Information on EC 1.1.1.81 - hydroxypyruvate reductase

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

EC NUMBER
COMMENTARY hide
1.1.1.81
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RECOMMENDED NAME
GeneOntology No.
hydroxypyruvate reductase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-glycerate + NAD(P)+ = hydroxypyruvate + 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
Biosynthesis of secondary metabolites
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formaldehyde assimilation I (serine pathway)
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Glycine, serine and threonine metabolism
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Glyoxylate and dicarboxylate metabolism
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Metabolic pathways
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serine metabolism
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SYSTEMATIC NAME
IUBMB Comments
D-glycerate:NADP+ 2-oxidoreductase
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CAS REGISTRY NUMBER
COMMENTARY hide
9059-44-3
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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
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
strain MB200, capable of producing glyoxylate from methanol
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Manually annotated by BRENDA team
strain MB200, capable of producing glyoxylate from methanol
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Manually annotated by BRENDA team
gene GRHPR
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Manually annotated by BRENDA team
Nicotiana tabacum cv. SR1
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
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NADH-HPR is extensively involved in carbon metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2,3-butandione + NAD(P)H
butan-2-ol-3-one + NAD(P)+
show the reaction diagram
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33 mM, 12% of activity with hydroxypyruvate
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?
acetoin + NAD(P)H + H+
2,3-butanediol + NAD(P)+
show the reaction diagram
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33 mM, 14% of activity with hydroxypyruvate
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?
glyoxylate + NAD(P)H
glycolate + NAD(P)+
show the reaction diagram
glyoxylate + NAD(P)H + H+
glycolate + NAD(P)+
show the reaction diagram
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?
glyoxylate + NADH
glycolate + NAD+
show the reaction diagram
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?
glyoxylate + NADPH
glycolate + NADP+
show the reaction diagram
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?
glyoxylate + NADPH + H+
glycolate + NADP+
show the reaction diagram
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?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
hydroxypyruvate + NAD(P)H + H+
D-glycerate + NAD(P)+
show the reaction diagram
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?
hydroxypyruvate + NADH
D-glycerate + NAD+
show the reaction diagram
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?
hydroxypyruvate + NADH + H+
D-glycerate + NAD+
show the reaction diagram
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?
hydroxypyruvate + NADPH
D-glycerate + NADP+
show the reaction diagram
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
show the reaction diagram
oxaloacetate + NAD(P)H
malate + NAD(P)+
show the reaction diagram
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33 mM, 32% of activity with hydroxypyruvate
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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
glyoxylate + NAD(P)H
glycolate + NAD(P)+
show the reaction diagram
glyoxylate + NADPH + H+
glycolate + NADP+
show the reaction diagram
Q9LE33
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?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
hydroxypyruvate + NAD(P)H + H+
D-glycerate + NAD(P)+
show the reaction diagram
Q9C9W5, Q9CA90
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?
hydroxypyruvate + NADH + H+
D-glycerate + NAD+
show the reaction diagram
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?
hydroxypyruvate + NADPH
D-glycerate + NADP+
show the reaction diagram
Q9LE33
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hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,3-diphospho-D-glycerate
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1 mM, 83% and 91% inhibition of hydroxypyruvate reduction and D-glycerate oxidation respectively
2-phospho-DL-glycerate
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1 mM, 93% and 81% inhibition of hydroxypyruvate reduction and D-glycerate oxidation respectively
3-phospho-D-glycerate
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1 mM, 53% and 65% inhibition of hydroxypyruvate reduction and D-glycerate oxidation respectively
Ag+
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0.1 mM, complete inhibition
alpha-D-fructose 1,6-diphosphate
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0.1 mM, 28% and 74% inhibition of hydroxypyruvate reduction and D-glycerate oxidation respectively
ATP
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1 mM, 62% and 64% inhibition of liver and spinal cord enzyme respectively, 73% and 89% inhibition of hydroxypyruvate reduction and D-glycerate oxidation respectively
bromide
citrate
Cl-
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100 mM, 50% inhibition of D-glycerate oxidation
CTP
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1 mM, 73% and 71% inhibition of liver and spinal cord enzyme respectively
D-glycerate
glycolate
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5 mM, 15% of NADPH linked reduction
glyoxylate
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10 mM, 55% inhibition of NADH linked hydroxypyruvate reduction, 15% of NADPH linked reduction, 80% of NAD+ linked glycerate oxidation
GTP
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1 mM, 94% and 93% inhibition of liver and spinal cord enzyme respectively
Hg2+
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0.1 mM, complete inhibition
Hydroxypyruvate
Iodide
NAD+
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4 mM, 10% inhibition of NADH linked hydroxypyruvate reduction, 60% of NADPH linked reduction
NADP+
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4 mM, 15% inhibition of NADH linked hydroxypyruvate reduction, 40% of NADPH linked reduction, 8% of NAD+ linked glycerate oxidation
NaNO3
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80 mM, 50% inhibition
NO3-
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100 mM, 87% inhibition of D-glycerate oxidation
oxalate
oxaloacetate
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2.5 mM, 10% inhibition of NADH linked hydroxypyruvate reduction, 20% of NADPH linked reduction
p-chloromercuribenzoate
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0.1 mM, complete inhibition
phosphohydroxypyruvate
pyruvate
SO42-
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100 mM, 55% inhibition of D-glycerate oxidation
Sodium bisulfite
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0.01 mM, 16% inhibition, 0.1 mM, 67% inhibition
Tartronate
UTP
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1 mM, 83% and 84% inhibition of liver and spinal cord enzyme respectively
additional information
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not inhibited by 2 mM acetohydroxamate
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
CsCl
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80 mM, 3fold increase in hydroxypyruvate reductase activity
F-
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100 mM, 67% activation of hydroxypyruvate reduction
KCl
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80 mM, 9fold increase in hydroxypyruvate reductase activity
N,N'-diphenylurea
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N6-benzyladenine
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NaCl
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80 mM, 8fold increase in hydroxypyruvate reductase activity, reaction rate increases with an increase in NaCl concentration up to 200 mM, but diminishes if the salt concentration is greater
trans-zeatin
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additional information
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in the dark, cytokinins mimic the regulatory effect of light upon algal cell division, metabolite content and stimulate carbon recycling for Calvin cycle reactions by enhancing of light-dependent NADH-HPR activity by up to 62%, overview
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.522
D-glycerate
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D-glycerate oxidation, 50 mM, NaCl, pH 9
1.4
DL-glycerate
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0.0038 - 40
Hydroxypyruvate
0.077 - 0.22
NAD+
0.0061 - 0.24
NADH
0.037
NADP+
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0.015 - 0.06
NADPH
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.1 - 11
NADH
1.8 - 2.4
NADPH
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0162
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enzyme activity in crude leaf extracts of LaPr 88/29 mutant which exhibits no NADH-dependent hydroxypyruvate activity
0.054
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enzyme activity in leaf extracts of LaPr 88/29 mutant which lacks NADH-prefering hydroxypyruvate reductase
0.068
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enzyme activity in leaf extracts of wild type
0.077
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oxidation of glycerate
0.0834
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enzyme activity in crude leaf extracts of wild type
0.1
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in cell-free extracts
0.135
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cofactor NADH
0.33
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cofactor NADPH
0.745
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0.9
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in cell-free extracts
1.06
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ammonium sulfate fractionated leaf extracts, 45-60% fraction
1.5
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in cell-free extracts
1.7
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in cell-free extracts
1.9
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in cell-free extracts
2.67
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13.01
Nicotiana tabacum cv. SR1
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enzyme activity in leaf tissue
104.8
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5
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broad optimum between pH 4.0 and 6.5 for hydroxypyruvate reduction
5.3
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sharp drop of activity below and above
6.2
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assay at
6.5
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hydroxypyruvate reduction
7
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hydroxypyruvate reduction
7.5
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assay at
9 - 11
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glycerate oxidation
9.3
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D-glycerate oxidation
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.3
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sharp drop of activity below and above
5.5 - 6
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strong decrease above
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
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assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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axenic cultures
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45000
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immunoprecipitation
50000
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gel filtration, two enzymes in low and high salt fractions after DEAE-cellulose chromatography
70000
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gel filtration
71000
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gradient PAGE
72000
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sedimentation velocity analysis
76500
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analytical ultracentrifugation
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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1 * 50000, SDS-PAGE, two enzymes in low and high salt fractions after DEAE-cellulose chromatography
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified detagged recombinant enzyme in ternary complex with product D-glycerate and cofactor NADPH, sitting drop vapour diffusion method, 5.5 mg/ml protein in 20 mM Tris-HCl, pH 8.5, 1 mM 2-mercaptoethanol, 0.2 mM NADPH, and 0.5 mm di-sodium oxalate, mixed with mother liquor, containing 15% w/v PEG 8000, 0.2 M ammonium sulfate, and 0.1 M sodium cacodylate, pH 6.5, to 0.002 ml drops, 18C, X-ray diffraction structure determination and analysis at 2.2 A resolution
sitting drop vapor diffusion method in the presence of NAD, crystal structure analysis reveals tightly bound NADP(H) at the enzyme originating from Escherichia coli expression, which is not replaceable by NAD
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
42
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half-life of 35 min in 50 mM phosphate buffer, pH 7.0
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
activity is slowly lost on storage at -15C interspersed with frequent thawing and re-freezing, about 20% activity is lost over 8 cycles of freezing and thawing
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dithiothreitol stabilizes
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 20 mM MOPS, pH 7.1, 14 mM 2-mercaptoethanol, 50% glycerol
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4C, 50 mM Tris-HCl, pH 7.5, 10% glycerol, 1 mM dithiothreitol, 2 months, 10% loss of activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His-tag protein from Escherichia coli
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recombinant His-tagged wild-type and mutant enzymes from Escherichia coli by nickel affinity chromatography, the His-tag is cleaved by thrombin followed by gel filtration, over 95% purity
recombinant protein from Escherichia coli
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed as His-tag fusion protein in Escherichia coli Turner (DE3); expressed in host strain to create the new strain Methylobacterium sp. MB201, 2fold increase in glyoxylate production
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expressed in Escherichia coli
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expressed in Escherichia coli BL21-CodonPlus(DE3)-RIL and Escherichia coli B834(DE3)pRARE
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expressed in Escherichia coli; recombinant expression of GFP-tagged HPR2 in transgenic Arabidospsis thaliana plants
expression in Escherichia coli
expression of His-tagged wild-type and mutant enzymes in Escherichia coli
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gene GRHPR, localization of chromosome 9q12, DNA and amino acid sequence determination and analysis, genetic structure and promoter analysis, expression analysis, expression as GFP-fusion protein in the cytosol of HEK293 cells, co-expression with PPARalpha in HepG2 cells and regulation, overview
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
promoter region of AtHPR1 is characterized. Promoter contains the core motif of the dehydration-responsive cis-acting element and AtHPR1 expression is inducible by drought stress
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G160R
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site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
G165D
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site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
M322R
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site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
R302C
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site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
G160R
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site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
G165D
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site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
M322R
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site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
R302C
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site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
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conditional and specific down-regulation of farnesyltransferase in canola using the AtHPR1 promoter driving an RNAi construct results in yield protection against drought stress in the field
synthesis
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