BRENDA - Enzyme Database show
show all sequences of 1.1.1.81

Structural basis of substrate specificity in human glyoxylate reductase/hydroxypyruvate reductase

Booth, M.P.; Conners, R.; Rumsby, G.; Brady, R.L.; J. Mol. Biol. 360, 178-189 (2006)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression of His-tagged wild-type and mutant enzymes in Escherichia coli
Homo sapiens
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
Mus musculus
Crystallization (Commentary)
Crystallization
Organism
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, 18°C, X-ray diffraction structure determination and analysis at 2.2 A resolution
Homo sapiens
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, 18°C, X-ray diffraction structure determination and analysis at 2.2 A resolution
Mus musculus
Engineering
Amino acid exchange
Commentary
Organism
G160R
site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
Homo sapiens
G160R
site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
Mus musculus
G165D
site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
Homo sapiens
G165D
site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
Mus musculus
M322R
site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
Homo sapiens
M322R
site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
Mus musculus
R302C
site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
Homo sapiens
R302C
site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
Mus musculus
Inhibitors
Inhibitors
Commentary
Organism
Structure
D-glycerate
the enzyme shows product inhibition
Homo sapiens
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
cytosol
-
Mus musculus
5829
-
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
glyoxylate + NAD(P)H
Mus musculus
-
glycolate + NAD(P)+
-
-
?
glyoxylate + NAD(P)H
Homo sapiens
the enzyme is involved in removal of the metabolic by-product from liver
glycolate + NAD(P)+
-
-
?
hydroxypyruvate + NAD(P)H
Mus musculus
-
D-glycerate + NAD(P)+
-
-
?
hydroxypyruvate + NAD(P)H
Homo sapiens
-
D-glycerate + NAD(P)+
-
-
?
additional information
Homo sapiens
enzyme deficiency leads to primary hyperoxaluria type 2 with increased urinary oxalate levels, formation of kidney stones, and renal failure
?
-
-
-
additional information
Mus musculus
the enzyme is transcriptionally regulated by the peroxisome proliferator-activated receptor alpha, PPARalpha, in liver, overview
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Homo sapiens
-
-
-
Mus musculus
-
gene GRHPR
-
Purification (Commentary)
Commentary
Organism
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
Homo sapiens
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
Mus musculus
Source Tissue
Source Tissue
Commentary
Organism
Textmining
kidney
-
Mus musculus
-
liver
-
Mus musculus
-
liver
-
Homo sapiens
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
glyoxylate + NAD(P)H
-
669886
Mus musculus
glycolate + NAD(P)+
-
-
-
?
glyoxylate + NAD(P)H
-
669886
Homo sapiens
glycolate + NAD(P)+
-
-
-
?
glyoxylate + NAD(P)H
the enzyme is involved in removal of the metabolic by-product from liver
669886
Homo sapiens
glycolate + NAD(P)+
-
-
-
?
hydroxypyruvate + NAD(P)H
-
669886
Mus musculus
D-glycerate + NAD(P)+
-
-
-
?
hydroxypyruvate + NAD(P)H
-
669886
Homo sapiens
D-glycerate + NAD(P)+
-
-
-
?
additional information
enzyme deficiency leads to primary hyperoxaluria type 2 with increased urinary oxalate levels, formation of kidney stones, and renal failure
669886
Homo sapiens
?
-
-
-
-
additional information
the enzyme is transcriptionally regulated by the peroxisome proliferator-activated receptor alpha, PPARalpha, in liver, overview
669886
Mus musculus
?
-
-
-
-
additional information
structural basis of enzyme substrate specificity, active site structure and substrate binding, no activity with pyruvate, overview
669886
Homo sapiens
?
-
-
-
-
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Homo sapiens
Cofactor
Cofactor
Commentary
Organism
Structure
NADH
-
Homo sapiens
NADH
-
Mus musculus
NADPH
binding structure
Homo sapiens
NADPH
-
Mus musculus
Cloned(Commentary) (protein specific)
Commentary
Organism
expression of His-tagged wild-type and mutant enzymes in Escherichia coli
Homo sapiens
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
Mus musculus
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADH
-
Homo sapiens
NADH
-
Mus musculus
NADPH
binding structure
Homo sapiens
NADPH
-
Mus musculus
Crystallization (Commentary) (protein specific)
Crystallization
Organism
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, 18°C, X-ray diffraction structure determination and analysis at 2.2 A resolution
Homo sapiens
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, 18°C, X-ray diffraction structure determination and analysis at 2.2 A resolution
Mus musculus
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
G160R
site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
Homo sapiens
G160R
site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
Mus musculus
G165D
site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
Homo sapiens
G165D
site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
Mus musculus
M322R
site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
Homo sapiens
M322R
site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
Mus musculus
R302C
site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
Homo sapiens
R302C
site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
Mus musculus
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
D-glycerate
the enzyme shows product inhibition
Homo sapiens
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
cytosol
-
Mus musculus
5829
-
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
glyoxylate + NAD(P)H
Mus musculus
-
glycolate + NAD(P)+
-
-
?
glyoxylate + NAD(P)H
Homo sapiens
the enzyme is involved in removal of the metabolic by-product from liver
glycolate + NAD(P)+
-
-
?
hydroxypyruvate + NAD(P)H
Mus musculus
-
D-glycerate + NAD(P)+
-
-
?
hydroxypyruvate + NAD(P)H
Homo sapiens
-
D-glycerate + NAD(P)+
-
-
?
additional information
Homo sapiens
enzyme deficiency leads to primary hyperoxaluria type 2 with increased urinary oxalate levels, formation of kidney stones, and renal failure
?
-
-
-
additional information
Mus musculus
the enzyme is transcriptionally regulated by the peroxisome proliferator-activated receptor alpha, PPARalpha, in liver, overview
?
-
-
-
Purification (Commentary) (protein specific)
Commentary
Organism
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
Homo sapiens
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
Mus musculus
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
kidney
-
Mus musculus
-
liver
-
Homo sapiens
-
liver
-
Mus musculus
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
glyoxylate + NAD(P)H
-
669886
Mus musculus
glycolate + NAD(P)+
-
-
-
?
glyoxylate + NAD(P)H
-
669886
Homo sapiens
glycolate + NAD(P)+
-
-
-
?
glyoxylate + NAD(P)H
the enzyme is involved in removal of the metabolic by-product from liver
669886
Homo sapiens
glycolate + NAD(P)+
-
-
-
?
hydroxypyruvate + NAD(P)H
-
669886
Mus musculus
D-glycerate + NAD(P)+
-
-
-
?
hydroxypyruvate + NAD(P)H
-
669886
Homo sapiens
D-glycerate + NAD(P)+
-
-
-
?
additional information
enzyme deficiency leads to primary hyperoxaluria type 2 with increased urinary oxalate levels, formation of kidney stones, and renal failure
669886
Homo sapiens
?
-
-
-
-
additional information
the enzyme is transcriptionally regulated by the peroxisome proliferator-activated receptor alpha, PPARalpha, in liver, overview
669886
Mus musculus
?
-
-
-
-
additional information
structural basis of enzyme substrate specificity, active site structure and substrate binding, no activity with pyruvate, overview
669886
Homo sapiens
?
-
-
-
-
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Homo sapiens
Other publictions for EC 1.1.1.81
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
739242
Zong
Up regulation of glyoxylate re ...
Homo sapiens
Pathol. Res. Pract.
212
365-371
2016
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1
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1
1
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739674
Lassalle
New insights into the mechanis ...
Pyrococcus furiosus, Pyrococcus horikoshii, Pyrococcus yayanosii, Pyrococcus yayanosii CH1
Sci. Rep.
6
20629
2016
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3
3
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4
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3
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6
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6
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737745
Hoover
Identification of catalyticall ...
Arabidopsis thaliana
Biochim. Biophys. Acta
1834
2663-2671
2013
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3
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1
1
726219
Timm
The hydroxypyruvate-reducing s ...
Arabidopsis thaliana
Plant Physiol.
155
694-705
2011
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1
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1
1
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695413
Piotrowska
-
Cellular response of light/dar ...
Chlorella vulgaris
Acta Physiol. Plant.
31
573-585
2009
5
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1
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1
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1
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1
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2
2
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705820
Wang
Shoot-specific down-regulation ...
Brassica napus
Mol. Plant
2
191-200
2009
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1
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5
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700736
Timm
A cytosolic pathway for the co ...
Arabidopsis thaliana
Plant Cell
20
2848-2859
2008
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6
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684141
Yoshikawa
Structure of archaeal glyoxyla ...
Pyrococcus horikoshii OT3
Acta Crystallogr. Sect. D
63
357-365
2007
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1
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688165
Shen
Over-expression of a hydroxypy ...
Methylobacterium sp., Methylobacterium sp. MB200
J. Ind. Microbiol. Biotechnol.
34
657-663
2007
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1
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669886
Booth
Structural basis of substrate ...
Homo sapiens, Mus musculus
J. Mol. Biol.
360
178-189
2006
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2
2
8
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1
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1
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6
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286510
Hagishita
Immunological characterization ...
Cucumis sativus, Hyphomicrobium methylovorum GM2, Methylobacterium extorquens AM1, Methylobacterium organophilum, Spinacia oleracea
FEMS Microbiol. Lett.
142
49-52
1996
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287364
Yoshida
Cloning and expression of the ...
Hyphomicrobium methylovorum GM2
Eur. J. Biochem.
223
727-732
1994
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287365
Oliver
Inhibition of tobacco NADH-hyd ...
Nicotiana tabacum cv. SR1
Mol. Gen. Genet.
239
425-434
1993
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286505
Kleczkowski
Oxalate as a potent and select ...
Spinacia oleracea
Biochem. J.
276
125-127
1991
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3
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286508
Chistoserdova
Purification and characterizat ...
Methylobacterium extorquens AM1
J. Bacteriol.
173
7228-7232
1991
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5
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1
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287368
Kleczkowski
Enzymology of the reduction of ...
Hordeum vulgare
Plant Physiol.
94
819-825
1990
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2
2
1
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4
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287369
Krema
-
Hydroxypyruvate reductase from ...
Methylobacterium extorquens AM1
Methods Enzymol.
188
373-378
1990
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2
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1
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287370
Kleczkowski
Identification of hydroxypyruv ...
Zea mays
Plant Physiol.
91
278-288
1989
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287371
Murray
Metabolism of hydroxypyruvate ...
Hordeum vulgare
Plant Physiol.
91
395-400
1989
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287372
Sautter
Import of peroxisomal hydroxyp ...
Citrullus lanatus subsp. vulgaris, Cucurbita pepo, Spinacia oleracea
Planta
176
149-158
1988
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3
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8
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287373
Kleczkowski
Subcellular location of NADPH- ...
Pisum sativum, Spinacia oleracea
Plant Physiol.
88
1182-1185
1988
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2
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2
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7
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287374
Kleczkowski
Purification and characterizat ...
Spinacia oleracea
Biochem. J.
250
145-152
1988
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1
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5
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1
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1
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287383
Coderch
Effect of salts on D-glycerate ...
Bos taurus
Biochim. Biophys. Acta
566
21-31
1979
3
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4
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287375
Bamforth
-
Hydroxypyruvate reductase acti ...
Paracoccus denitrificans
J. Gen. Microbiol.
101
259-267
1977
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3
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6
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287376
Feld
Comparison of D-glycerate dehy ...
Bos taurus, Sus scrofa
Arch. Biochem. Biophys.
166
417-425
1975
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3
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287377
Feld
D-Glycerate dehydrogenase from ...
Sus scrofa
Methods Enzymol.
41B
289-293
1975
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287378
Sugimoto
Mechanisms of inhibition and a ...
Bos taurus
J. Biochem.
72
1317-1325
1972
6
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6
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287379
Sugimoto
Purification and properties of ...
Bos taurus
J. Biochem.
72
1307-1315
1972
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1
9
4
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1
1
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1
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9
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2
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287380
Uhr
Glycine and serine inhibition ...
Rattus norvegicus
FEBS Lett.
17
137-140
1971
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2
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287381
Kohn
Tartaric acid metabolism. VII. ...
Delftia acidovorans
J. Biol. Chem.
243
2494-2499
1968
5
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1
1
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287382
Kohn
-
Hydroxypyruvate reductase (D-g ...
Delftia acidovorans
Methods Enzymol.
9
229-232
1966
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2
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1
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1
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