Information on EC 2.7.1.169 - pantoate kinase

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The enzyme appears in viruses and cellular organisms

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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
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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 (archaebacteria)
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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.
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ORGANISM
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LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
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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
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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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?
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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?
GTP + pantoate
GDP + 4-phosphopantoate
show the reaction diagram
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-
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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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?
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METALS and IONS
ORGANISM
UNIPROT
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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
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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
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LITERATURE
IMAGE
0.32 - 0.47
ATP
0.34
CTP
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pH 7.5, 42°C
0.43
GTP
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pH 7.5, 42°C
1.2 - 2.92
Pantoate
1.3
pantothenate
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42°C
0.17
UTP
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pH 7.5, 42°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
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LITERATURE
IMAGE
1.48
ATP
0.47
CTP
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pH 7.5, 42°C
0.32
GTP
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pH 7.5, 42°C
1.56 - 2.82
Pantoate
0.21
pantothenate
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42°C
1.11
UTP
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pH 7.5, 42°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
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LITERATURE
IMAGE
2.2 - 3.1
ATP
1.4
CTP
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pH 7.5, 42°C
0.74
GTP
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pH 7.5, 42°C
1.3
Pantoate
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42°C
0.17
pantothenate
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42°C
6.5
UTP
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pH 7.5, 42°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
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LITERATURE
IMAGE
9.75
Pantoate
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pH 7.5, 42°C
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pH OPTIMUM
ORGANISM
UNIPROT
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LITERATURE
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pH RANGE
ORGANISM
UNIPROT
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LITERATURE
8 - 9.5
more than 80% of maximum activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
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LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
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LITERATURE
60
no residual activity
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
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LITERATURE
32748
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2 * 32748, calculated from sequence
34000
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2 * 34000, SDS-PAGE
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SUBUNITS
ORGANISM
UNIPROT
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LITERATURE
dimer
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2 * 32748, calculated from sequence; 2 * 34000, SDS-PAGE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression in Thermococcus kodakarensis
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ENGINEERING
ORGANISM
UNIPROT
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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
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LINKS TO OTHER DATABASES (specific for EC-Number 2.7.1.169)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)