5.3.3.2: isopentenyl-diphosphate DELTA-isomerase
This is an abbreviated version!
For detailed information about isopentenyl-diphosphate DELTA-isomerase, go to the full flat file.
Word Map on EC 5.3.3.2
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5.3.3.2
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isoprenoids
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mevalonate
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farnesyl
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geranyl
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geranylgeranyl
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isoprene
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isomerases
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phosphomevalonate
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prenyltransferase
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methylerythritol
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haematococcus
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synthesis
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carbocationic
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1-deoxy-d-xylulose-5-phosphate
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biotechnology
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industry
- 5.3.3.2
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isoprenoids
- mevalonate
-
farnesyl
-
geranyl
-
geranylgeranyl
- isoprene
- isomerases
- phosphomevalonate
- prenyltransferase
- methylerythritol
- haematococcus
- synthesis
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carbocationic
- 1-deoxy-d-xylulose-5-phosphate
- biotechnology
- industry
Reaction
Synonyms
fcd1, FNI, IDI, IDI-1, Idi-2, IDI1, IDP isomerase, IPI, IPI1, IPP isomerase, IPP-isomerase, IPP:DMAPP, IPPI, IPPI1, IPPI2, IPPISOM, Isomerase, isopentenylpyrophosphate DELTA-, Isopententenyl diphosphate:dimethylallyl diphosphate isomerase, isopentenyl diphosphate isomerase, isopentenyl diphosphate isomerase 1, isopentenyl diphosphate:dimethylallyl diphosphate isomerase, Isopentenyl pyrophosphate isomerase, Isopentenyl pyrophosphate isomerase:dimethylallyl pyrophosphate isomerase, isopentenyl-diphosphate delta-isomerase 1, Isopentenyldiphosphate DELTA-isomerase, Isopentenylpyrophosphate isomerase, Methylbutenylpyrophosphate isomerase, SlIPI, type 1 IPP isomerase, type 2 isopentenyl diphosphate isomerase, type 2 isopentenyl diphosphate: dimethylallyl diphosphate isomerase, type 2 isopentenyl diphosphate:dimethylallyl diphosphate isomerase, type 2 isopentenyl-diphosphate isomerase, type I isopentenyl diphosphate isomerase, type II isopentenyl diphosphate isomerase, type II isopentenyl diphosphate:dimethylallyl diphosphate isomerase, type-2 isopentenyl diphosphate isomerase, type-I isopentenyl pyrophosphate isomerase
ECTree
5.3.3.2 isopentenyl-diphosphate DELTA-isomeraseAdvanced search results
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results (Engineering
Engineering on EC 5.3.3.2 - isopentenyl-diphosphate DELTA-isomerase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
E116Q
E87Q
K55A
the ratio of maximal velocity to turnover number is 66% of that of the wild-type enzyme
K55R
the ratio of maximal velocity to turnover number is 28% of that of the wild-type enzyme
R51K
the ratio of maximal velocity to turnover number is 4.2% of that of the wild-type enzyme
R83K
the ratio of maximal velocity to turnover number is 104% of that of the wild-type enzyme
W161F
the ratio of maximal velocity to turnover number is 0.8% of that of the wild-type enzyme
Y104A
0.1% of wild-type activity. Crystallization data. The M2+ metal-binding site is absent in the structure, but Mg2+ is still present and bound to C67, E87, and four water molecules
Y104F
0.1% of wild-type activity. Crystallization data. General fold of enzyme is similar to wild-type
E13R/R235E
the mutant and the wild-type enzyme show similar Vmax values, while the Km of E13R/R235E is smaller than that of the wild type. The mutant is in the tetrameric state even at a concentration where the wild-type enzyme dominantly forms an octamer
Q160E
Q160H
Q160K
Q160L
Q160N
L141H/W256C
the mutations enhance the enzyme activity 1.65fold
L141H/Y195F
the mutations enhance the enzyme activity 2.03fold
L141H/Y195F/W256C
the mutation enhances the enzyme activity 3.13fold
Y195F/W256C
the mutations enhance the enzyme activity 1.14fold
N37A
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the mutant is a monomeric but active enzyme with by 20°C lowered melting temperature and reduced binding affinities of FMN (40fold) and a minimal effect on the kcat value compared to the wild type enzyme
additional information
E116Q
the ratio of maximal velocity to turnover number is 0.09%% of that of the wild-type enzyme
E87Q
the ratio of maximal velocity to turnover number is 0.07% of that of the wild-type enzyme
Q160N
the mutant shows a 150fold decrease in kcat, although kcat/Km only decreases 66fold
additional information
mutants lacking isoform idi1 activity have no major morphological or chemical differences from the wild-type. Mutants lacking both isoforms idi1 and idi2 are non-viable
additional information
mutants lacking isoform idi1 activity have no major morphological or chemical differences from the wild-type. Mutants lacking both isoforms idi1 and idi2 are non-viable
additional information
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mutants lacking isoform idi1 activity have no major morphological or chemical differences from the wild-type. Mutants lacking both isoforms idi1 and idi2 are non-viable
additional information
mutants lacking isoform idi2 activity have no major morphological or chemical differences from the wild-type except for flowers with fused sepals and underdeveloped petals. Mutants lacking both isoforms idi1 and idi2 are non-viable
additional information
mutants lacking isoform idi2 activity have no major morphological or chemical differences from the wild-type except for flowers with fused sepals and underdeveloped petals. Mutants lacking both isoforms idi1 and idi2 are non-viable
additional information
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mutants lacking isoform idi2 activity have no major morphological or chemical differences from the wild-type except for flowers with fused sepals and underdeveloped petals. Mutants lacking both isoforms idi1 and idi2 are non-viable
additional information
mutants lacking isoform ipi1 activity are phenotypically normal. Mutants lacking the activities of both isoforms ipi1 and ipi2 exhibit dwarfism and male sterility under long-day conditions, and decreased pigmentation under continuous light. The sterol and ubiquinone levels of the double mutant are less than 50% of wild-type level. The male-sterile phenotype is complemented by squalene
additional information
mutants lacking isoform ipi1 activity are phenotypically normal. Mutants lacking the activities of both isoforms ipi1 and ipi2 exhibit dwarfism and male sterility under long-day conditions, and decreased pigmentation under continuous light. The sterol and ubiquinone levels of the double mutant are less than 50% of wild-type level. The male-sterile phenotype is complemented by squalene
additional information
mutants lacking isoform ipi2 activity are phenotypically normal. Mutants lacking the activities of both isoforms ipi1 and ipi2 exhibit dwarfism and male sterility under long-day conditions, and decreased pigmentation under continuous light. The sterol and ubiquinone levels of the double mutant are less than 50% of wild-type level. The male-sterile phenotype is complemented by squalene
additional information
mutants lacking isoform ipi2 activity are phenotypically normal. Mutants lacking the activities of both isoforms ipi1 and ipi2 exhibit dwarfism and male sterility under long-day conditions, and decreased pigmentation under continuous light. The sterol and ubiquinone levels of the double mutant are less than 50% of wild-type level. The male-sterile phenotype is complemented by squalene
additional information
functional expression in engineered Escherichia coli restores the carotenoid pathway
additional information
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functional expression in engineered Escherichia coli restores the carotenoid pathway
additional information
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gene IPI can accelerate the accumulation of beta-carotene in Escherichia coli transformants
additional information
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isoform IDI2 can complete isomerase function in an idi1-deficient yeast strain
additional information
recombinant expression in Escherichia coli. Gene IBI can take the role of Arabidopsis thaliana IDI to produce the orange beta-carotene
