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Literature summary for 4.2.1.130 extracted from

  • Choi, D.; Kim, J.; Ha, S.; Kwon, K.; Kim, E.H.; Lee, H.Y.; Ryu, K.S.; Park, C.
    Stereospecific mechanism of DJ-1 glyoxalases inferred from their hemithioacetal-containing crystal structures (2014), FEBS J., 281, 5447-5462.
    View publication on PubMed
Search for more literature for 4.2.1.130

Cloned(Commentary)

Cloned (Comment) Organism
gene PARK7, sequence comparisons Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Inhibitors

Inhibitors Comment Organism Structure
glyceraldehyde about 60% inhibition at 10 mM Homo sapiens
glycolaldehyde about 60% inhibition at 10 mM Homo sapiens
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
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

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
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
13
-
 Phenylglyoxal pH and temperature not specified in the publication Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2-oxopropanal + H2O Homo sapiens
-
 (R)-lactate
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens Q99497
-
-

Reaction

Reaction Comment Organism Reaction ID
(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
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-oxopropanal + H2O
-
 Homo sapiens (R)-lactate
-
 ?
2-oxopropanal + H2O i.e. methylglyoxal Homo sapiens (R)-lactate
-
 ?
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 ?
-
 ?
phenylglyoxal + H2O
-
 Homo sapiens ?
-
 ?

Subunits

Subunits Comment Organism
monomer enzyme structure comparisons, overview Homo sapiens

Synonyms

Synonyms Comment Organism
DJ-1
-
 Homo sapiens
DJ-1 glyoxalase
-
 Homo sapiens
glyoxalase III
-
 Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.0272
-
 Phenylglyoxal pH and temperature not specified in the publication Homo sapiens

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.14
-
 glyoxylate pH and temperature not specified in the publication Homo sapiens

General Information

General Information Comment Organism
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
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
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

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.0021
-
 Phenylglyoxal pH and temperature not specified in the publication Homo sapiens