Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.7.1.165 extracted from

  • Liu, B.; Hong, Y.; Wu, L.; Li, Z.; Ni, J.; Sheng, D.; Shen, Y.
    A unique highly thermostable 2-phosphoglycerate forming glycerate kinase from the hyperthermophilic archaeon Pyrococcus horikoshii: gene cloning, expression and characterization (2007), Extremophiles, 11, 733-739.
    View publication on PubMed

Activating Compound

Activating Compound Comment 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)

Cloned (Comment) Organism
-
Pyrococcus horikoshii
expressed in Escherichia coli Pyrococcus horikoshii

Inhibitors

Inhibitors Comment 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 Comment Organism Structure
0.044
-
D-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

Metals/Ions Comment Organism Structure
Co2+ 10 mM, 68% of the activity with Mg2+ Pyrococcus horikoshii
K+ 7.94fold increase of activity at 50 mM Pyrococcus horikoshii
K+ 50 mM, 7.9fold activation Pyrococcus horikoshii
Li+ 2.28fold increase of activity at 50 mM Pyrococcus horikoshii
Li+ 50 mM, 2.3fold activation Pyrococcus horikoshii
Mg2+ 10 mM, required for activity 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
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 Pyrococcus horikoshii
Na+ 50 mM, 3.5fold activation Pyrococcus horikoshii
NH4+ 7.83fold increase of activity at 50 mM Pyrococcus horikoshii
NH4+ 50 mM, 7.8fold activation Pyrococcus horikoshii
Ni2+ 10 mM, 11% of the activity with Mg2+ Pyrococcus horikoshii

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
47000
-
SDS-PAGE Pyrococcus horikoshii
47000
-
2 * 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

Organic Solvent Comment 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 UniProt Comment Textmining
Pyrococcus horikoshii
-
-
-
Pyrococcus horikoshii O58231
-
-

Purification (Commentary)

Purification (Comment) 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 Comment Substrates Organism Products Comment (Products) Rev. Reac.
ADP + (R)-glycerate at 32% of the activity with ATP Pyrococcus horikoshii AMP + 3-phospho-(R)-glycerate
-
?
ADP + (R)-glycerate 32% of the activity with ATP Pyrococcus horikoshii AMP + 2-phospho-(R)-glycerate
-
?
ATP + (R)-glycerate
-
Pyrococcus horikoshii ADP + 3-phospho-(R)-glycerate
-
?
ATP + (R)-glycerate
-
Pyrococcus horikoshii ADP + 2-phospho-(R)-glycerate
-
?
ATP + D-glycerate
-
Pyrococcus horikoshii ADP + 2-phospho-D-glycerate
-
?
CTP + (R)-glycerate at 73% of the activity with ATP Pyrococcus horikoshii CDP + 3-phospho-(R)-glycerate
-
?
CTP + (R)-glycerate 73% of the activity with ATP Pyrococcus horikoshii CDP + 2-phospho-(R)-glycerate
-
?
diphosphate + (R)-glycerate at 112% of the activity with ATP Pyrococcus horikoshii phosphate + 3-phospho-(R)-glycerate
-
?
diphosphate + (R)-glycerate 112% of the activity with ATP Pyrococcus horikoshii phosphate + 2-phospho-(R)-glycerate
-
?
GTP + (R)-glycerate at 64% of the activity with ATP Pyrococcus horikoshii GDP + 3-phospho-(R)-glycerate
-
?
GTP + (R)-glycerate 64% of the activity with ATP Pyrococcus horikoshii GDP + 2-phospho-(R)-glycerate
-
?
additional information AMP is not a substrate Pyrococcus horikoshii ?
-
?
UTP + (R)-glycerate at 29% of the activity with ATP Pyrococcus horikoshii UDP + 3-phospho-(R)-glycerate
-
?
UTP + (R)-glycerate 29% of the activity with ATP Pyrococcus horikoshii UDP + 2-phospho-(R)-glycerate
-
?

Subunits

Subunits Comment Organism
dimer 2 * 47000, SDS-PAGE Pyrococcus horikoshii
dimer 2 * 50000, gel filtration Pyrococcus horikoshii

Synonyms

Synonyms Comment Organism
2-PGA forming glycerate kinase
-
Pyrococcus horikoshii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
45
-
-
Pyrococcus horikoshii

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment 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] Comment 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 Comment 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
-
D-glycerate
-
Pyrococcus horikoshii
500.6
-
ATP
-
Pyrococcus horikoshii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
-
Pyrococcus horikoshii

pH Range

pH Minimum pH Maximum Comment Organism
6 10 50% of maximal activity at pH 6.0 and 10.0 Pyrococcus horikoshii

pH Stability

pH Stability pH Stability Maximum Comment Organism
6 10 half of the maximum activity remains at pH 6-10 Pyrococcus horikoshii

Cofactor

Cofactor Comment Organism Structure
ATP
-
Pyrococcus horikoshii