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Information on EC 2.7.1.169 - pantoate kinase for references in articles please use BRENDA:EC2.7.1.169
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EC Tree
IUBMB Comments The conversion of (R)-pantoate to (R)-4'-phosphopantothenate is part of the pathway leading to biosynthesis of 4'-phosphopantetheine, an essential cofactor of coenzyme A and acyl-carrier protein. In bacteria and eukaryotes this conversion is performed by condensation with beta-alanine, followed by phosphorylation (EC 6.3.2.1 and EC 2.7.1.33, respectively). In archaea the order of these two steps is reversed, and phosphorylation precedes condensation with beta-alanine.
The enzyme appears in viruses and cellular organisms
Synonyms
COG1829, Mhun_0831, PoK,
TK2141 , TK2141 protein,
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ATP + (R)-pantoate = ADP + (R)-4-phosphopantoate
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ATP:(R)-pantoate 4-phosphotransferase
The conversion of (R)-pantoate to (R)-4'-phosphopantothenate is part of the pathway leading to biosynthesis of 4'-phosphopantetheine, an essential cofactor of coenzyme A and acyl-carrier protein. In bacteria and eukaryotes this conversion is performed by condensation with beta-alanine, followed by phosphorylation (EC 6.3.2.1 and EC 2.7.1.33, respectively). In archaea the order of these two steps is reversed, and phosphorylation precedes condensation with beta-alanine.
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ATP + (R)-pantoate
ADP + (R)-phosphopantoate
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ATP + pantoate
ADP + 4-phosphopantoate
ATP + pantothenate
ADP + 4'-phosphopantothenate
kcat/Km value with pantoate as a substrate is over 7fold higher than that observed with pantothenate
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CTP + pantoate
CDP + 4-phosphopantoate
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GTP + pantoate
GDP + 4-phosphopantoate
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UTP + (R)-pantoate
UDP + (R)-phosphopantoate
52.7% of the activity with ATP
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UTP + pantoate
UDP + 4-phosphopantoate
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additional information
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enzyme displays broad nucleotide specificity and utilizes ATP, GTP, UTP, and CTP with comparable kcat/Km values
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ATP + pantoate
ADP + 4-phosphopantoate
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ATP + pantoate
ADP + 4-phosphopantoate
kcat/Km value with pantoate as a substrate is over 7fold higher than that observed with pantothenate
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ATP + pantoate
ADP + 4-phosphopantoate
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reaction displays Michaelis-Menten kinetics toward ATP, whereas substrate inhibition is observed with pantoate
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ATP + pantoate
ADP + 4-phosphopantoate
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Ca2+
broadly accepts Ca2+, Fe2+, Co2+, Mn2+, Zn2+, or Ni2+ in place of Mg2+
Co2+
broadly accepts Ca2+, Fe2+, Co2+, Mn2+, Zn2+, or Ni2+ in place of Mg2+
Fe2+
broadly accepts Ca2+, Fe2+, Co2+, Mn2+, Zn2+, or Ni2+ in place of Mg2+
K+
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moderate stimulation, optimum at 10 mM
Mn2+
broadly accepts Ca2+, Fe2+, Co2+, Mn2+, Zn2+, or Ni2+ in place of Mg2+
Ni2+
broadly accepts Ca2+, Fe2+, Co2+, Mn2+, Zn2+, or Ni2+ in place of Mg2+
Zn2+
broadly accepts Ca2+, Fe2+, Co2+, Mn2+, Zn2+, or Ni2+ in place of Mg2+
additional information
not accepted: Cu2+
Mg2+
maximum activity in presence of Mg2+
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CoA
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no inhibition in presence of 0.1 mM CoA, activity decrases by 20% in presence of 1 mM CoA
malonyl-CoA
0.2 mM, 83% residual activity
Pantoate
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substrate inhibition
additional information
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no detectable decrase in activity at 0.1 mM: acetyl-CoA, dephospho-CoA, or 4'-phosphopantothenate
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additional information
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not inhibitory: CoA, acetyl-CoA
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0.32
ATP
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pH 7.5, 42°C
1.2
Pantoate
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42°C
2.92
Pantoate
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pH 7.5, 42°C
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1.48
ATP
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42°C
1.56
Pantoate
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42°C
2.82
Pantoate
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pH 7.5, 42°C
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2.2
ATP
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pH 7.5, 42°C
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9.75
Pantoate
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pH 7.5, 42°C
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8 - 9.5
more than 80% of maximum activity
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UniProt
brenda
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UniProt
brenda
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malfunction
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the deletion mutant strain grows well in media supplemented with 1 mM CoA. The deletion mutant strain could not grow at all in the absence of CoA
physiological function
coexpression of genes Mhun_0831 and Mhun_0832 complements the poor growth of the temperature-sensitive Escherichia coli pantothenate kinase mutant ts9. The recombinant Mhun_0831 and Mhun_0832 genes expressed in Escherichia coli cells exhibit pantoate kinase and phosphopantothenate synthetase activities, respectively
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Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
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32748
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2 * 32748, calculated from sequence
34000
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2 * 34000, SDS-PAGE
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dimer
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2 * 32748, calculated from sequence; 2 * 34000, SDS-PAGE
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D143
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residue is the base responsible for proton abstraction from the pantoate hydroxy group
E134A
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residue is involved in binding with Mg2+
H131A
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residue is involved in pantoate recognition. 77% of wild-type activity in presence of 6 mM pantoate and 4 mM ATP
R155A
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residue is involved in pantoate recognition and plays an important role in catalysis
S104A
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residue is involved in binding with phosphate
S28A
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residue is involved in pantoate recognition. 3.7% of wild-type activity in presence of 6 mM pantoate and 4 mM ATP
T186A
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residue is involved in pantoate recognition and plays an important role in catalysis. Thr186 is involved in dimer assambly
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expression in Escherichia coli
expression in Thermococcus kodakarensis
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Yokooji, Y.; Tomita, H.; Atomi, H.; Imanaka, T.
Pantoate kinase and phosphopantothenate synthetase, two novel enzymes necessary for CoA biosynthesis in the archaea
J. Biol. Chem.
284
28137-28145
2009
Thermococcus kodakarensis (Q5JHF1), Thermococcus kodakarensis
brenda
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
J. Bacteriol.
194
5434-5443
2012
Thermococcus kodakarensis (Q5JHF1), Thermococcus kodakarensis
brenda
Katoh, H.; Tamaki, H.; Tokutake, Y.; Hanada, S.; Chohnan, S.
Identification of pantoate kinase and phosphopantothenate synthetase from Methanospirillum hungatei
J. Biosci. Bioeng.
115
372-376
2013
Methanospirillum hungatei (Q2FUB2)
brenda
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Enzyme Nomenclature
2.7.1.169 pantoate kinase
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