BRENDA - Enzyme Database show
show all sequences of 1.1.1.79

Purification and enzymatic properties of glyoxylate reductase II from baker's yeast

Fukuda, H.; Moriguchi, M.; Tochikura, T.; J. Biochem. 87, 841-846 (1980)

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
iodoacetamide
isoenzyme 2, 1 mM, 87% inhibition, isoenzyme 1, 1 mM, 17% inhibition
Saccharomyces cerevisiae
iodoacetate
isoenzyme 2, 1 mM, 97% inhibition, isoenzyme 1, 1 mM, 18% inhibition
Saccharomyces cerevisiae
N-ethylmaleimide
1 mM, 58% inhibition
Saccharomyces cerevisiae
p-chloromercuribenzoate
isoenzyme 2, 1 mM, complete inhibition, 0.1 mM, 88% inhibition, 29% inhibition in the presence of 1 mM dithiothreitol, 21% inhibition in the presence of 1 mM L-cysteine, isoenzyme 1, 1 mM, 59% inhibition
Saccharomyces cerevisiae
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0057
-
NADPH
-
Saccharomyces cerevisiae
0.43
-
NADH
-
Saccharomyces cerevisiae
1.4
-
Hydroxypyruvate
-
Saccharomyces cerevisiae
16
-
glyoxylate
-
Saccharomyces cerevisiae
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
glyoxylate + NAD(P)H
Saccharomyces cerevisiae
-
glycolate + NAD(P)+
-
Saccharomyces cerevisiae
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Saccharomyces cerevisiae
-
-
-
Purification (Commentary)
Commentary
Organism
isoenzyme 2, protamine sulfate, DEAE-cellulose, hydroxyapatite, Sephadex G-150, phosphocellulose
Saccharomyces cerevisiae
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
61.7
-
isoenzyme 2
Saccharomyces cerevisiae
Storage Stability
Storage Stability
Organism
isoenzyme 2, 4°C, 10 mM, potassium phosphate, pH 7.0, 20% glycerol, 1 week, 10% loss of activity
Saccharomyces cerevisiae
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
glyoxylate + NAD(P)H
-
287325
Saccharomyces cerevisiae
glycolate + NAD(P)+
-
287325
Saccharomyces cerevisiae
?
glyoxylate + NAD(P)H
7% of activity with glyoxylate
287325
Saccharomyces cerevisiae
glycolate + NAD(P)+
-
287325
Saccharomyces cerevisiae
-
hydroxypyruvate + NAD(P)H
-
287325
Saccharomyces cerevisiae
glycerate + NAD(P)+
-
287325
Saccharomyces cerevisiae
?
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
40
-
isoenzyme 2, 90% loss of activity after 5 min, 20% glycerol protects from inactivation, enzyme retains 65% of its activity after 5 min at 40°C
Saccharomyces cerevisiae
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6
6.3
-
Saccharomyces cerevisiae
6
7.5
reduction of hydroxypyruvate
Saccharomyces cerevisiae
Cofactor
Cofactor
Commentary
Organism
Structure
NAD(P)H
-
Saccharomyces cerevisiae
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD(P)H
-
Saccharomyces cerevisiae
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
iodoacetamide
isoenzyme 2, 1 mM, 87% inhibition, isoenzyme 1, 1 mM, 17% inhibition
Saccharomyces cerevisiae
iodoacetate
isoenzyme 2, 1 mM, 97% inhibition, isoenzyme 1, 1 mM, 18% inhibition
Saccharomyces cerevisiae
N-ethylmaleimide
1 mM, 58% inhibition
Saccharomyces cerevisiae
p-chloromercuribenzoate
isoenzyme 2, 1 mM, complete inhibition, 0.1 mM, 88% inhibition, 29% inhibition in the presence of 1 mM dithiothreitol, 21% inhibition in the presence of 1 mM L-cysteine, isoenzyme 1, 1 mM, 59% inhibition
Saccharomyces cerevisiae
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0057
-
NADPH
-
Saccharomyces cerevisiae
0.43
-
NADH
-
Saccharomyces cerevisiae
1.4
-
Hydroxypyruvate
-
Saccharomyces cerevisiae
16
-
glyoxylate
-
Saccharomyces cerevisiae
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
Saccharomyces cerevisiae
-
glycolate + NAD(P)+
-
Saccharomyces cerevisiae
?
Purification (Commentary) (protein specific)
Commentary
Organism
isoenzyme 2, protamine sulfate, DEAE-cellulose, hydroxyapatite, Sephadex G-150, phosphocellulose
Saccharomyces cerevisiae
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
61.7
-
isoenzyme 2
Saccharomyces cerevisiae
Storage Stability (protein specific)
Storage Stability
Organism
isoenzyme 2, 4°C, 10 mM, potassium phosphate, pH 7.0, 20% glycerol, 1 week, 10% loss of activity
Saccharomyces cerevisiae
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
glyoxylate + NAD(P)H
-
287325
Saccharomyces cerevisiae
glycolate + NAD(P)+
-
287325
Saccharomyces cerevisiae
?
glyoxylate + NAD(P)H
7% of activity with glyoxylate
287325
Saccharomyces cerevisiae
glycolate + NAD(P)+
-
287325
Saccharomyces cerevisiae
-
hydroxypyruvate + NAD(P)H
-
287325
Saccharomyces cerevisiae
glycerate + NAD(P)+
-
287325
Saccharomyces cerevisiae
?
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
40
-
isoenzyme 2, 90% loss of activity after 5 min, 20% glycerol protects from inactivation, enzyme retains 65% of its activity after 5 min at 40°C
Saccharomyces cerevisiae
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6
6.3
-
Saccharomyces cerevisiae
6
7.5
reduction of hydroxypyruvate
Saccharomyces cerevisiae
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
-
-
-
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
-
-
2
-
-
-
3
8
-
-
1
2
10
2
-
-
2
-
-
-
-
-
5
1
2
-
4
8
1
1
-
4
-
-
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-
-
2
4
-
-
-
-
3
-
8
-
-
1
2
10
-
-
2
-
-
-
-
5
1
2
-
4
8
1
1
-
-
-
-
-
-
-
-
688090
Simpson
Identification and characteriz ...
Arabidopsis thaliana
J. Exp. Bot.
59
2545-2554
2008
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-
1
-
2
-
1
4
2
-
4
4
-
7
-
-
1
-
-
1
-
4
15
1
-
-
-
4
1
1
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2
-
2
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-
2
4
-
2
-
-
1
-
4
2
-
4
4
-
-
-
1
-
1
-
4
15
1
-
-
-
4
1
1
-
2
-
-
-
-
-
-
688091
Allan
Gamma-hydroxybutyrate accumula ...
Arabidopsis thaliana, Nicotiana tabacum
J. Exp. Bot.
59
2555-2564
2008
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-
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-
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2
-
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
-
-
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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1
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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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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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1
1
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8
2
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1
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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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3
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6
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1
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1
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1
2
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1
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2
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3
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6
-
1
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1
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-
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669886
Booth
Structural basis of substrate ...
Homo sapiens
J. Mol. Biol.
360
178-189
2006
-
-
1
1
4
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1
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3
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2
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1
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2
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1
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4
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2
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5
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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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8
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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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4
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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1
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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
1
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1
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1
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1
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15
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4
1
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1
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1
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1
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287319
Husic
NADH:hydroxypyruvate reductase ...
Chlamydomonas reinhardtii
Arch. Biochem. Biophys.
252
396-408
1987
-
-
-
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1
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1
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1
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1
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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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4
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2
3
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3
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1
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1
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1
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3
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3
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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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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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1
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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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287324
Fukuda
Purification and properties of ...
Neurospora crassa
Agric. Biol. Chem.
45
1153-1158
1981
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2
4
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1
1
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1
4
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1
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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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-
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287325
Fukuda
Purification and enzymatic pro ...
Saccharomyces cerevisiae
J. Biochem.
87
841-846
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
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4
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-
1
-
-
-
1
-
-
1
1
3
-
-
-
1
-
2
-
-
-
-
-
-
-
-
-
287326
Sagisaka
Occurrence of nicotinamide ade ...
Populus gelrica
Plant Physiol.
65
377-381
1980
-
-
-
-
-
-
-
1
-
-
-
1
-
1
-
-
1
-
-
1
1
-
1
-
-
-
-
-
1
1
-
2
-
-
-
-
-
-
2
-
-
-
-
-
-
1
-
-
-
1
-
-
-
1
-
1
1
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
287327
Yokota
Occurrence and properties of t ...
Euglena gracilis
Biochem. J.
184
189-192
1979
-
-
-
-
-
-
-
2
3
-
-
1
-
5
-
-
-
-
-
2
1
-
1
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
2
3
-
-
1
-
-
-
-
-
2
1
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
287328
Tochikura
Purification and properties of ...
Saccharomyces cerevisiae
J. Biochem.
86
105-110
1979
-
-
-
-
-
-
10
2
-
-
1
1
-
1
-
-
1
-
-
-
1
1
5
-
-
-
1
-
1
-
-
2
-
-
-
-
-
-
2
-
-
-
-
10
-
2
-
-
1
1
-
-
-
1
-
-
1
1
5
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
287329
Zeltich
Effect of glycidate, an inhibi ...
Nicotiana tabacum
Plant Physiol.
61
236-241
1978
-
-
-
-
-
-
1
-
-
-
-
1
-
1
-
-
-
-
-
1
1
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
1
-
-
-
-
-
1
-
-
-
-
-
1
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-