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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
pantoate kinase, mhun_0831, cog1829,
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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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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
reaction displays Michaelis-Menten kinetics toward ATP, whereas substrate inhibition is observed with pantoate
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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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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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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+
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
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
substrate inhibition
additional information
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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no detectable decrase in activity at 0.1 mM: acetyl-CoA, dephospho-CoA, or 4'-phosphopantothenate
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additional information
not inhibitory: CoA, acetyl-CoA
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additional information
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not inhibitory: CoA, acetyl-CoA
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0.32
ATP
pH 7.5, 42°C
1.2
Pantoate
42°C
2.92
Pantoate
pH 7.5, 42°C
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1.48
ATP
42°C
1.56
Pantoate
42°C
2.82
Pantoate
pH 7.5, 42°C
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2.2
ATP
pH 7.5, 42°C
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9.75
Pantoate
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
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
2 * 32748, calculated from sequence
34000
2 * 34000, SDS-PAGE
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dimer
2 * 32748, calculated from sequence; 2 * 34000, SDS-PAGE
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D143
residue is the base responsible for proton abstraction from the pantoate hydroxy group
E134A
residue is involved in binding with Mg2+
H131A
residue is involved in pantoate recognition. 77% of wild-type activity in presence of 6 mM pantoate and 4 mM ATP
R155A
residue is involved in pantoate recognition and plays an important role in catalysis
S104A
residue is involved in binding with phosphate
S28A
residue is involved in pantoate recognition. 3.7% of wild-type activity in presence of 6 mM pantoate and 4 mM ATP
T186A
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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Transporter Classification Database (TCDB):
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2.7.1.169 pantoate kinase
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