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Information on EC 4.2.1.130 - D-lactate dehydratase and Organism(s) Schizosaccharomyces pombe and UniProt Accession Q09675

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EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.1 Hydro-lyases
                4.2.1.130 D-lactate dehydratase
IUBMB 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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Schizosaccharomyces pombe
UNIPROT: Q09675
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Word Map
The taxonomic range for the selected organisms is: Schizosaccharomyces pombe
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
hsp31, glyoxalase iii, dj-1a, dj-1b, glutathione-independent glyoxalase, hsp3101, hsp3102, glutathione-independent glyoxalase iii, heat shock protein 31, dj-1 glyoxalase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glutathione-independent glyoxalase III
-
GSH-independent glyoxalase III
-
glutathione-independent glyoxalase III
-
glyoxylase III
-
-
-
-
GSH-independent glyoxalase III
-
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) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(R)-lactate
2-oxopropanal + H2O
show the reaction diagram
acetate
2-oxoethanal + H2O
show the reaction diagram
-
-
-
?
(R)-lactate
2-oxopropanal + H2O
show the reaction diagram
acetate
2-oxoethanal + H2O
show the reaction diagram
-
-
-
?
methylglyoxal + H2O
(R)-lactate
show the reaction diagram
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(R)-lactate
2-oxopropanal + H2O
show the reaction diagram
glyoxalase III (GLO3) converts methylglyoxal directly into D-lactate in a single step, independent of glutathione GSH
-
-
?
acetate
2-oxoethanal + H2O
show the reaction diagram
-
-
-
?
(R)-lactate
2-oxopropanal + H2O
show the reaction diagram
glyoxalase III (GLO3) converts methylglyoxal directly into D-lactate in a single step, independent of glutathione GSH
-
-
?
acetate
2-oxoethanal + H2O
show the reaction diagram
-
-
-
?
methylglyoxal + H2O
(R)-lactate
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
10.8 - 58
methylglyoxal
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.518 - 1.43
methylglyoxal
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.03 - 0.383
methylglyoxal
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
fungal Hsp31 proteins are the major glyoxalases III GLO3 that may have some role in protecting cells from reactive carbonyl species toxicity in fungi. The GLO3 activity of Hsp31 proteins may have evolved independently from GLO3 activity of DJ-1 proteins. DJ-1 and Hsp31 proteins belong to different subfamilies of the DJ-1/Hsp31/PfpI superfamily, which encompasses a wide variety of functionally diverse proteins, detailed phylogenetic analysis of DJ-1 and Hsp31 proteins, distribution of Hsp31 proteins in fungi, overview
evolution
physiological function
glyoxalase III is responsible for the detoxification of reactive carbonyl species, e.g. methylglyoxal and glyoxal, via the GSH-independent pathway, overview
additional information
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C111A
site-directed mutagenesis, catalytically inactive mutant
E16A
site-directed mutagenesis, catalytically inactive mutant
H130A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
additional information
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene hsp3102 encoding a Hsp31 protein, sequence comparisons, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant overexpression of Schizosaccharomyces pombe hsp3101 in Schizosaccharomyces pombe wild-type cells or GLO1 deletion cells
expression of C-terminally GFP-tagged SpDJ-1, expression of wild-type and mutant SpDj-1 proteins in Escherichia coli strain BL21(DE3), detailed phylogenetic analysis of GLOIII, DJ-1 and HSP31 proteins, overview
gene hsp3101 encoding a Hsp31 protein, DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic analysis, recombinant overexpression of Schizosaccharomyces pombe hsp3101 in Schizosaccharomyces pombe wild-type cells or GLO1 deletion cells
gene hsp3101, expression of C-terminally GFP-tagged HSP31 proteins, expression of HSP3101 protein in Escherichia coli strain BL21(DE3), detailed phylogenetic analysis of GLOIII, DJ-1 and HSP31 proteins, overview
gene hsp3106 encoding DJ-1 protein, DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic analysis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zhao, Q.; Su, Y.; Wang, Z.; Chen, C.; Wu, T.; Huang, Y.
Identification of glutathione (GSH)-independent glyoxalase III from Schizosaccharomyces pombe
BMC Evol. Biol.
14
86
2014
Saccharomyces cerevisiae (Q04432), Schizosaccharomyces pombe, Schizosaccharomyces pombe (O74914), Schizosaccharomyces pombe (Q09675), Schizosaccharomyces pombe (Q10356), Schizosaccharomyces pombe 972 (O74914)
Manually annotated by BRENDA team