Information on EC 2.7.4.26 - isopentenyl phosphate kinase

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The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria

EC NUMBER
COMMENTARY hide
2.7.4.26
-
RECOMMENDED NAME
GeneOntology No.
isopentenyl phosphate kinase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + isopentenyl phosphate = ADP + isopentenyl diphosphate
show the reaction diagram
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of antibiotics
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Biosynthesis of secondary metabolites
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mevalonate pathway II (archaea)
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mevalonate pathway III (archaea)
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Terpenoid backbone biosynthesis
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mevalonate metabolism
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SYSTEMATIC NAME
IUBMB Comments
ATP:isopentenyl phosphate phosphotransferase
The enzyme is involved in the mevalonate pathway in Archaea [1]. The activity has also been identified in the plant Mentha piperita (peppermint) [2]. It is strictly specific for ATP but can use other phosphate acceptors such as dimethylallyl phosphate, geranyl phosphate, or fosfomycin.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
AtIPK knockout or knockdown affects formation of two of the three predominant Arabidopsis sterols. Similar sterol levels in knockout (ipk1) and knockdown (ipk2) mutants indicate that remaining AtIPK expression in ipk2 supports only marginal flux toward IPP/DMAPP formation without increasing downstream terpenoid production relative to the null ipk knockout. The lack of reduction in stigmasterol levels suggests that the reduced pool of sitosterol, the immediate precursor of stigmasterol, is still sufficient to sustain unaltered production of the latter. In addition, emission of beta-caryophyllene, the most abundant sesquiterpene compound in Arabidopsis is reduced by 25-31% in flowers of ipk mutants compared with wild-type
metabolism
physiological function
IPK may be functionally connected to the mevalonate (MVA) pathway and biosynthesis of downstream terpenoids, including sesquiterpenes, triterpenes, and sterols. Enzyme IPK catalyzes the final step in the formation of isopentanyl diphosphate. Plants IPK plays a role in modulating the formation and pool sizes of farnesyl diphosphate-derived terpenoids. IPK also contributes to formation of geranyl diphosphate-derived terpenoids in plastids
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + (2E,6E)-farnesyl phosphate
ADP + (2E,6E)-farnesyl diphosphate
show the reaction diagram
ATP + but-3-en-1-yl phosphate
ADP + but-3-en-1-yl diphosphate
show the reaction diagram
ATP + butyl phosphate
ADP + butyl diphosphate
show the reaction diagram
ATP + dimethyl allylalcohol
ADP + dimethylallyl phosphate
show the reaction diagram
very low activity
-
-
?
ATP + dimethylallyl alcohol
ADP + dimethylally phophate
show the reaction diagram
ATP + dimethylallyl phosphate
ADP + dimethylallyl diphosphate
show the reaction diagram
ATP + fosfomycin
ADP + ((2R,3S)-3-methyloxiran-2-yl)phosphonic phosphoric anhydride
show the reaction diagram
ATP + geranyl phosphate
ADP + geranyl diphosphate
show the reaction diagram
ATP + isopentenyl phosphate
ADP + isopentenyl diphosphate
show the reaction diagram
ATP + isopentenyl thiolophosphate
ADP + isopentenyl thiolodiphosphate
show the reaction diagram
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 + dimethylallyl phosphate
ADP + dimethylallyl diphosphate
show the reaction diagram
ATP + geranyl phosphate
ADP + geranyl diphosphate
show the reaction diagram
Q8H1F7
low activity
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-
?
ATP + isopentenyl phosphate
ADP + isopentenyl diphosphate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
fosfomycin
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0031 - 0.013
ADP
0.006 - 0.559
ATP
0.0297 - 0.103
but-3-en-1-yl phosphate
0.0263 - 0.173
butyl phosphate
0.033 - 0.174
dimethylallyl phosphate
0.11 - 0.15
fosfomycin
0.22 - 4.7
geranyl phosphate
0.0027 - 0.0076
isopentenyl diphosphate
0.0028 - 0.256
isopentenyl phosphate
0.0145 - 0.0237
isopentenyl thiolophosphate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
16.3
ATP
Haloferax volcanii
D4GWT7
pH 7.5, 30°C
8.07 - 20.5
but-3-en-1-yl phosphate
9.9 - 31.8
butyl phosphate
2.7 - 34
dimethylallyl phosphate
0.03 - 0.04
fosfomycin
0.0039 - 0.047
geranyl phosphate
2.75 - 4.5
isopentenyl diphosphate
0.04 - 330
isopentenyl phosphate
2.84 - 8.22
isopentenyl thiolophosphate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
340 - 1200
ADP
13
1300 - 2200
ATP
4
7.8 - 69
but-3-en-1-yl phosphate
19570
5.7 - 120
butyl phosphate
15671
6.5 - 790
dimethylallyl phosphate
11615
0.0025 - 0.0026
fosfomycin
1153
0.01 - 0.19
geranyl phosphate
9852
1 - 2800
isopentenyl phosphate
4149
200 - 350
isopentenyl thiolophosphate
19569
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8.4
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less than 50% of maximal activity above and below
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55 - 75
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.06
calculated from sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
not in chloroplasts
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Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
26417
x * 26417, His-tagged enzyme, matrix-assisted laser desorption ionization-time of flight mass spectrometry
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
X-ray structure determination
X-ray structure determination
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70
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stable up to
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, dialysis, and ultrafiltration
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli BL21
expression of an N-terminally His-tagged enzyme form in Haloferax volcanii H1209
gene ipk, recombinant expression of His-tagged codon-optimized wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
gene ipk2, analysis of genes coexpressing with AtIPK, At1g26640, overview. Overexpression of gene ipk1 in transgenic tobacco plants
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F83A/I86A/I156A
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the mutant shows a 27% rate of conversion of (2E,6E)-farnesyl phosphate to (2E,6E)-farnesyl diphosphate. The reaction is not catalyzed by the wild-type enzyme
H60Q
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His60 plays a key role in binding and catalysis, the mutant enzyme shows increased values for Km and decreased vaules for kcat and kcat/Km
F83A/I86A/I156A
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the mutant shows a 27% rate of conversion of (2E,6E)-farnesyl phosphate to (2E,6E)-farnesyl diphosphate. The reaction is not catalyzed by the wild-type enzyme
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H60Q
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His60 plays a key role in binding and catalysis, the mutant enzyme shows increased values for Km and decreased vaules for kcat and kcat/Km
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A53V
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme, the mutant shows increased activity compared to the wild-type enzyme
G44A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
G45A
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
G49A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
I140V
site-directed mutagenesis, the mutant shows highly increased activity compared to the wild-type enzyme
K204G
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
V130A
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
V73I
site-directed mutagenesis, the mutant shows highly increased activity compared to the wild-type enzyme
V73I/K204G
site-directed mutagenesis, the mutant shows highly increased activity compared to the wild-type enzyme
V73I/Y141V
site-directed mutagenesis, the mutant shows highly increased activity compared to the wild-type enzyme
V73I/Y141V/K204G
site-directed mutagenesis, the mutant shows highly increased activity compared to the wild-type enzyme
V73T
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
Y141L
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
Y141V
site-directed mutagenesis, the mutant shows highly increased activity compared to the wild-type enzyme
Y141V/K204G
site-directed mutagenesis, the mutant shows highly increased activity compared to the wild-type enzyme
K204A
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kinetic values similar to wild-type
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additional information
Show AA Sequence (371 entries)
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