Information on EC 4.2.1.130 - D-lactate dehydratase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
4.2.1.130
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RECOMMENDED NAME
GeneOntology No.
D-lactate dehydratase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(R)-lactate = methylglyoxal + H2O
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
methylglyoxal degradation
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Microbial metabolism in diverse environments
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Pyruvate metabolism
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SYSTEMATIC NAME
IUBMB Comments
(R)-lactate hydro-lyase
The enzyme converts methylglyoxal to D-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).
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
gene ScHSP31
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
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the stationary-phase Escherichia coli cells becomes more susceptible to methylglyoxal when hchA is deleted
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
methylglyoxal + H2O
(R)-lactate
show the reaction diagram
phenylglyoxal + H2O
?
show the reaction diagram
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the rate with phenylglyoxal is about 15% of that with methylglyoxal
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ir
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
methylglyoxal + H2O
(R)-lactate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
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enhances activity
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5,5'-dithiobis-(2-nitrobenzoate)
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0.4 mM, 15 min, complete inactivation. 5 mM DTT restores activity almost completely
Borate
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boric acid/borate buffer is moderately inhibitory
Cu2+
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maximal inhibition below 0.025 mM
EDTA
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an extensive dialysis of Hsp31 with 10 mM EDTA does not significantly decrease the glyoxalase III activity of more than 30%
hydrogen peroxide
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sensitivity of glyoxalase III is special and might relate to the thiol group that is essential for its activity and possibly to the binding of iron adjacent to the active site thiol
N-ethylmaleimide
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0.4 mM, 15 min, complete inactivation. 5 mM DTT restores activity almost completely
p-hydroxymercuribenzoate
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0.4 mM, 15 min, complete inactivation. 5 mM DTT restores activity almost completely
superoxide
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sensitivity of glyoxalase III is special and might relate to the thiol group that is essential for its activity and possibly to the binding of iron adjacent to the active site thiol
Zn2+
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maximal inhibition above 0.3 mM, 10% inhibition at 0.025 mM, more than 50% inhibition at 0.1 mM
additional information
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S-methylglutathione and S-octylglutathione, even at concentrations of 20 mM and 0.25 mM respectively, have no inhibitory effect on Escherichia coli glyoxalase III
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.19 - 58
methylglyoxal
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.095 - 2.61
methylglyoxal
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.03 - 1.8
methylglyoxal
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.254
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pH 7.5, temperature not specified in the publication
37
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pH 8.0, 37C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
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assay at
8
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assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 10
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pH 5.0: sharp decrease in reaction rate below, pH 10.0: activity 20-25% lower than the rate at physiological pH
5 - 9
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pH 5.0: about 45% of maximal activity, pH 9.0: about 45% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 50
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25C: about 55% of maximal activity, 50C: about 75% of maximal activity
PDB
SCOP
CATH
ORGANISM
UNIPROT
Candida albicans (strain SC5314 / ATCC MYA-2876)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
82000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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2 * 40000, SDS-PAGE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
DTT and either sucrose or mannitol are required for stability
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15C, 1 mM DTT and 10% sucrose, almost completely stable
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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, 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 ScHSP31, expression in Escherichia coli strain BL21(DE3), detailed phylogenetic analysis of GLOIII, DJ-1 and HSP31 proteins, overview. Overexpression of ScHSP31 can confer methylglyoxal and glyoxal resistance on either wild-type Schizosaccharomyces pombe cells or GLO1-deletion of Schizosaccharomyces pombe
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
glyoxalase III is a stationary-phase enzyme. Its activity reaches a maximum at the entry into the stationary phase and remained high for at least 20 h. Glyoxalase III is regulated by rpoS
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glyoxalase III is not elevated in Escherichia coli cells deleted for glyoxalase I
no induction of glyoxalase III by growth in the presence of methylglyoxal. Paraquat, which can increase the aerobic production of superoxide, suppresses glyoxalase III in JI132
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C185A
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mutation almost completely abolishes glyoxalase activity
E77A
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mutation almost completely abolishes glyoxalase activity
H184A
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kcat/KM is 3.6fold lower compared to the wild-type value
H186A
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mutant enzyme shows approximately 17% remaining activity
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
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