BRENDA - Enzyme Database
show all sequences of 2.7.1.169

Biochemical characterization of pantoate kinase, a novel enzyme necessary for coenzyme A biosynthesis in the Archaea

Tomita, H.; Yokooji, Y.; Ishibashi, T.; Imanaka, T.; Atomi, H.; J. Bacteriol. 194, 5434-5443 (2012)

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
expression in Thermococcus kodakarensis
Thermococcus kodakarensis
Engineering
Protein Variants
Commentary
Organism
D143
residue is the base responsible for proton abstraction from the pantoate hydroxy group
Thermococcus kodakarensis
E134A
residue is involved in binding with Mg2+
Thermococcus kodakarensis
H131A
residue is involved in pantoate recognition. 77% of wild-type activity in presence of 6 mM pantoate and 4 mM ATP
Thermococcus kodakarensis
R155A
residue is involved in pantoate recognition and plays an important role in catalysis
Thermococcus kodakarensis
S104A
residue is involved in binding with phosphate
Thermococcus kodakarensis
S28A
residue is involved in pantoate recognition. 3.7% of wild-type activity in presence of 6 mM pantoate and 4 mM ATP
Thermococcus kodakarensis
T186A
residue is involved in pantoate recognition and plays an important role in catalysis. Thr186 is involved in dimer assambly
Thermococcus kodakarensis
Inhibitors
Inhibitors
Commentary
Organism
Structure
additional information
not inhibitory: CoA, acetyl-CoA
Thermococcus kodakarensis
Pantoate
substrate inhibition
Thermococcus kodakarensis
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.17
-
UTP
pH 7.5, 42°C
Thermococcus kodakarensis
0.32
-
ATP
pH 7.5, 42°C
Thermococcus kodakarensis
0.34
-
CTP
pH 7.5, 42°C
Thermococcus kodakarensis
0.43
-
GTP
pH 7.5, 42°C
Thermococcus kodakarensis
2.92
-
Pantoate
pH 7.5, 42°C
Thermococcus kodakarensis
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
K+
moderate stimulation, optimum at 10 mM
Thermococcus kodakarensis
Mg2+
required
Thermococcus kodakarensis
Organism
Organism
UniProt
Commentary
Textmining
Thermococcus kodakarensis
Q5JHF1
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
ATP + pantoate
reaction displays Michaelis-Menten kinetics toward ATP, whereas substrate inhibition is observed with pantoate
722549
Thermococcus kodakarensis
ADP + 4-phosphopantoate
-
-
-
?
CTP + pantoate
-
722549
Thermococcus kodakarensis
CDP + 4-phosphopantoate
-
-
-
?
GTP + pantoate
-
722549
Thermococcus kodakarensis
GDP + 4-phosphopantoate
-
-
-
?
additional information
enzyme displays broad nucleotide specificity and utilizes ATP, GTP, UTP, and CTP with comparable kcat/Km values
722549
Thermococcus kodakarensis
?
-
-
-
?
UTP + pantoate
-
722549
Thermococcus kodakarensis
UDP + 4-phosphopantoate
-
-
-
?
Synonyms
Synonyms
Commentary
Organism
PoK
-
Thermococcus kodakarensis
TK2141
-
Thermococcus kodakarensis
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
80
-
-
Thermococcus kodakarensis
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.32
-
GTP
pH 7.5, 42°C
Thermococcus kodakarensis
0.47
-
CTP
pH 7.5, 42°C
Thermococcus kodakarensis
1.11
-
UTP
pH 7.5, 42°C
Thermococcus kodakarensis
1.48
-
ATP
pH 7.5, 42°C
Thermococcus kodakarensis
2.82
-
Pantoate
pH 7.5, 42°C
Thermococcus kodakarensis
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
-
Thermococcus kodakarensis
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
9.75
-
Pantoate
pH 7.5, 42°C
Thermococcus kodakarensis
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Thermococcus kodakarensis
Thermococcus kodakarensis
Engineering (protein specific)
Protein Variants
Commentary
Organism
D143
residue is the base responsible for proton abstraction from the pantoate hydroxy group
Thermococcus kodakarensis
E134A
residue is involved in binding with Mg2+
Thermococcus kodakarensis
H131A
residue is involved in pantoate recognition. 77% of wild-type activity in presence of 6 mM pantoate and 4 mM ATP
Thermococcus kodakarensis
R155A
residue is involved in pantoate recognition and plays an important role in catalysis
Thermococcus kodakarensis
S104A
residue is involved in binding with phosphate
Thermococcus kodakarensis
S28A
residue is involved in pantoate recognition. 3.7% of wild-type activity in presence of 6 mM pantoate and 4 mM ATP
Thermococcus kodakarensis
T186A
residue is involved in pantoate recognition and plays an important role in catalysis. Thr186 is involved in dimer assambly
Thermococcus kodakarensis
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
additional information
not inhibitory: CoA, acetyl-CoA
Thermococcus kodakarensis
Pantoate
substrate inhibition
Thermococcus kodakarensis
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
9.75
-
Pantoate
pH 7.5, 42°C
Thermococcus kodakarensis
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.17
-
UTP
pH 7.5, 42°C
Thermococcus kodakarensis
0.32
-
ATP
pH 7.5, 42°C
Thermococcus kodakarensis
0.34
-
CTP
pH 7.5, 42°C
Thermococcus kodakarensis
0.43
-
GTP
pH 7.5, 42°C
Thermococcus kodakarensis
2.92
-
Pantoate
pH 7.5, 42°C
Thermococcus kodakarensis
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
K+
moderate stimulation, optimum at 10 mM
Thermococcus kodakarensis
Mg2+
required
Thermococcus kodakarensis
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
ATP + pantoate
reaction displays Michaelis-Menten kinetics toward ATP, whereas substrate inhibition is observed with pantoate
722549
Thermococcus kodakarensis
ADP + 4-phosphopantoate
-
-
-
?
CTP + pantoate
-
722549
Thermococcus kodakarensis
CDP + 4-phosphopantoate
-
-
-
?
GTP + pantoate
-
722549
Thermococcus kodakarensis
GDP + 4-phosphopantoate
-
-
-
?
additional information
enzyme displays broad nucleotide specificity and utilizes ATP, GTP, UTP, and CTP with comparable kcat/Km values
722549
Thermococcus kodakarensis
?
-
-
-
?
UTP + pantoate
-
722549
Thermococcus kodakarensis
UDP + 4-phosphopantoate
-
-
-
?
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
80
-
-
Thermococcus kodakarensis
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.32
-
GTP
pH 7.5, 42°C
Thermococcus kodakarensis
0.47
-
CTP
pH 7.5, 42°C
Thermococcus kodakarensis
1.11
-
UTP
pH 7.5, 42°C
Thermococcus kodakarensis
1.48
-
ATP
pH 7.5, 42°C
Thermococcus kodakarensis
2.82
-
Pantoate
pH 7.5, 42°C
Thermococcus kodakarensis
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
-
Thermococcus kodakarensis
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.74
-
GTP
pH 7.5, 42°C
Thermococcus kodakarensis
1.4
-
CTP
pH 7.5, 42°C
Thermococcus kodakarensis
2.2
-
ATP
pH 7.5, 42°C
Thermococcus kodakarensis
6.5
-
UTP
pH 7.5, 42°C
Thermococcus kodakarensis
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.74
-
GTP
pH 7.5, 42°C
Thermococcus kodakarensis
1.4
-
CTP
pH 7.5, 42°C
Thermococcus kodakarensis
2.2
-
ATP
pH 7.5, 42°C
Thermococcus kodakarensis
6.5
-
UTP
pH 7.5, 42°C
Thermococcus kodakarensis
Other publictions for EC 2.7.1.169
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
Synonyms
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)
722842
Katoh
Identification of pantoate kin ...
Methanospirillum hungatei
J. Biosci. Bioeng.
115
372-376
2013
-
-
1
-
-
-
1
-
-
8
-
-
-
15
-
-
-
-
-
-
-
-
2
-
2
1
1
-
-
1
1
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
-
-
8
-
-
-
-
-
-
-
-
-
-
2
-
1
1
-
-
1
1
-
-
-
1
1
-
-
-
722549
Tomita
Biochemical characterization o ...
Thermococcus kodakarensis
J. Bacteriol.
194
5434-5443
2012
-
-
1
-
7
-
2
5
-
2
-
-
-
9
-
-
-
-
-
-
-
-
5
-
2
1
-
-
5
1
-
-
-
1
-
-
-
-
1
-
-
7
-
-
2
1
5
-
2
-
-
-
-
-
-
-
-
-
-
5
-
1
-
-
5
1
-
-
-
-
-
-
-
4
4
704547
Yokooji
Pantoate kinase and phosphopan ...
Thermococcus kodakarensis
J. Biol. Chem.
284
28137-28145
2009
-
-
-
-
-
-
2
3
-
-
2
1
-
5
-
-
-
-
-
-
-
-
3
2
2
1
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
3
-
-
2
1
-
-
-
-
-
-
-
-
3
2
1
-
-
3
-
-
-
-
-
1
1
-
3
3