Information on EC 2.7.1.169 - pantoate kinase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.7.1.169
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RECOMMENDED NAME
GeneOntology No.
pantoate kinase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + (R)-pantoate = ADP + (R)-4-phosphopantoate
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
phosphopantothenate biosynthesis III
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pantothenate biosynthesis
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Pantothenate and CoA biosynthesis
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Metabolic pathways
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SYSTEMATIC NAME
IUBMB Comments
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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + (R)-pantoate
ADP + (R)-phosphopantoate
show the reaction diagram
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-
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?
ATP + pantoate
ADP + 4-phosphopantoate
show the reaction diagram
ATP + pantothenate
ADP + 4'-phosphopantothenate
show the reaction diagram
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
show the reaction diagram
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-
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?
GTP + pantoate
GDP + 4-phosphopantoate
show the reaction diagram
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?
UTP + (R)-pantoate
UDP + (R)-phosphopantoate
show the reaction diagram
52.7% of the activity with ATP
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?
UTP + pantoate
UDP + 4-phosphopantoate
show the reaction diagram
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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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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + pantoate
ADP + 4-phosphopantoate
show the reaction diagram
Q5JHF1
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.32 - 0.47
ATP
0.34
CTP
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pH 7.5, 42C
0.43
GTP
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pH 7.5, 42C
1.2 - 2.92
Pantoate
1.3
pantothenate
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42C
0.17
UTP
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pH 7.5, 42C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.48
ATP
0.47
CTP
Thermococcus kodakarensis
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pH 7.5, 42C
0.32
GTP
Thermococcus kodakarensis
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pH 7.5, 42C
1.56 - 2.82
Pantoate
0.21
pantothenate
Thermococcus kodakarensis
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42C
1.11
UTP
Thermococcus kodakarensis
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pH 7.5, 42C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.2 - 3.1
ATP
4
1.4
CTP
Thermococcus kodakarensis
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pH 7.5, 42C
60
0.74
GTP
Thermococcus kodakarensis
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pH 7.5, 42C
37
1.3
Pantoate
Thermococcus kodakarensis
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42C
2576
0.17
pantothenate
Thermococcus kodakarensis
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42C
1509
6.5
UTP
Thermococcus kodakarensis
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pH 7.5, 42C
65
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
9.75
Pantoate
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pH 7.5, 42C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8 - 9.5
more than 80% of maximum activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
no residual activity
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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2 * 32748, calculated from sequence; 2 * 34000, SDS-PAGE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression in Thermococcus kodakarensis
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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