BRENDA - Enzyme Database show
show all sequences of 1.1.1.79

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
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, 18C, X-ray diffraction structure determination and analysis at 2.2 A resolution; sitting-drop vapour-diffusipon method. Crystal structure at 2.2 resolution. There are four copies of GRHPR in the crystallographic asymmetric unit: in each homodimer, one subunit forms a ternary (enzyme/NADPH/reduced substrate) complex, and the other a binary (enzyme/NADPH) form. The spatial arrangement of the two enzyme domains is the same in binary and ternary forms
Homo sapiens
Engineering
Amino acid exchange
Commentary
Organism
G160R
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
Homo sapiens
M322R
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
Homo sapiens
Inhibitors
Inhibitors
Commentary
Organism
Structure
D-glycerate
the enzyme shows product inhibition
Homo sapiens
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
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
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
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Homo sapiens
-
-
-
Purification (Commentary)
Commentary
Organism
recombinant enzyme; 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
Source Tissue
Source Tissue
Commentary
Organism
Textmining
liver
; the enzyme plays a critical role in the removal of the metabolic by-product glyoxylate from within the liver. Deficiency of this enzyme is the underlying cause of primary hyperoxaluria type 2 (PH2) and leads to increased urinary oxalate levels, formation of kidney stones and renal failure
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
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
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
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
NADPH
; binding structure
Homo sapiens
Cloned(Commentary) (protein specific)
Commentary
Organism
expression of His-tagged wild-type and mutant enzymes in Escherichia coli
Homo sapiens
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADH
-
Homo sapiens
NADPH
; binding structure
Homo sapiens
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, 18C, X-ray diffraction structure determination and analysis at 2.2 A resolution; sitting-drop vapour-diffusipon method. Crystal structure at 2.2 resolution. There are four copies of GRHPR in the crystallographic asymmetric unit: in each homodimer, one subunit forms a ternary (enzyme/NADPH/reduced substrate) complex, and the other a binary (enzyme/NADPH) form. The spatial arrangement of the two enzyme domains is the same in binary and ternary forms
Homo sapiens
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
G165D
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
Homo sapiens
R302C
site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
Homo sapiens
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
D-glycerate
the enzyme shows product inhibition
Homo sapiens
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
Homo sapiens
the enzyme is involved in removal of the metabolic by-product from liver
glycolate + 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
?
-
-
-
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant enzyme; 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
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
liver
; the enzyme plays a critical role in the removal of the metabolic by-product glyoxylate from within the liver. Deficiency of this enzyme is the underlying cause of primary hyperoxaluria type 2 (PH2) and leads to increased urinary oxalate levels, formation of kidney stones and renal failure
Homo sapiens
-
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
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
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
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 1.1.1.79
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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4
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3
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1
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1
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1
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1
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3
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1
-
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-
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1
1
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-
722899
Ching
Glyoxylate reductase isoform 1 ...
Arabidopsis thaliana
J. Integr. Plant Biol.
54
152-168
2012
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1
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2
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2
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1
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3
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2
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4
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1
4
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2
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2
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3
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2
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2
2
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696125
Allan
Role of plant glyoxylate reduc ...
Arabidopsis thaliana
Biochem. J.
423
15-22
2009
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1
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2
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1
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2
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685774
Ogino
Characterization of recombinan ...
Thermus thermophilus, Thermus thermophilus HB27
Biotechnol. Prog.
24
321-325
2008
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2
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3
8
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1
2
10
2
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2
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5
1
2
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4
8
1
1
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4
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2
4
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3
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8
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1
2
10
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2
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5
1
2
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4
8
1
1
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688090
Simpson
Identification and characteriz ...
Arabidopsis thaliana
J. Exp. Bot.
59
2545-2554
2008
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1
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2
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1
4
2
-
4
4
-
7
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1
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1
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4
15
1
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4
1
1
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2
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2
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2
4
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2
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1
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4
2
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4
4
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1
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1
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4
15
1
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4
1
1
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2
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688091
Allan
Gamma-hydroxybutyrate accumula ...
Arabidopsis thaliana, Nicotiana tabacum
J. Exp. Bot.
59
2555-2564
2008
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2
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2
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5
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5
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2
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7
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2
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2
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2
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2
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5
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2
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7
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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
1
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4
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2
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1
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1
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4
1
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4
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2
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1
2
1
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4
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1
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4
1
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4
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685902
Hoover
Kinetic mechanism of a recombi ...
Arabidopsis thaliana
Can. J. Bot.
85
896-902
2007
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1
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3
2
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1
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1
1
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2
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1
8
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2
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2
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690207
Rintala
The ORF YNL274c (GOR1) codes f ...
Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4742
Yeast
24
129-136
2007
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1
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1
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2
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21
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6
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6
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1
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1
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669886
Booth
Structural basis of substrate ...
Homo sapiens
J. Mol. Biol.
360
178-189
2006
-
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1
1
4
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1
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2
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1
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667814
Mdluli
A preliminary account of the p ...
Homo sapiens
Biochim. Biophys. Acta
1753
209-216
2005
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1
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7
1
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2
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1
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1
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669351
Genolet
Promoter rearrangements cause ...
Homo sapiens, Mus musculus
J. Biol. Chem.
280
24143-24152
2005
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287318
Kleczkowski
-
Kinetics and regulation of the ...
Spinacia oleracea
Z. Naturforsch. C
50
21-28
1995
1
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15
4
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287319
Husic
NADH:hydroxypyruvate reductase ...
Chlamydomonas reinhardtii
Arch. Biochem. Biophys.
252
396-408
1987
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287320
Kleczkowski
Purification and characterizat ...
Glycine max, Spinacia oleracea, Triticum aestivum
Biochem. J.
239
653-659
1986
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1
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1
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287321
Yokota
Purification and some properti ...
Euglena gracilis
Biochem. J.
227
211-216
1985
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4
2
3
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1
1
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3
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1
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1
1
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4
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1
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2
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4
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3
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1
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1
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4
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1
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287322
Mulligan
Effects of glyoxylate on photo ...
Spinacia oleracea
Plant Physiol.
72
415-419
1983
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286409
Yokota
Occurrence and subcellular dis ...
Euglena gracilis
Agric. Biol. Chem.
45
15-22
1981
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1
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1
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1
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1
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1
1
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1
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1
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1
1
4
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1
-
2
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2
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2
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2
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4
-
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1
1
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1
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1
1
4
-
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1
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2
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Fukuda
Purification and enzymatic pro ...
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1980
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4
4
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1
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1
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1
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1
1
3
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1
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2
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1
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1
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4
-
4
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1
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1
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1
1
3
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1
-
2
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Sagisaka
Occurrence of nicotinamide ade ...
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1980
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1
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1
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1
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1
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1
1
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1
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1
1
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2
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2
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1
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-
1
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1
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1
1
-
1
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1
1
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287327
Yokota
Occurrence and properties of t ...
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5
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2
1
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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
3
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1
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2
1
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1
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1
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Tochikura
Purification and properties of ...
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1979
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1
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1
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1
1
5
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1
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1
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2
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2
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10
-
2
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1
1
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1
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1
1
5
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1
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1
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287329
Zeltich
Effect of glycidate, an inhibi ...
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61
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1978
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1
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1
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1
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1
1
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1
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1
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1
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1
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1
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1
1
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1
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