Information on EC 1.1.1.60 - 2-hydroxy-3-oxopropionate reductase

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

EC NUMBER
COMMENTARY hide
1.1.1.60
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RECOMMENDED NAME
GeneOntology No.
2-hydroxy-3-oxopropionate reductase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-glycerate + NAD(P)+ = 2-hydroxy-3-oxopropanoate + NAD(P)H + H+
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
D-galactarate degradation I
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D-glucarate degradation I
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degradation of sugar acids
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Glyoxylate and dicarboxylate metabolism
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Metabolic pathways
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SYSTEMATIC NAME
IUBMB Comments
D-glycerate:NAD(P)+ oxidoreductase
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CAS REGISTRY NUMBER
COMMENTARY hide
9028-68-6
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
OX1
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
putative
Q4PBC1
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
Q4PBC1
over-expression of the gene results in improved glycerol assimilation. Glycolipid accumulation is reduced by 45.2% in the knockout mutant whereas over-expression of the gene increases it by 40.4%
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(R)-beta-hydroxybutyrate + NAD+
?
show the reaction diagram
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-
-
-
?
(R)-glycerate + NAD(P)+
tartronate semialdehyde + NAD(P)H
show the reaction diagram
2-hydroxy-3-oxopropanoate + NADH + H+
D-glycerate + NAD+
show the reaction diagram
Q4PBC1
-
-
-
?
D-glycerate + NADP+
2-hydroxy-3-oxopropanoate + NADPH + H+
show the reaction diagram
Q4PBC1
enzyme shows strong specificity and enantioselectivity for D-glycerate
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?
D-threonine + NAD+
?
show the reaction diagram
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?
hydroxypyruvate + NAD(P)H
glycerate + NAD(P)+
show the reaction diagram
L-glycerate + NADP+
2-hydroxy-3-oxopropanoate + NADPH + H+
show the reaction diagram
Q4PBC1
enzyme shows strong specificity and enantioselectivity for D-glycerate
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-
?
malonic semialdehyde + NADH
3-hydroxypropanoate + NAD+
show the reaction diagram
mesoxalic semialdehyde + NADH
hydroxypyruvate + NAD+
show the reaction diagram
tartronate semialdehyde + NAD(P)H
(R)-glycerate + NAD(P)+
show the reaction diagram
tartronate semialdehyde + NADH
(R)-glycerate + NAD+
show the reaction diagram
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as cofactor in the final stage of D-glycerate biosynthesis
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?
tartronate semialdehyde + NADH + H+
(R)-glycerate + NAD+
show the reaction diagram
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?
additional information
?
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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
tartronate semialdehyde + NAD(P)H
(R)-glycerate + NAD(P)+
show the reaction diagram
tartronate semialdehyde + NADH
(R)-glycerate + NAD+
show the reaction diagram
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as cofactor in the final stage of D-glycerate biosynthesis
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
NADPH
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,4,6-Trinitrobenzene sulfonate
beta-Mercaptopyruvate
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Dihydroxyfumarate
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EDTA
Q4PBC1
severe inhibition
fluoroacetate
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glycolate
glyoxylate
Malonic semialdehyde
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Succinic semialdehyde
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.048
(R)-beta-hydroxybutyrate
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0.00019
2-hydroxy-3-oxopropanoate
Q4PBC1
pH 8.5, 40C
0.0177 - 3.7
D-glycerate
0.06
D-threonine
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0.123 - 4.2
L-Glycerate
0.2
Malonic semialdehyde
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0.04
NAD+
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0.0143 - 0.027
NADH
0.0003
NADP+
Q4PBC1
pH 8.5, 40C
0.036 - 0.05
NADPH
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0.05 - 0.4
tartronate semialdehyde
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
243
NADH
Pseudomonas putida
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.5
Q4PBC1
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
Q4PBC1
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Polaromonas sp. (strain JS666 / ATCC BAA-500)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
85000
Q4PBC1
gel filtration
91000
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sedimentation equilibrium
104000
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sedimentation velocity
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
Q4PBC1
2 * 40000, SDS-PAGE, 2 * 41000, calculated, recombinant protein
tetramer
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4 * 26000, sedimentation velocity after treatment with guanidine hydrochloride and mercaptoethanol, amino acid analysis
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
enzyme with L-tartrate bound to the active site, sitting drop vapour diffusion method, mixing of 0.0005 ml of the protein solution, containing 107 mg/ml protein in in 10 mM HEPES pH 8.0, 200 mM NaCl, with 0.0005 ml of 0.1 M imidazole buffer pH 8.0, 1 M potassium/sodium L-tartrate and 0.2 M sodium chloride, and equilibrated at 16C over 0.135 ml of this solution, overnight, X-ray diffraction structure determination and analysis at 1.65 A resolution, the single-wavelength anomalous diffraction method
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
Q4PBC1
rapidly precipitates below
726270
7
Q4PBC1
phosphate buffer, pH 7.0, improved solubility
726270
8
Q4PBC1
Tris-HCl, highly unstable, precipitates during storage
726270
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
2C, suspension in ammonium sulfate, pH 7.5, 10% loss in 1 month
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4C, phosphate buffer, pH 7.0, improved solubility
Q4PBC1
4C, Tris-HCl, pH 8.0, highly unstable, precipitates during storage
Q4PBC1
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
of recombinant protein
recombinant His6-tagged GarR from Escherichia coli strain BL21, the tag is removed by TEV protease, purification by nickel affinity chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
Q4PBC1
gene garR, expression of the His6-tagged enzyme in Escherichia coli strain BL21
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overexpression in Escherichia coli
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