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Information on EC 2.7.4.26 - isopentenyl phosphate kinase
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2.7.4.26 isopentenyl phosphate kinaseIUBMB Comments
The enzyme is involved in the mevalonate pathway in Archaea . The activity has also been identified in the plant Mentha piperita (peppermint) . It is strictly specific for ATP but can use other phosphate acceptors such as prenyl phosphate, geranyl phosphate, or fosfomycin.
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Word Map
- 2.7.4.26
-
isoprenoids
- thermoplasma
- acidophilum
- jannaschii
-
dimethylallyl
-
farnesyl
-
dmapp
- diphosphomevalonate
-
methanocaldococcus
- 1-deoxy-d-xylulose
-
3,5-bisphosphate
- chloroflexi
-
aeropyrum
- eukarya
-
geranyl
- r-mevalonate
- thermautotrophicus
- pernix
-
five-carbon
-
methanothermobacter
- volcanii
-
haloferax
-
triangle
- synthesis
The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria
Synonyms
isopentenyl phosphate kinase, mj0044, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
HvIpk
HVO_2762
IPK
MJ0044
MM_1763
Ta0103
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + isopentenyl phosphate = ADP + isopentenyl diphosphate
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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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 prenyl phosphate, geranyl phosphate, or fosfomycin.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + (2E)-hex-2-en-1-yl phosphate
ADP + (2E)-hex-2-en-1-yl diphosphate
-
-
-
-
?
ATP + (2Z)-hex-2-en-1-yl phosphate
ADP + (2Z)-hex-2-en-1-yl diphosphate
-
-
-
-
?
ATP + 2-methylprop-2-en-1-yl phosphate
ADP + 2-methylprop-2-en-1-yl diphosphate
-
-
-
-
?
ATP + 3-bromobut-3-en-1-yl phosphate
ADP + 3-bromobut-3-en-1-yl diphosphate
-
-
-
-
?
ATP + but-2-yn-1-yl phosphate
ADP + but-2-yn-1-yl diphosphate
-
-
-
-
?
ATP + but-3-yn-1-yl phosphate
ADP + but-3-yn-1-yl diphosphate
-
-
-
-
?
ATP + dimethyl allylalcohol
ADP + dimethylallyl phosphate
very low activity
-
-
?
ATP + hex-5-yn-1-yl phosphate
ADP + hex-5-yn-1-yl diphosphate
-
-
-
-
?
ATP + pent-4-en-1-yl phosphate
ADP + pent-4-en-1-yl diphosphate
-
-
-
-
?
ATP + pent-4-en-2-yl phosphate
ADP + pent-4-en-2-yl diphosphate
-
-
-
-
?
ATP + pent-4-yn-1-yl phosphate
ADP + pent-4-yn-1-yl diphosphate
-
-
-
-
?
additional information
?
-
-
no substrates: geranyl monophosphate, neryl monophosphate, and farnesyl monophosphate
-
-
-
ATP + (2E,6E)-farnesyl phosphate
ADP + (2E,6E)-farnesyl diphosphate
the mutant F83A/I86A/I156A shows a 27% rate of conversion of (2E,6E)-farnesyl phosphate to (2E,6E)-farnesyl diphosphate. This reaction is not catalyzed by the wild-type enzyme
-
-
?
ATP + (2E,6E)-farnesyl phosphate
ADP + (2E,6E)-farnesyl diphosphate
the mutant F83A/I86A/I156A shows a 27% rate of conversion of (2E,6E)-farnesyl phosphate to (2E,6E)-farnesyl diphosphate. This reaction is not catalyzed by the wild-type enzyme
-
-
?
ATP + but-3-en-1-yl phosphate
ADP + but-3-en-1-yl diphosphate
low reaction rate
-
-
?
ATP + but-3-en-1-yl phosphate
ADP + but-3-en-1-yl diphosphate
low reaction rate
-
-
?
ATP + but-3-en-1-yl phosphate
ADP + but-3-en-1-yl diphosphate
-
-
-
-
?
ATP + but-3-en-1-yl phosphate
ADP + but-3-en-1-yl diphosphate
low reaction rate
-
-
?
ATP + butyl phosphate
ADP + butyl diphosphate
low reaction rate
-
-
?
ATP + butyl phosphate
ADP + butyl diphosphate
low reaction rate
-
-
?
ATP + butyl phosphate
ADP + butyl diphosphate
low reaction rate
-
-
?
ATP + dimethylallyl alcohol
ADP + dimethylallyl phosphate
molecular docking analysis indicates that dimethylallyl alcohol is a substrate for the archaeal IPK, although with low activity for thwild-type. The mutant enzymes show increased activity with dimethylallyl alcohol as substrate
-
-
?
ATP + dimethylallyl alcohol
ADP + dimethylallyl phosphate
molecular docking analysis indicates that dimethylallyl alcohol is a substrate for the archaeal IPK, although with low activity for thwild-type. The mutant enzymes show increased activity with dimethylallyl alcohol as substrate
-
-
?
ATP + dimethylallyl alcohol
ADP + dimethylallyl phosphate
molecular docking analysis indicates that dimethylallyl alcohol is a substrate for the archaeal IPK, although with low activity for the wild-type. The mutant enzymes show increased activity with dimethylallyl alcohol as substrate
-
-
?
ATP + dimethylallyl alcohol
ADP + dimethylallyl phosphate
molecular docking analysis indicates that dimethylallyl alcohol is a substrate for the archaeal IPK, although with low activity for the wild-type. The mutant enzymes show increased activity with dimethylallyl alcohol as substrate
-
-
?
ATP + dimethylallyl alcohol
ADP + dimethylallyl phosphate
molecular docking analysis indicates that dimethylallyl alcohol is a substrate for the archaeal IPK, although with low activity for the wild-type. The mutant enzymes show increased activity with dimethylallyl alcohol as substrate
-
-
?
ATP + dimethylallyl phosphate
ADP + dimethylallyl diphosphate
-
-
-
?
ATP + dimethylallyl phosphate
ADP + dimethylallyl diphosphate
-
-
-
?
ATP + dimethylallyl phosphate
ADP + dimethylallyl diphosphate
-
-
-
?
ATP + dimethylallyl phosphate
ADP + dimethylallyl diphosphate
-
-
-
?
ATP + dimethylallyl phosphate
ADP + dimethylallyl diphosphate
low reaction rate
-
-
?
ATP + dimethylallyl phosphate
ADP + dimethylallyl diphosphate
low reaction rate
-
-
?
ATP + dimethylallyl phosphate
ADP + dimethylallyl diphosphate
-
-
-
?
ATP + dimethylallyl phosphate
ADP + dimethylallyl diphosphate
-
-
-
-
?
ATP + dimethylallyl phosphate
ADP + dimethylallyl diphosphate
-
-
-
?
ATP + dimethylallyl phosphate
ADP + dimethylallyl diphosphate
low reaction rate
-
-
?
ATP + fosfomycin
ADP + ((2R,3S)-3-methyloxiran-2-yl)phosphonic phosphoric anhydride
i.e. [(2R,3S)-3-methyl-2-oxiranyl]phosphonic acid
-
-
?
ATP + fosfomycin
ADP + ((2R,3S)-3-methyloxiran-2-yl)phosphonic phosphoric anhydride
i.e. [(2R,3S)-3-methyl-2-oxiranyl]phosphonic acid
-
-
?
ATP + geranyl phosphate
ADP + geranyl diphosphate
low activity
-
-
?
ATP + geranyl phosphate
ADP + geranyl diphosphate
low reaction rate
-
-
?
ATP + geranyl phosphate
ADP + geranyl diphosphate
low reaction rate
-
-
?
ATP + isopentenyl phosphate
ADP + isopentenyl diphosphate
-
-
-
?
ATP + isopentenyl phosphate
ADP + isopentenyl diphosphate
the enzyme is involved in the mevalonate pathway in archaea
-
-
?
ATP + isopentenyl phosphate
ADP + isopentenyl diphosphate
-
-
-
?
ATP + isopentenyl phosphate
ADP + isopentenyl diphosphate
the enzyme is involved in the mevalonate pathway in archaea
-
-
?
ATP + isopentenyl phosphate
ADP + isopentenyl diphosphate
involved in the deoxyxylulose pathway in plants
-
-
?
ATP + isopentenyl phosphate
ADP + isopentenyl diphosphate
strictly specific for ATP, no activity with deoxyxylulose 5-phosphate, deoxyxylulose, 2-C-methylerythritol 4-phosphate
-
-
?
ATP + isopentenyl phosphate
ADP + isopentenyl diphosphate
-
-
-
?
ATP + isopentenyl phosphate
ADP + isopentenyl diphosphate
strictly specific for ATP
-
-
?
ATP + isopentenyl phosphate
ADP + isopentenyl diphosphate
involved in the mevalonate pathway
-
-
?
ATP + isopentenyl phosphate
ADP + isopentenyl diphosphate
-
-
-
?
ATP + isopentenyl phosphate
ADP + isopentenyl diphosphate
strictly specific for ATP
-
-
?
ATP + isopentenyl phosphate
ADP + isopentenyl diphosphate
involved in the mevalonate pathway
-
-
?
ATP + isopentenyl phosphate
ADP + isopentenyl diphosphate
-
-
-
?
ATP + isopentenyl phosphate
ADP + isopentenyl diphosphate
-
-
-
?
ATP + isopentenyl phosphate
ADP + isopentenyl diphosphate
-
-
-
-
?
ATP + isopentenyl phosphate
ADP + isopentenyl diphosphate
-
-
-
?
ATP + isopentenyl phosphate
ADP + isopentenyl diphosphate
-
-
-
r
ATP + isopentenyl phosphate
ADP + isopentenyl diphosphate
-
-
-
?, r
ATP + isopentenyl phosphate
ADP + isopentenyl diphosphate
-
-
-
?
ATP + isopentenyl phosphate
ADP + isopentenyl diphosphate
-
-
-
?
ATP + isopentenyl phosphate
ADP + isopentenyl diphosphate
-
-
-
?, r
ATP + isopentenyl phosphate
ADP + isopentenyl diphosphate
-
-
-
?
ATP + isopentenyl phosphate
ADP + isopentenyl diphosphate
-
-
-
?
ATP + isopentenyl phosphate
ADP + isopentenyl diphosphate
-
-
-
r
ATP + isopentenyl thiolophosphate
ADP + isopentenyl thiolodiphosphate
low reaction rate
-
-
?
ATP + isopentenyl thiolophosphate
ADP + isopentenyl thiolodiphosphate
low reaction rate
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + geranyl phosphate
ADP + geranyl diphosphate
low activity
-
-
?
ATP + dimethylallyl phosphate
ADP + dimethylallyl diphosphate
-
-
-
?
ATP + dimethylallyl phosphate
ADP + dimethylallyl diphosphate
-
-
-
?
ATP + dimethylallyl phosphate
ADP + dimethylallyl diphosphate
-
-
-
?
ATP + dimethylallyl phosphate
ADP + dimethylallyl diphosphate
-
-
-
?
ATP + dimethylallyl phosphate
ADP + dimethylallyl diphosphate
-
-
-
?
ATP + dimethylallyl phosphate
ADP + dimethylallyl diphosphate
-
-
-
?
ATP + isopentenyl phosphate
ADP + isopentenyl diphosphate
-
-
-
?
ATP + isopentenyl phosphate
ADP + isopentenyl diphosphate
the enzyme is involved in the mevalonate pathway in archaea
-
-
?
ATP + isopentenyl phosphate
ADP + isopentenyl diphosphate
the enzyme is involved in the mevalonate pathway in archaea
-
-
?
ATP + isopentenyl phosphate
ADP + isopentenyl diphosphate
involved in the deoxyxylulose pathway in plants
-
-
?
ATP + isopentenyl phosphate
ADP + isopentenyl diphosphate
-
-
-
?
ATP + isopentenyl phosphate
ADP + isopentenyl diphosphate
involved in the mevalonate pathway
-
-
?
ATP + isopentenyl phosphate
ADP + isopentenyl diphosphate
-
-
-
?
ATP + isopentenyl phosphate
ADP + isopentenyl diphosphate
involved in the mevalonate pathway
-
-
?
ATP + isopentenyl phosphate
ADP + isopentenyl diphosphate
-
-
-
?
ATP + isopentenyl phosphate
ADP + isopentenyl diphosphate
-
-
-
?
ATP + isopentenyl phosphate
ADP + isopentenyl diphosphate
-
-
-
-
?
ATP + isopentenyl phosphate
ADP + isopentenyl diphosphate
-
-
-
?
ATP + isopentenyl phosphate
ADP + isopentenyl diphosphate
-
-
-
?
ATP + isopentenyl phosphate
ADP + isopentenyl diphosphate
-
-
-
?
ATP + isopentenyl phosphate
ADP + isopentenyl diphosphate
-
-
-
?
ATP + isopentenyl phosphate
ADP + isopentenyl diphosphate
-
-
-
?
ATP + isopentenyl phosphate
ADP + isopentenyl diphosphate
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.198
ATP
wild-type enzyme, pH 8.0, temperature not specified in the publication
0.559
ATP
mutant H60Q, pH 8.0, temperature not specified in the publication
0.033
dimethylallyl phosphate
pH and temperature not specified in the publication
0.22
geranyl phosphate
pH and temperature not specified in the publication
0.0043
isopentenyl phosphate
wild-type enzyme, pH 8.0, temperature not specified in the publication
0.032
isopentenyl phosphate
pH and temperature not specified in the publication
0.0345
isopentenyl phosphate
mutant H60Q, pH 8.0, temperature not specified in the publication
0.0237
isopentenyl thiolophosphate
pH 7.5, 37°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.7
dimethylallyl phosphate
pH and temperature not specified in the publication
0.0039
geranyl phosphate
pH and temperature not specified in the publication
4.5
isopentenyl diphosphate
pH 7.5, 37°C, reverse reaction
0.04
isopentenyl phosphate
mutant H60Q, pH 8.0, temperature not specified in the publication
1.46
isopentenyl phosphate
wild-type enzyme, pH 8.0, temperature not specified in the publication
3.7
isopentenyl phosphate
pH and temperature not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
85
dimethylallyl phosphate
pH and temperature not specified in the publication
0.018
geranyl phosphate
pH and temperature not specified in the publication
1
isopentenyl phosphate
mutant H60Q, pH 8.0, temperature not specified in the publication
101
isopentenyl phosphate
pH and temperature not specified in the publication
340
isopentenyl phosphate
wild-type enzyme, pH 8.0, temperature not specified in the publication
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 9
7 - 9
less than 50% of maximal activity above and below
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
70
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
55 - 75
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
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
metabolism
the enzyme is involved in the isopentenyl phosphate kinase pathway. The absence of two components of the mevalonate (MVA) pathway from archaeal genomes leads to the discovery of an alternative mevalonate pathway with isopentenyl phosphate kinase (IPK) catalyzing the final step, the formation of isopentenyl diphosphate. Despite the fact that plants contain the complete classical mevalonate pathway, IPK homologues are identified in every sequenced green plant genome. Position and potential role of IPK in the plant terpenoid metabolic network, overview
metabolism
the enzyme is involved in the mevalonate pathway forming the building blocks for isoprenoid biosynthesis, overview
metabolism
the enzyme is involved in the mevalonate pathway forming the building blocks for isoprenoid biosynthesis, overview
metabolism
the enzyme is involved in the mevalonate pathway forming the building blocks for isoprenoid biosynthesis, overview
metabolism
-
the enzyme is involved in the mevalonate pathway forming the building blocks for isoprenoid biosynthesis, overview
-
metabolism
-
the enzyme is involved in the mevalonate pathway forming the building blocks for isoprenoid biosynthesis, overview
-
Show AA Sequence and Transmembrane Helices (3791 entries)
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Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
26417
x * 26417, His-tagged enzyme, matrix-assisted laser desorption ionization-time of flight mass spectrometry
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
?
x * 26417, His-tagged enzyme, matrix-assisted laser desorption ionization-time of flight mass spectrometry
?
-
x * 26417, His-tagged enzyme, matrix-assisted laser desorption ionization-time of flight mass spectrometry
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
X-ray structure determination
catalytically competent structure in complex with Mg2+ . Substrate binding results in significant conformational change of residues Lys204, Glu207, and Lys211 located on the alphaG helix to form a strong salt bridge network with Asp145, which in turn tethers the invariant Ser142 via H-bond interaction. The conformational change shuts the subtrate entrance channel formed between the alphaG and alphaE helices
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F83A/I86A/I156A
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
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
-
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
-
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
-
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
K204A
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
additional information
K204A
site-directed mutagenesis, the mutant shows highly increased activity compared to the wild-type enzyme
additional information
generation of two Arabidopsis T-DNA insertion lines (ipk1, ipk2) by reverse genetics. Quantitative RT-PCR (qRT-PCR) expression analysis with two sets of gene-specific primers, one located upstream of T-DNA insertions and the other downstream near the 3' end of the gene. No AtIPK transcripts are detected in ipk1, whereas transcript levels are reduced by 83% in ipk2, with remaining expression likely a result of residual splicing despite the intron-localized T-DNA insertion. Both ipk1 and ipk2 seedlings show a significant decrease in campesterol and sitosterol content (50% and 37% of wild-type, respectively), while the stigmasterol levels are unchanged
additional information
analysis and evaluation of a method of rational design that is able to identify desired mutants by analyzing the coevolution of protein sequence, use for evolving an archaeal isopentenyl phosphate kinase that can convert dimethylallyl alcohol into precursor of isoprenoids, overview. Site-directed mutagenesis of sites idetified as coevolved in the IPK family proteins
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, dialysis, and ultrafiltration
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, dialysis, and ultrafiltration
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, dialysis, and ultrafiltration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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
gene ipk, recombinant expression of His-tagged codon-optimized wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
gene ipk, recombinant expression of His-tagged codon-optimized wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
gene ipk, recombinant expression of His-tagged codon-optimized wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
expression of genes encoding enzymes of the mevalonate pathway from mevalonate to isopentenyl diphosphate in an engineered Escherichia coli strain that produces red carotinoid pigment lycopene. The archaeal pathway can function in bacterial cells to convert mevalonate into isopentenyl diphosphate
synthesis
-
expression of genes encoding enzymes of the mevalonate pathway from mevalonate to isopentenyl diphosphate in an engineered Escherichia coli strain that produces red carotinoid pigment lycopene. The archaeal pathway can function in bacterial cells to convert mevalonate into isopentenyl diphosphate
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Chen, M.; Poulter, C.D.
Characterization of thermophilic archaeal isopentenyl phosphate kinases.
Biochemistry
49
207-217
2010
Methanothermobacter thermautotrophicus (O26153), Thermoplasma acidophilum (Q9HLX1), Methanothermobacter thermautotrophicus Delta H (O26153)
brenda
Mabanglo, M.F.; Serohijos, A.W.; Poulter, C.D.
The Streptomyces-produced antibiotic fosfomycin is a promiscuous substrate for archaeal isopentenyl phosphate kinase
Biochemistry
52
917-925
2012
Streptomyces wedmorensis (Q56187), Streptomyces wedmorensis, Thermoplasma acidophilum (Q9HLX1), Thermoplasma acidophilum
brenda
Mabanglo, M.F.; Schubert, H.L.; Chen, M.; Hill, C.P.; Poulter, C.D.
X-ray structures of isopentenyl phosphate kinase
Chem. Biol.
5
517-527
2010
Methanothermobacter thermautotrophicus (O26153), Methanothermobacter thermautotrophicus, Thermoplasma acidophilum (Q9HLX1), Thermoplasma acidophilum, Methanothermobacter thermautotrophicus Delta H (O26153)
brenda
Dellas, N.; Noel, J.P.
Mutation of archaeal isopentenyl phosphate kinase highlights mechanism and guides phosphorylation of additional isoprenoid monophosphates
Chem. Biol.
5
589-601
2010
Methanocaldococcus jannaschii (Q60352), Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661 (Q60352)
brenda
Grochowski, L.L.; Xu, H.; White, R.H.
Methanocaldococcus jannaschii uses a modified mevalonate pathway for biosynthesis of isopentenyl diphosphate
J. Bacteriol.
188
3192-3198
2006
Methanocaldococcus jannaschii (Q60352), Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661 (Q60352)
brenda
Lange, B.M., Croteau R.
Isopentenyl diphosphate biosynthesis via a mevalonate-independent pathway: isopentenyl monophosphate kinase catalyzes the terminal enzymatic step
Proc. Natl. Acad. Sci. USA
96
13714-13719
1999
Mentha x piperita (P56848)
brenda
Vannice, J.C.; Skaff, D.A.; Keightley, A.; Addo, J.K.; Wyckoff, G.J.; Miziorko, H.M.
Identification in Haloferax volcanii of phosphomevalonate decarboxylase and isopentenyl phosphate kinase as catalysts of the terminal enzyme reactions in an archaeal alternate mevalonate pathway
J. Bacteriol.
196
1055-1063
2014
Haloferax volcanii (D4GWT7), Haloferax volcanii, Haloferax volcanii DSM 3757 (D4GWT7)
brenda
Henry, L.K.; Gutensohn, M.; Thomas, S.T.; Noel, J.P.; Dudareva, N.
Orthologs of the archaeal isopentenyl phosphate kinase regulate terpenoid production in plants
Proc. Natl. Acad. Sci. USA
112
10050-10055
2015
Arabidopsis thaliana (Q8H1F7)
brenda
Liu, Y.; Yan, Z.; Lu, X.; Xiao, D.; Jiang, H.
Improving the catalytic activity of isopentenyl phosphate kinase through protein coevolution analysis
Sci. Rep.
6
24117
2016
Methanocaldococcus jannaschii (Q60352), Methanocaldococcus jannaschii DSM 2661 (Q60352), Methanothermobacter thermautotrophicus (O26153), Methanothermobacter thermautotrophicus DSM 1053 (O26153), Thermoplasma acidophilum (Q9HLX1)
brenda
Yoshida, R.; Yoshimura, T.; Hemmi, H.
Reconstruction of the ''archaeal'' mevalonate pathway from the methanogenic archaeon Methanosarcina mazei in Escherichia coli cells
Appl. Environ. Microbiol.
86
1-12
2020
Methanosarcina mazei (Q8PW38), Methanosarcina mazei, Methanosarcina mazei DSM 3647 (Q8PW38)
brenda
Lund, S.; Courtney, T.; Williams, G.J.
Probing the substrate promiscuity of isopentenyl phosphate kinase as a platform for hemiterpene analogue production
ChemBioChem
20
2217-2221
2019
Thermoplasma acidophilum
brenda
McClory, J.; Timson, D.J.; Singh, W.; Zhang, J.; Huang, M.
Reaction mechanism of isopentenyl phosphate kinase A QM/MM study
J. Phys. Chem. B
121
11062-11071
2017
Thermoplasma acidophilum (Q9HLX1)
brenda
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