2.7.4.26: isopentenyl phosphate kinase
This is an abbreviated version!
For detailed information about isopentenyl phosphate kinase, go to the full flat file.
Word Map on EC 2.7.4.26
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2.7.4.26
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isoprenoids
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thermoplasma
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acidophilum
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jannaschii
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dimethylallyl
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farnesyl
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dmapp
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diphosphomevalonate
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methanocaldococcus
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1-deoxy-d-xylulose
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3,5-bisphosphate
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chloroflexi
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aeropyrum
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eukarya
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geranyl
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r-mevalonate
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thermautotrophicus
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pernix
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five-carbon
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methanothermobacter
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volcanii
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haloferax
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triangle
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synthesis
- 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
Reaction
Synonyms
HvIpk, HVO_2762, IPK, Ipk2, isopentenyl phosphate kinase, MJ0044, MM_1763, Ta0103
ECTree
Advanced search results
Engineering
Engineering on EC 2.7.4.26 - isopentenyl phosphate kinase
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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
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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
-
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
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
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