Literature summary for 2.7.1.169 extracted from

Tomita, H.; Yokooji, Y.; Ishibashi, T.; Imanaka, T.; Atomi, H.
Biochemical characterization of pantoate kinase, a novel enzyme necessary for coenzyme A biosynthesis in the Archaea (2012), J. Bacteriol., 194, 5434-5443.

Search for more literature for 2.7.1.169

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Thermococcus kodakarensis	Thermococcus kodakarensis

Protein Variants

Protein Variants	Comment	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	Comment	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	Comment	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	Comment	Organism	Structure
K+	moderate stimulation, optimum at 10 mM	Thermococcus kodakarensis
Mg2+	required	Thermococcus kodakarensis

Organism

Organism	UniProt	Comment	Textmining
Thermococcus kodakarensis	Q5JHF1	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + pantoate	reaction displays Michaelis-Menten kinetics toward ATP, whereas substrate inhibition is observed with pantoate	Thermococcus kodakarensis	ADP + 4-phosphopantoate	-	?
CTP + pantoate	-	Thermococcus kodakarensis	CDP + 4-phosphopantoate	-	?
GTP + pantoate	-	Thermococcus kodakarensis	GDP + 4-phosphopantoate	-	?
additional information	enzyme displays broad nucleotide specificity and utilizes ATP, GTP, UTP, and CTP with comparable kcat/Km values	Thermococcus kodakarensis	?	-	?
UTP + pantoate	-	Thermococcus kodakarensis	UDP + 4-phosphopantoate	-	?

Synonyms

Synonyms	Comment	Organism
PoK	-	Thermococcus kodakarensis
TK2141	-	Thermococcus kodakarensis

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
80	-	-	Thermococcus kodakarensis

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	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	Comment	Organism
7.5	-	-	Thermococcus kodakarensis

Ki Value [mM]

Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
9.75	-	Pantoate	pH 7.5, 42°C	Thermococcus kodakarensis

kcat/KM [mM/s]

kcat/KM Value [1/mMs^-1]	kcat/KM Value Maximum [1/mMs^-1]	Substrate	Comment	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

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Release 2023.1 (January 2023)