyoxal | pH and temperature not specified in the publication | Homo sapiens |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.2.1.130 | 2-oxopropanal + H2O | Homo sapiens | - |
(R)-lactate | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
4.2.1.130 | Homo sapiens | Q99497 | - |
- |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
4.2.1.130 | (R)-lactate = 2-oxopropanal + H2O | proton transfer mechanism in the enzyme reaction of DJ-1 glyoxalase, whose stereospecificity is determined by the location of neighboring His residues. hDJ-1 contains a single His residue (H126) | Homo sapiens |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.2.1.130 | 2-oxopropanal + H2O | - |
Homo sapiens | (R)-lactate | - |
? | |
4.2.1.130 | 2-oxopropanal + H2O | i.e. methylglyoxal | Homo sapiens | (R)-lactate | - |
? | |
4.2.1.130 | additional information | the glyoxalase mechanism of the DJ-1 superfamily proteins involves an enediol proton transfer mediated by a basic residue rather than a [1,2]-hydride shift. D- or L-lactate production by DJ-1 glyoxalase is simulated by molecular modeling | Homo sapiens | ? | - |
? | |
4.2.1.130 | phenylglyoxal + H2O | - |
Homo sapiens | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
4.2.1.130 | monomer | enzyme structure comparisons, overview | Homo sapiens |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
4.2.1.130 | DJ-1 | - |
Homo sapiens |
4.2.1.130 | DJ-1 glyoxalase | - |
Homo sapiens |
4.2.1.130 | glyoxalase III | - |
Homo sapiens |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
4.2.1.130 | 0.0272 | - |
Phenylglyoxal | pH and temperature not specified in the publication | Homo sapiens |
EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|---|
4.2.1.130 | 0.14 | - |
glyoxylate | pH and temperature not specified in the publication | Homo sapiens |
EC Number | General Information | Comment | Organism |
---|---|---|---|
4.2.1.130 | evolution | the enzyme belongs to the DJ-1 superfamily. DJ-1 superfamily proteins share the structural similarity, comprising central beta-strands surrounded by alpha-helices. Based on their primary sequences and 3D structures, the DJ-1 superfamily members are classified into three groups: DJ-1/YajL, YhbO/PfpI, and Hsp31/Ydr533C. The configuration of the active site of hDJ-1 is very different from that of Arabidopsis taliana atDJ-1d, apparently lacking some catalytic residues | Homo sapiens |
4.2.1.130 | additional information | human enzyme DJ-1 covalently bound to glyoxylate, an analogue of methylglyoxal, forms a hemithioacetal that presumably mimics an intermediate structure in catalysis of methylglyoxal to lactate. Reaction stereospecificity modelling by a molecular modeling simulation with methylglyoxal hemithioacetal superimposed on the glyoxylate hemithioacetal. The mechanism of DJ-1 glyoxalase provides a basis for understanding the His residue-based stereospecificity, overview. Enzyme structure comparisons, the presence of the conserved Glu and Cys residues is critical for the glyoxalase activity of hDJ-1 | Homo sapiens |
4.2.1.130 | physiological function | human DJ-1 (hDJ-1) is associated with autosomal recessive Parkinson's disease unction as a molecular chaperone as well as a transcriptional regulator | Homo sapiens |
EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
4.2.1.130 | 0.0021 | - |
Phenylglyoxal | pH and temperature not specified in the publication | Homo sapiens |