BRENDA - Enzyme Database show
show all sequences of 2.7.1.165

A unique highly thermostable 2-phosphoglycerate forming glycerate kinase from the hyperthermophilic archaeon Pyrococcus horikoshii: gene cloning, expression and characterization

Liu, B.; Hong, Y.; Wu, L.; Li, Z.; Ni, J.; Sheng, D.; Shen, Y.; Extremophiles 11, 733-739 (2007)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
additional information
50 mM NaN3, 10 mM phenylmethyl sulfonylfluoride, and H2O2 have no obvious effect on the enzymatic activity
Pyrococcus horikoshii
Cloned(Commentary)
Commentary
Organism
; expressed in Escherichia coli
Pyrococcus horikoshii
Inhibitors
Inhibitors
Commentary
Organism
Structure
CuCl2
1 mM, 61% inhibition; 61% inhibition at 1 mM
Pyrococcus horikoshii
HgCl2
11% inhibition at 1 mM; 1 mM, 11% inhibition
Pyrococcus horikoshii
additional information
resistant to the urea, ethanol, 2-propanol, n-butanol and DMSO (10% v/v each)
Pyrococcus horikoshii
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.044
-
glycerate
-
Pyrococcus horikoshii
0.044
-
(R)-glycerate
the reaction mixture contains 1 mM (R)-glycerate, 1 mM ATP, 10 mM MgCl2, 0.3 mM NADH, 1 mM phosphoenolpyruvate, 10 nM purified glycerate kinase, 3.5 units pyruvate kinase and 5 units lactate dehydrogenase in 50 mM potassium phosphate (pH 7.0), at 45°C
Pyrococcus horikoshii
0.102
-
ATP
; the reaction mixture contains 1 mM (R)-glycerate, 1 mM ATP, 10 mM MgCl2, 0.3 mM NADH, 1 mM phosphoenolpyruvate, 10 nM purified glycerate kinase, 3.5 units pyruvate kinase and 5 units lactate dehydrogenase in 50 mM potassium phosphate (pH 7.0), at 45°C
Pyrococcus horikoshii
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Co2+
10 mM, 68% of the activity with Mg2+
Pyrococcus horikoshii
K+
50 mM, 7.9fold activation; 7.94fold increase of activity at 50 mM
Pyrococcus horikoshii
Li+
2.28fold increase of activity at 50 mM; 50 mM, 2.3fold activation
Pyrococcus horikoshii
Mg2+
10 mM, required for activity; no activity is observed in the absence of divalent metal ion and maximal activity is observed in the presence of Mg2+ (10 mM)
Pyrococcus horikoshii
Mn2+
10 mM, 76% of the activity with Mg2+
Pyrococcus horikoshii
additional information
when Mn2+, Co2+, Ca2+, Sr2+ and Ni2+ is substituted for Mg2+, respectively, Mn2+, Co2+ and Ni2+ show 76, 68 and 11% activity of that for Mg2+
Pyrococcus horikoshii
Na+
3.49fold increase of activity at 50 mM; 50 mM, 3.5fold activation
Pyrococcus horikoshii
NH4+
50 mM, 7.8fold activation; 7.83fold increase of activity at 50 mM
Pyrococcus horikoshii
Ni2+
10 mM, 11% of the activity with Mg2+
Pyrococcus horikoshii
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
47000
-
2 * 47000, SDS-PAGE; SDS-PAGE
Pyrococcus horikoshii
47400
-
calculated from amino acid sequence
Pyrococcus horikoshii
50000
-
2 * 50000, gel filtration
Pyrococcus horikoshii
100000
-
gel filtration; gel filtration
Pyrococcus horikoshii
Organic Solvent Stability
Organic Solvent
Commentary
Organism
2-propanol
resistant to
Pyrococcus horikoshii
DMSO
resistant to
Pyrococcus horikoshii
Ethanol
resistant to
Pyrococcus horikoshii
n-Butanol
resistant to
Pyrococcus horikoshii
urea
resistant to
Pyrococcus horikoshii
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Pyrococcus horikoshii
-
-
-
Pyrococcus horikoshii
O58231
-
-
Purification (Commentary)
Commentary
Organism
nickel affinity chromatography, HiTrap Q ion exchange chromatography, and SephacrylTM S-200 HR gel filtration
Pyrococcus horikoshii
Storage Stability
Storage Stability
Organism
90°C, 50 mM Tris-HCl and 100 mM NaCl buffer (pH 8.0), 12 h, almost no loss of activity
Pyrococcus horikoshii
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ADP + (R)-glycerate
at 32% of the activity with ATP
673501
Pyrococcus horikoshii
AMP + 3-phospho-(R)-glycerate
-
-
-
?
ADP + (R)-glycerate
32% of the activity with ATP
673501
Pyrococcus horikoshii
AMP + 2-phospho-(R)-glycerate
-
-
-
?
ATP + (R)-glycerate
-
673501
Pyrococcus horikoshii
ADP + 3-phospho-(R)-glycerate
-
-
-
?
ATP + (R)-glycerate
-
673501
Pyrococcus horikoshii
ADP + 2-phospho-(R)-glycerate
-
-
-
?
CTP + (R)-glycerate
at 73% of the activity with ATP
673501
Pyrococcus horikoshii
CDP + 3-phospho-(R)-glycerate
-
-
-
?
CTP + (R)-glycerate
73% of the activity with ATP
673501
Pyrococcus horikoshii
CDP + 2-phospho-(R)-glycerate
-
-
-
?
diphosphate + (R)-glycerate
at 112% of the activity with ATP
673501
Pyrococcus horikoshii
phosphate + 3-phospho-(R)-glycerate
-
-
-
?
diphosphate + (R)-glycerate
112% of the activity with ATP
673501
Pyrococcus horikoshii
phosphate + 2-phospho-(R)-glycerate
-
-
-
?
GTP + (R)-glycerate
at 64% of the activity with ATP
673501
Pyrococcus horikoshii
GDP + 3-phospho-(R)-glycerate
-
-
-
?
GTP + (R)-glycerate
64% of the activity with ATP
673501
Pyrococcus horikoshii
GDP + 2-phospho-(R)-glycerate
-
-
-
?
additional information
AMP is not a substrate
673501
Pyrococcus horikoshii
?
-
-
-
-
UTP + (R)-glycerate
at 29% of the activity with ATP
673501
Pyrococcus horikoshii
UDP + 3-phospho-(R)-glycerate
-
-
-
?
UTP + (R)-glycerate
29% of the activity with ATP
673501
Pyrococcus horikoshii
UDP + 2-phospho-(R)-glycerate
-
-
-
?
Subunits
Subunits
Commentary
Organism
dimer
2 * 47000, SDS-PAGE; 2 * 50000, gel filtration
Pyrococcus horikoshii
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
45
-
;
Pyrococcus horikoshii
Temperature Range [°C]
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
30
50
strong activity at 30-50°C
Pyrococcus horikoshii
45
100
45°C: optimum, 100°C: about 50% of maximal activity
Pyrococcus horikoshii
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
90
-
12 h, no loss of activity
Pyrococcus horikoshii
100
-
about half of the maximal activity remains at 100°C
Pyrococcus horikoshii
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
360
-
(R)-glycerate
the reaction mixture contains 1 mM (R)-glycerate, 1 mM ATP, 10 mM MgCl2, 0.3 mM NADH, 1 mM phosphoenolpyruvate, 10 nM purified glycerate kinase, 3.5 units pyruvate kinase and 5 units lactate dehydrogenase in 50 mM potassium phosphate (pH 7.0), at 45°C
Pyrococcus horikoshii
489.2
-
glycerate
-
Pyrococcus horikoshii
500.6
-
ATP
-
Pyrococcus horikoshii
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
;
Pyrococcus horikoshii
pH Range
pH Minimum
pH Maximum
Commentary
Organism
6
10
50% of maximal activity at pH 6.0 and 10.0
Pyrococcus horikoshii
pH Stability
pH Stability
pH Stability Maximum
Commentary
Organism
6
10
half of the maximum activity remains at pH 6-10
Pyrococcus horikoshii
Cofactor
Cofactor
Commentary
Organism
Structure
ATP
-
Pyrococcus horikoshii
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
additional information
50 mM NaN3, 10 mM phenylmethyl sulfonylfluoride, and H2O2 have no obvious effect on the enzymatic activity
Pyrococcus horikoshii
Cloned(Commentary) (protein specific)
Commentary
Organism
-
Pyrococcus horikoshii
expressed in Escherichia coli
Pyrococcus horikoshii
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
ATP
-
Pyrococcus horikoshii
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
CuCl2
1 mM, 61% inhibition
Pyrococcus horikoshii
CuCl2
61% inhibition at 1 mM
Pyrococcus horikoshii
HgCl2
1 mM, 11% inhibition
Pyrococcus horikoshii
HgCl2
11% inhibition at 1 mM
Pyrococcus horikoshii
additional information
resistant to the urea, ethanol, 2-propanol, n-butanol and DMSO (10% v/v each)
Pyrococcus horikoshii
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.044
-
glycerate
-
Pyrococcus horikoshii
0.044
-
(R)-glycerate
the reaction mixture contains 1 mM (R)-glycerate, 1 mM ATP, 10 mM MgCl2, 0.3 mM NADH, 1 mM phosphoenolpyruvate, 10 nM purified glycerate kinase, 3.5 units pyruvate kinase and 5 units lactate dehydrogenase in 50 mM potassium phosphate (pH 7.0), at 45°C
Pyrococcus horikoshii
0.102
-
ATP
-
Pyrococcus horikoshii
0.102
-
ATP
the reaction mixture contains 1 mM (R)-glycerate, 1 mM ATP, 10 mM MgCl2, 0.3 mM NADH, 1 mM phosphoenolpyruvate, 10 nM purified glycerate kinase, 3.5 units pyruvate kinase and 5 units lactate dehydrogenase in 50 mM potassium phosphate (pH 7.0), at 45°C
Pyrococcus horikoshii
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Co2+
10 mM, 68% of the activity with Mg2+
Pyrococcus horikoshii
K+
50 mM, 7.9fold activation
Pyrococcus horikoshii
K+
7.94fold increase of activity at 50 mM
Pyrococcus horikoshii
Li+
50 mM, 2.3fold activation
Pyrococcus horikoshii
Li+
2.28fold increase of activity at 50 mM
Pyrococcus horikoshii
Mg2+
no activity is observed in the absence of divalent metal ion and maximal activity is observed in the presence of Mg2+ (10 mM)
Pyrococcus horikoshii
Mg2+
10 mM, required for activity
Pyrococcus horikoshii
Mn2+
10 mM, 76% of the activity with Mg2+
Pyrococcus horikoshii
additional information
when Mn2+, Co2+, Ca2+, Sr2+ and Ni2+ is substituted for Mg2+, respectively, Mn2+, Co2+ and Ni2+ show 76, 68 and 11% activity of that for Mg2+
Pyrococcus horikoshii
Na+
50 mM, 3.5fold activation
Pyrococcus horikoshii
Na+
3.49fold increase of activity at 50 mM
Pyrococcus horikoshii
NH4+
50 mM, 7.8fold activation
Pyrococcus horikoshii
NH4+
7.83fold increase of activity at 50 mM
Pyrococcus horikoshii
Ni2+
10 mM, 11% of the activity with Mg2+
Pyrococcus horikoshii
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
47000
-
2 * 47000, SDS-PAGE
Pyrococcus horikoshii
47000
-
SDS-PAGE
Pyrococcus horikoshii
47400
-
calculated from amino acid sequence
Pyrococcus horikoshii
50000
-
2 * 50000, gel filtration
Pyrococcus horikoshii
100000
-
gel filtration
Pyrococcus horikoshii
Organic Solvent Stability (protein specific)
Organic Solvent
Commentary
Organism
2-propanol
resistant to
Pyrococcus horikoshii
DMSO
resistant to
Pyrococcus horikoshii
Ethanol
resistant to
Pyrococcus horikoshii
n-Butanol
resistant to
Pyrococcus horikoshii
urea
resistant to
Pyrococcus horikoshii
Purification (Commentary) (protein specific)
Commentary
Organism
nickel affinity chromatography, HiTrap Q ion exchange chromatography, and SephacrylTM S-200 HR gel filtration
Pyrococcus horikoshii
Storage Stability (protein specific)
Storage Stability
Organism
90°C, 50 mM Tris-HCl and 100 mM NaCl buffer (pH 8.0), 12 h, almost no loss of activity
Pyrococcus horikoshii
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ADP + (R)-glycerate
at 32% of the activity with ATP
673501
Pyrococcus horikoshii
AMP + 3-phospho-(R)-glycerate
-
-
-
?
ADP + (R)-glycerate
32% of the activity with ATP
673501
Pyrococcus horikoshii
AMP + 2-phospho-(R)-glycerate
-
-
-
?
ATP + (R)-glycerate
-
673501
Pyrococcus horikoshii
ADP + 3-phospho-(R)-glycerate
-
-
-
?
ATP + (R)-glycerate
-
673501
Pyrococcus horikoshii
ADP + 2-phospho-(R)-glycerate
-
-
-
?
CTP + (R)-glycerate
at 73% of the activity with ATP
673501
Pyrococcus horikoshii
CDP + 3-phospho-(R)-glycerate
-
-
-
?
CTP + (R)-glycerate
73% of the activity with ATP
673501
Pyrococcus horikoshii
CDP + 2-phospho-(R)-glycerate
-
-
-
?
diphosphate + (R)-glycerate
at 112% of the activity with ATP
673501
Pyrococcus horikoshii
phosphate + 3-phospho-(R)-glycerate
-
-
-
?
diphosphate + (R)-glycerate
112% of the activity with ATP
673501
Pyrococcus horikoshii
phosphate + 2-phospho-(R)-glycerate
-
-
-
?
GTP + (R)-glycerate
at 64% of the activity with ATP
673501
Pyrococcus horikoshii
GDP + 3-phospho-(R)-glycerate
-
-
-
?
GTP + (R)-glycerate
64% of the activity with ATP
673501
Pyrococcus horikoshii
GDP + 2-phospho-(R)-glycerate
-
-
-
?
additional information
AMP is not a substrate
673501
Pyrococcus horikoshii
?
-
-
-
-
UTP + (R)-glycerate
at 29% of the activity with ATP
673501
Pyrococcus horikoshii
UDP + 3-phospho-(R)-glycerate
-
-
-
?
UTP + (R)-glycerate
29% of the activity with ATP
673501
Pyrococcus horikoshii
UDP + 2-phospho-(R)-glycerate
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
dimer
2 * 47000, SDS-PAGE
Pyrococcus horikoshii
dimer
2 * 50000, gel filtration
Pyrococcus horikoshii
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
45
-
-
Pyrococcus horikoshii
Temperature Range [°C] (protein specific)
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
30
50
strong activity at 30-50°C
Pyrococcus horikoshii
45
100
45°C: optimum, 100°C: about 50% of maximal activity
Pyrococcus horikoshii
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
90
-
12 h, no loss of activity
Pyrococcus horikoshii
100
-
about half of the maximal activity remains at 100°C
Pyrococcus horikoshii
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
360
-
(R)-glycerate
the reaction mixture contains 1 mM (R)-glycerate, 1 mM ATP, 10 mM MgCl2, 0.3 mM NADH, 1 mM phosphoenolpyruvate, 10 nM purified glycerate kinase, 3.5 units pyruvate kinase and 5 units lactate dehydrogenase in 50 mM potassium phosphate (pH 7.0), at 45°C
Pyrococcus horikoshii
489.2
-
glycerate
-
Pyrococcus horikoshii
500.6
-
ATP
-
Pyrococcus horikoshii
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
-
Pyrococcus horikoshii
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
6
10
50% of maximal activity at pH 6.0 and 10.0
Pyrococcus horikoshii
pH Stability (protein specific)
pH Stability
pH Stability Maximum
Commentary
Organism
6
10
half of the maximum activity remains at pH 6-10
Pyrococcus horikoshii
Other publictions for EC 2.7.1.165
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)
739276
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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
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6
1
1
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4
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1
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2
2
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1
3
2
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1
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6
1
1
-
-
4
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-
-
-
-
1
1
-
-
-
722379
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Homo sapiens
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-
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1
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3
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-
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-
-
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1
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2
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1
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1
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3
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2
-
-
1
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
696906
Liu
A MOFRL family glycerate kinas ...
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31
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-
-
1
-
-
1
13
-
-
8
2
2
-
2
-
-
1
-
-
-
-
-
20
1
1
1
1
-
1
1
-
1
-
-
-
-
-
1
1
-
-
1
-
13
-
-
-
8
2
2
-
-
-
1
-
-
-
-
20
1
1
1
1
-
1
1
-
-
-
-
-
-
-
-
686769
Bartsch
Only plant-type (GLYK) glycera ...
Escherichia coli K-12, Synechocystis sp.
FEBS Lett.
582
3025-3028
2008
1
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-
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6
-
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3
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3
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1
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6
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3
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672800
Kehrer
Glycerate kinase of the hypert ...
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