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Information on EC 4.2.1.130 - D-lactate dehydratase and Organism(s) Homo sapiens and UniProt Accession Q99497
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4.2.1.130 D-lactate dehydrataseIUBMB Comments
The enzyme, described from the fungi Candida albicans and Schizosaccharomyces pombe, converts 2-oxopropanal to (R)-lactate in a single glutathione (GSH)-independent step. The other known route for this conversion is the two-step GSH-dependent pathway catalysed by EC 4.4.1.5 (lactoylglutathione lyase) and EC 3.1.2.6 (hydroxyacylglutathione hydrolase).
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Word Map
- 4.2.1.130
- methylglyoxal
- parkinsonism
- glyoxals
-
glyoxalases
- methylglyoxalase
-
deglycase
-
diauxic
- horikoshii
- agriculture
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
hsp31, glyoxalase iii, dj-1a, dj-1b, glutathione-independent glyoxalase, glutathione-independent glyoxalase iii, hsp3101, hsp3102, dj-1 glyoxalase, hsp31p glyoxalase iii, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
glyoxylase III
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(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)
PATHWAY SOURCE
PATHWAYS
BRENDA
SYSTEMATIC NAME
IUBMB Comments
(R)-lactate hydro-lyase
The enzyme, described from the fungi Candida albicans and Schizosaccharomyces pombe, converts 2-oxopropanal to (R)-lactate in a single glutathione (GSH)-independent step. The other known route for this conversion is the two-step GSH-dependent pathway catalysed by EC 4.4.1.5 (lactoylglutathione lyase) and EC 3.1.2.6 (hydroxyacylglutathione hydrolase).
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
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-
?
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
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
additional information
poor or no inhibition by acrolein, acetaldehyde, propionaldehyde, butyraldehyde, valeraldehyde, acetol, 2,3-butanedione, dihydroxyacetone, 1,2-propanediol, and oxalic acid
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additional information
-
poor or no inhibition by acrolein, acetaldehyde, propionaldehyde, butyraldehyde, valeraldehyde, acetol, 2,3-butanedione, dihydroxyacetone, 1,2-propanediol, and oxalic acid
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
900
methylglyoxal
30°C, pH not specified in the publication, wild-type enzyme
1900
methylglyoxal
30°C, pH not specified in the publication, mutant enzyme L166P
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
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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
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
additional information
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
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PDB
SCOP
CATH
UNIPROT
ORGANISM
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
L166P
the Km-value for methylglyoxal of the mutant enzyme is about 2fold higher compared to the wild-type enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DJ-1 gene is subcloned from pLenti6-DJ-1-V5-WT plasmid into the pRetroX-Tight-Puro Advanced vector. The confirmed clone is transfected into HEK-293 cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
FEBS J.
281
5447-5462
2014
Homo sapiens (Q99497), Homo sapiens
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