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Information on EC 5.3.3.2 - isopentenyl-diphosphate DELTA-isomerase for references in articles please use BRENDA:EC5.3.3.2
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EC Tree
IUBMB Comments The enzyme from Streptomyces sp. strain CL190 requires FMN and NAD(P)H as cofactors. Activity is reduced if FMN is replaced by FAD, but the enzyme becomes inactive when NAD(P)H is replaced by NAD+ or NADP+. That enzyme also requires Mg2+, Mn2+ or Ca2+ for activity.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
ipp isomerase, isopentenyl diphosphate isomerase, idi-2, isopentenyl pyrophosphate isomerase, idi-1, slipi, isopentenyl diphosphate:dimethylallyl diphosphate isomerase, type 2 isopentenyl diphosphate isomerase, type ii isopentenyl diphosphate:dimethylallyl diphosphate isomerase, idp isomerase,
more
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Isomerase, isopentenylpyrophosphate DELTA-
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Isopententenyl diphosphate:dimethylallyl diphosphate isomerase
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isopentenyl diphosphate isomerase
isopentenyl diphosphate isomerase 1
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isopentenyl diphosphate:dimethylallyl diphosphate isomerase
Isopentenyl pyrophosphate isomerase
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Isopentenyl pyrophosphate isomerase:dimethylallyl pyrophosphate isomerase
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isopentenyl-diphosphate delta-isomerase 1
Isopentenyldiphosphate DELTA-isomerase
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Isopentenylpyrophosphate isomerase
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Methylbutenylpyrophosphate isomerase
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type 2 isopentenyl diphosphate isomerase
type 2 isopentenyl diphosphate: dimethylallyl diphosphate isomerase
type 2 isopentenyl diphosphate:dimethylallyl diphosphate isomerase
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type 2 isopentenyl-diphosphate isomerase
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type I isopentenyl diphosphate isomerase
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type II isopentenyl diphosphate isomerase
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type II isopentenyl diphosphate:dimethylallyl diphosphate isomerase
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type-2 isopentenyl diphosphate isomerase
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type-I isopentenyl pyrophosphate isomerase
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IDI
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Idi-2
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IDI1
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IPI
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IPP isomerase
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IPPI
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IPPI1
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IPPISOM
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IPPISOM
Vitis vinifera x Vitis vinifera
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isopentenyl diphosphate isomerase
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isopentenyl diphosphate isomerase
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isopentenyl diphosphate isomerase
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isopentenyl diphosphate isomerase
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isopentenyl diphosphate isomerase
A0A067K3N5
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isopentenyl diphosphate isomerase
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isopentenyl diphosphate isomerase
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isopentenyl diphosphate isomerase
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isopentenyl diphosphate isomerase
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isopentenyl diphosphate isomerase
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isopentenyl diphosphate isomerase
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isopentenyl diphosphate isomerase
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isopentenyl diphosphate isomerase
A9LRT7
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isopentenyl diphosphate isomerase
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isopentenyl diphosphate isomerase
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isopentenyl diphosphate isomerase
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isopentenyl diphosphate:dimethylallyl diphosphate isomerase
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isopentenyl diphosphate:dimethylallyl diphosphate isomerase
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isopentenyl-diphosphate delta-isomerase 1
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isopentenyl-diphosphate delta-isomerase 1
Vitis vinifera x Vitis vinifera
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type 2 isopentenyl diphosphate isomerase
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type 2 isopentenyl diphosphate isomerase
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type 2 isopentenyl diphosphate: dimethylallyl diphosphate isomerase
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type 2 isopentenyl diphosphate: dimethylallyl diphosphate isomerase
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Isopentenyl diphosphate = dimethylallyl diphosphate
Isopentenyl diphosphate = dimethylallyl diphosphate
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Isopentenyl diphosphate = dimethylallyl diphosphate
catalytic mechanism in which a cysteine initiates the reaction by protonating the carbon-carbon double bond, with the antarafacial rearrangement ultimately achieved by one of the glutamates involved in the metal coordination sphere
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Isopentenyl diphosphate = dimethylallyl diphosphate
reaction involves protonation and deprotonation of the isoprenoid unit and proceeds through a carbocationic transition state. Glu116/Tyr104 and Cys67 are involved in the antarafacial addition/elimination of protons during isomerization
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Isopentenyl diphosphate = dimethylallyl diphosphate
the mechanism of isomerizaion reaction involves protonation of the unactivated carbon-carbon double bond in the substrate, Glu116 is involved in the protonation step and Cys67 is involved in the elimination step
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Isopentenyl diphosphate = dimethylallyl diphosphate
interconversion of substrate is catalyzed by a stereoselective antarafacial [1.3] transposition of a proton involving residues C87, E149, W197 and Y137
Isopentenyl diphosphate = dimethylallyl diphosphate
in the rate determining step, the C2-H bond of isopentenyl diphosphate is cleaved. General acid/base catalysis may be involved during turnover
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intramolecular oxidoreduction
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isomerization
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MetaCyc
all-trans-farnesol biosynthesis , bisabolene biosynthesis (engineered) , isoprene biosynthesis II (engineered) , methylerythritol phosphate pathway I , methylerythritol phosphate pathway II , mevalonate pathway I , mevalonate pathway II (archaea) , mevalonate pathway III (archaea) , mono-trans, poly-cis decaprenyl phosphate biosynthesis , trans, trans-farnesyl diphosphate biosynthesis
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isopentenyl-diphosphate DELTA3-DELTA2-isomerase
The enzyme from Streptomyces sp. strain CL190 requires FMN and NAD(P)H as cofactors. Activity is reduced if FMN is replaced by FAD, but the enzyme becomes inactive when NAD(P)H is replaced by NAD+ or NADP+. That enzyme also requires Mg2+, Mn2+ or Ca2+ for activity.
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(Z)-3-(difluoromethyl)-2-buten-1-yl diphosphate
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about 2% of the activity with isopenteyl diphosphate
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(Z)-3-(fluoromethyl)-2-buten-1-yl diphosphate
?
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about 2% of the activity with isopenteyl diphosphate
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3-(fluoromethyl)-3-buten-1-yl diphosphate
?
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competition between isomerization and alkylation of the flavin cofactor
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?
3-cyclopropyl-3-buten-1-yl diphosphate
(2Z)-3-cyclopropylbut-2-en-1-yl diphosphate
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r
3-Ethylbut-3-enyl diphosphate
trans-3-Methylpent-3-enyl diphosphate
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ir
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3-methylene-4-penten-1-yl diphosphate
?
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competition between isomerization and alkylation of the flavin cofactor
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?
Isopentenyl diphosphate
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isopentenyl diphosphate
dimethylallyl diphosphate
isopentenyl diphosphate
dimethylallyl phosphate
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?
pyruvate
lactate
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?
trans-3-Methylpent-3-enyl diphosphate
trans-3-Methylpent-2-enyl diphosphate
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r
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additional information
?
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Isopentenyl diphosphate
?
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essential activation step in isoprenoid biosynthetic pathway
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Isopentenyl diphosphate
?
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Isopentenyl diphosphate
?
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isopentenyl diphosphate
dimethylallyl diphosphate
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isopentenyl diphosphate
dimethylallyl diphosphate
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?
isopentenyl diphosphate
dimethylallyl diphosphate
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steady-state equilibrium ratio of isopentenyl diphosphate/dimethylallyl diphosphate of approximately 1:7
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r
isopentenyl diphosphate
dimethylallyl diphosphate
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r
isopentenyl diphosphate
dimethylallyl diphosphate
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r
isopentenyl diphosphate
dimethylallyl diphosphate
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isopentenyl diphosphate
dimethylallyl diphosphate
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isopentenyl diphosphate
dimethylallyl diphosphate
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?
isopentenyl diphosphate
dimethylallyl diphosphate
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?
isopentenyl diphosphate
dimethylallyl diphosphate
Cinchona robusta
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r
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isopentenyl diphosphate
dimethylallyl diphosphate
Citrus sp.
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isopentenyl diphosphate
dimethylallyl diphosphate
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isopentenyl diphosphate
dimethylallyl diphosphate
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isopentenyl diphosphate
dimethylallyl diphosphate
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isopentenyl diphosphate
dimethylallyl diphosphate
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isopentenyl diphosphate
dimethylallyl diphosphate
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isopentenyl diphosphate
dimethylallyl diphosphate
Cucurbita sp.
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isopentenyl diphosphate
dimethylallyl diphosphate
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?
isopentenyl diphosphate
dimethylallyl diphosphate
-
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?
isopentenyl diphosphate
dimethylallyl diphosphate
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r
isopentenyl diphosphate
dimethylallyl diphosphate
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?
isopentenyl diphosphate
dimethylallyl diphosphate
the enzyme catalyzes a crucial activation step in the isoprenoid biosynthesis pathway
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?
isopentenyl diphosphate
dimethylallyl diphosphate
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isopentenyl diphosphate
dimethylallyl diphosphate
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isopentenyl diphosphate
dimethylallyl diphosphate
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isopentenyl diphosphate
dimethylallyl diphosphate
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isopentenyl diphosphate
dimethylallyl diphosphate
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isopentenyl diphosphate
dimethylallyl diphosphate
-
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isopentenyl diphosphate
dimethylallyl diphosphate
-
-
-
-
?
isopentenyl diphosphate
dimethylallyl diphosphate
-
-
-
?
isopentenyl diphosphate
dimethylallyl diphosphate
A0A067K3N5
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-
?
isopentenyl diphosphate
dimethylallyl diphosphate
-
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-
r
isopentenyl diphosphate
dimethylallyl diphosphate
-
-
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?
isopentenyl diphosphate
dimethylallyl diphosphate
-
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isopentenyl diphosphate
dimethylallyl diphosphate
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-
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?
isopentenyl diphosphate
dimethylallyl diphosphate
-
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?
isopentenyl diphosphate
dimethylallyl diphosphate
-
the enzyme catalyzes the interconversion of the fundamental five carbon homoallylic and allylic diphosphate building blocks required for biosynthesis of isoprenoid compounds
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?
isopentenyl diphosphate
dimethylallyl diphosphate
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isopentenyl diphosphate
dimethylallyl diphosphate
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isopentenyl diphosphate
dimethylallyl diphosphate
-
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isopentenyl diphosphate
dimethylallyl diphosphate
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-
?
isopentenyl diphosphate
dimethylallyl diphosphate
-
-
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isopentenyl diphosphate
dimethylallyl diphosphate
-
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isopentenyl diphosphate
dimethylallyl diphosphate
-
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-
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isopentenyl diphosphate
dimethylallyl diphosphate
-
-
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?
isopentenyl diphosphate
dimethylallyl diphosphate
-
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isopentenyl diphosphate
dimethylallyl diphosphate
-
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-
?
isopentenyl diphosphate
dimethylallyl diphosphate
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?
isopentenyl diphosphate
dimethylallyl diphosphate
-
a mechanism is proposed where the reduced flavin cofactor acts as a general acid/base catalyst and helps stabilize the carbocationic intermediate formed by protonation
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?
isopentenyl diphosphate
dimethylallyl diphosphate
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isopentenyl diphosphate
dimethylallyl diphosphate
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isopentenyl diphosphate
dimethylallyl diphosphate
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isopentenyl diphosphate
dimethylallyl diphosphate
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isopentenyl diphosphate
dimethylallyl diphosphate
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isopentenyl diphosphate
dimethylallyl diphosphate
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isopentenyl diphosphate
dimethylallyl diphosphate
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isopentenyl diphosphate
dimethylallyl diphosphate
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?
isopentenyl diphosphate
dimethylallyl diphosphate
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r
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isopentenyl diphosphate
dimethylallyl diphosphate
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the enzyme catalyses the interconversion of isopentenyl diphosphate and dimethylallyl diphosphate with a rather low degree of stereochemical fidelity. At least three kinetically distinguishable exchange processes are detected
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isopentenyl diphosphate
dimethylallyl diphosphate
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r
isopentenyl diphosphate
dimethylallyl diphosphate
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isopentenyl diphosphate
dimethylallyl diphosphate
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isopentenyl diphosphate
dimethylallyl diphosphate
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isopentenyl diphosphate
dimethylallyl diphosphate
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isopentenyl diphosphate
dimethylallyl diphosphate
-
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r
isopentenyl diphosphate
dimethylallyl diphosphate
A9LRT7
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r
isopentenyl diphosphate
dimethylallyl diphosphate
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?
isopentenyl diphosphate
dimethylallyl diphosphate
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r
isopentenyl diphosphate
dimethylallyl diphosphate
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accumulation of a reduced neutral dihydroflavin intermediate upon incubation of the reduced enzyme with isopentenyl diphosphate or dimethylallyl diphosphate. The intermediate forms and decays at kinetically competent rates in the pre-steady-state
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r
isopentenyl diphosphate
dimethylallyl diphosphate
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?
isopentenyl diphosphate
dimethylallyl diphosphate
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r
isopentenyl diphosphate
dimethylallyl diphosphate
-
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r
isopentenyl diphosphate
dimethylallyl diphosphate
-
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r
isopentenyl diphosphate
dimethylallyl diphosphate
-
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isopentenyl diphosphate
dimethylallyl diphosphate
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isopentenyl diphosphate
dimethylallyl diphosphate
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isopentenyl diphosphate
dimethylallyl diphosphate
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?
isopentenyl diphosphate
dimethylallyl diphosphate
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?
isopentenyl diphosphate
dimethylallyl diphosphate
-
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r
isopentenyl diphosphate
dimethylallyl diphosphate
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?
isopentenyl diphosphate
dimethylallyl diphosphate
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r
additional information
?
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Cinchona robusta
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induced after addition of a homogenate of the phytopathogenic fungus Phytophthora cinnamomi. Enzyme may be involved in the biosynthesis of anthraquinone phytoalexins that accumulate rapidly after elicitation of Cinchona cells
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additional information
?
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zinc is located in an unusual six-coordinate pocket and may facilitate protonation of the unactivated carbon-carbon double bond in isopentenyl diphosphate. The sulfhydryl moiety C67, perhaps in the thiolate form, is in position to remove a proton from the resulting tertiary carbocation to complete the reaction
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?
additional information
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key enzyme in biosynthesis of isoprenoids
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?
additional information
?
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key enzyme in biosynthesis of isoprenoids
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?
additional information
?
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3-butyn-1-yl diphosphate and 2,3-butadien-1-yl diphosphate are no substrates for IDI-1
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additional information
?
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enzyme in the pathway of conversion of isopentenyl diphosphate to phytoene
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additional information
?
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enzyme of the isoprenoid pathway
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additional information
?
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the enzyme also has NADH dehydrogenase activity although it catalyzes the isomerase reaction without consuming any detectable amount of NADH. O2 acts as electron acceptor in the NADH dehydrogenase reaction
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?
additional information
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the enzyme also has NADH dehydrogenase activity although it catalyzes the isomerase reaction without consuming any detectable amount of NADH. O2 acts as electron acceptor in the NADH dehydrogenase reaction
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?
additional information
?
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enzyme in the pathway of conversion of isopentenyl diphosphate to phytoene
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additional information
?
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substrate binds to the inactive oxidized and active reduced form of enzyme with similar affinities. Substrate-dependent accumulation of the neutral flavin semiquinone during both the flavoenzyme reduction and reoxidation processes
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additional information
?
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3-butyn-1-yl diphosphate and 2,3-butadien-1-yl diphosphate are no substrates for IDI-2
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additional information
?
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ìsoform IDI-2 catalyzes exchange of the vinyl hydrogens in 1-OPP without concomitant isomerization
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Isopentenyl diphosphate
?
isopentenyl diphosphate
dimethylallyl diphosphate
additional information
?
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Isopentenyl diphosphate
?
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essential activation step in isoprenoid biosynthetic pathway
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Isopentenyl diphosphate
?
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Isopentenyl diphosphate
?
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isopentenyl diphosphate
dimethylallyl diphosphate
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?
isopentenyl diphosphate
dimethylallyl diphosphate
-
steady-state equilibrium ratio of isopentenyl diphosphate/dimethylallyl diphosphate of approximately 1:7
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r
isopentenyl diphosphate
dimethylallyl diphosphate
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isopentenyl diphosphate
dimethylallyl diphosphate
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?
isopentenyl diphosphate
dimethylallyl diphosphate
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?
isopentenyl diphosphate
dimethylallyl diphosphate
Q46822
the enzyme catalyzes a crucial activation step in the isoprenoid biosynthesis pathway
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?
isopentenyl diphosphate
dimethylallyl diphosphate
Q13907
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?
isopentenyl diphosphate
dimethylallyl diphosphate
A0A067K3N5
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?
isopentenyl diphosphate
dimethylallyl diphosphate
A0A067ZIC8
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r
isopentenyl diphosphate
dimethylallyl diphosphate
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?
isopentenyl diphosphate
dimethylallyl diphosphate
-
the enzyme catalyzes the interconversion of the fundamental five carbon homoallylic and allylic diphosphate building blocks required for biosynthesis of isoprenoid compounds
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?
isopentenyl diphosphate
dimethylallyl diphosphate
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isopentenyl diphosphate
dimethylallyl diphosphate
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isopentenyl diphosphate
dimethylallyl diphosphate
P61615
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isopentenyl diphosphate
dimethylallyl diphosphate
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isopentenyl diphosphate
dimethylallyl diphosphate
P15496
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isopentenyl diphosphate
dimethylallyl diphosphate
H6VLF2
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r
isopentenyl diphosphate
dimethylallyl diphosphate
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r
isopentenyl diphosphate
dimethylallyl diphosphate
A9LRT7
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r
isopentenyl diphosphate
dimethylallyl diphosphate
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r
isopentenyl diphosphate
dimethylallyl diphosphate
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r
isopentenyl diphosphate
dimethylallyl diphosphate
B2ILS5
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r
isopentenyl diphosphate
dimethylallyl diphosphate
B2ILS5
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r
isopentenyl diphosphate
dimethylallyl diphosphate
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?
isopentenyl diphosphate
dimethylallyl diphosphate
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?
additional information
?
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Cinchona robusta
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induced after addition of a homogenate of the phytopathogenic fungus Phytophthora cinnamomi. Enzyme may be involved in the biosynthesis of anthraquinone phytoalexins that accumulate rapidly after elicitation of Cinchona cells
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additional information
?
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key enzyme in biosynthesis of isoprenoids
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?
additional information
?
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key enzyme in biosynthesis of isoprenoids
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?
additional information
?
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enzyme in the pathway of conversion of isopentenyl diphosphate to phytoene
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additional information
?
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enzyme of the isoprenoid pathway
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additional information
?
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enzyme in the pathway of conversion of isopentenyl diphosphate to phytoene
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NADH
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or NADPH required under aerobic, not under anaerobic conditions
additional information
-
IDI showed almost the same activity in the presence of NADH or dithionite. Data indicate that the reduced form of FMN is sufficient
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FMN
strictly dependent on
FMN
bound only with very moderate affinity and is therefore completely lost during purification. However, the enzyme can be reconstituted in the crystals by soaking with FMN
FMN
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nearly no activity with the flavin analogue 5-deazaFMN
FMN
maximal activity with 10 microM FMN
FMN
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required under aerobic and anaerobic conditions
FMN
-
reduced flavin is required. The neutral semiquinone state of the flavin is stabilized thermodynamically relative to free FMN in solution. Kd value is 0.0047 mM at pH 7.0, 37°C
FMN
-
FMN must be in reduced state to be catalytically active
FMN
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required, IDI-2 reconstituted with cofactor analogues such as 5-deaza-FMN show no activity
FMN
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IDI-2 requires reduced flavin
FMN
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the reduced FMN coenzyme of IDI-2 functions as an acid/base catalyst, with the N5 atom of the flavin likely playing a critical role in the deprotonation of isopentenyl diphosphate en route to dimethylallyl diphosphate formation
FMN
-
a mechanism is proposed where the reduced flavin cofactor acts as a general acid/base catalyst and helps stabilize the carbocationic intermediate formed by protonation
NAD(P)H
required
NAD(P)H
-
proposed mechanism: reduction of FMN
NAD(P)H
-
used only for the reduction of FMN, can be replaced with Na2S2O4
NADPH
-
-
NADPH
maximal acitivity with 1 mM NADPH
NADPH
-
or NADH required under aerobic, not under anaerobic conditions
NADPH
-
required for reductive activation of inactive oxidized enzyme. Kd value is 0.11 mM at pH 7.0, 37°C
NADPH
-
needed only in catalytic amounts to activate the enzyme for multiple turnovers. Hydride transfer from NADPH to reduce FMN is pro-S stereospecific
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Cd2+
-
reconstitution of metal-free enzyme with Mg2+, Mn2+, Zn2+, Co2+, Ni2+ or Cd2+ generates active enzyme
Cu2+
-
10mM, relative activity under 0.005%
Zinc
-
essential cofactor. Type I enzyme contains an atom of tinc. The metal is located in an unusual six-coordinate pocket and may facilitate protonation of the unactivated carbon-carbon double bond in isopentenyl diphosphate
Ca2+
lower activity as with Mg2+
Ca2+
-
10mM, relative activity 100%
Co2+
-
10mM, relative activity under 0.005%
Co2+
-
reconstitution of metal-free enzyme with Mg2+, Mn2+, Zn2+, Co2+, Ni2+ or Cd2+ generates active enzyme
Mg2+
-
required, 2fold increase in activity with 10 mM Mg2+
Mg2+
-
10mM, relative activity 65%
Mg2+
-
Mn2+ is a better activator than Mg2+; Mn2+ or Mg2+ required
Mg2+
-
preference for Mn2+ over Mg2+
Mg2+
Cinchona robusta
-
activation by a mixture of Mg2+ and Mn2+ gives the highest activity; isomerase II: maximal activation at 2-8 mM Mg2+, the maximal activation is 35% lower than the activation obtained with Mn2+; isomerase I is activated by concentrations below 1 mM of Mn2+ or Mg2+, increasing concentrations are inhibitory; Mn2+ or Mg2+ required
Mg2+
-
maximal activation at 0.2 mM; Mn2+ or Mg2+ required
Mg2+
-
the enzyme requires one Mn2+ or Mg2+ ion to fold in its active conformation, forming a distorted octahedral metal coordination site composed of three histidines and two glutamates and located in the active site
Mg2+
-
the enzyme is fully active in the absence of Mn2+ as long as Mg2+ is present in the buffer
Mg2+
-
0.72 mol per mol of enzyme. Reconstitution of metal-free enzyme with Mg2+, Mn2+, Zn2+, Co2+, Ni2+ or Cd2+ generates active enzyme
Mg2+
-
required for activity
Mg2+
-
maximal activation at 20 mM; Mn2+ or Mg2+ required
Mg2+
-
preference for Mn2+ over Mg2+
Mg2+
-
IDI-2 requires a divalent cation such as Mg2+ for activity
Mg2+
-
required. The enzyme requires the combined presence of FMN, NADPH and Mg2+
Mg2+
-
Mn2+ or Mg2+ required
Mg2+
-
Mn2+ or Mg2+ required
Mg2+
-
maximal activation at 5 mM; restores activity after EDTA treatment
Mg2+
-
preference for Mn2+ over Mg2+
Mg2+
-
Kd value is 0.13 mM at pH 7.0, 37°C
Mg2+
-
required for activity
Mn2+
-
required, 2.5fold increase in activity with 0.1 mM Mn2+
Mn2+
lower activity as with Mg2+
Mn2+
-
10mM, relative activity 17%
Mn2+
-
Mn2+ is a better activator than Mg2+; Mn2+ or Mg2+ required
Mn2+
-
preference for Mn2+ over Mg2+
Mn2+
Cinchona robusta
-
activation by a mixture of Mg2+ and Mn2+ gives the highest activity; isomerase I is activated by concentrations below 1 mM of Mn2+ or Mg2+, increasing concentrations are inhibitory; Mn2+ or Mg2+ required
Mn2+
-
Mn2+ or Mg2+ required
Mn2+
-
the enzyme requires one Mn2+ or Mg2+ ion to fold in its active conformation, forming a distorted octahedral metal coordination site composed of three histidines and two glutamates and located in the active site
Mn2+
-
the enzyme is fully active in the absence of Mn2+ as long as Mg2+ is present in the buffer
Mn2+
-
0.10 mol per mol of enzyme. Reconstitution of metal-free enzyme with Mg2+, Mn2+, Zn2+, Co2+, Ni2+ or Cd2+ generates active enzyme
Mn2+
-
isomerase I: maximal activation at 0.5 mM, isomerase II, III or IV: maximal activation at 0.25 mM
Mn2+
-
maximal activation at 0.1 mM; Mn2+ or Mg2+ required
Mn2+
-
maximal activity at 0.01 mM
Mn2+
-
preference for Mn2+ over Mg2+
Mn2+
-
maximal activation at 0.5 mM; Mn2+ or Mg2+ required
Mn2+
-
Mn2+ or Mg2+ required
Mn2+
-
maximal activation at 2 mM, activity maximum obtained with Mn2+ is about 3times that with Mg2+; restores activity after EDTA treatment
Mn2+
-
preference for Mn2+ over Mg2+
Ni2+
-
10mM, relative activity under 0.005%
Ni2+
-
reconstitution of metal-free enzyme with Mg2+, Mn2+, Zn2+, Co2+, Ni2+ or Cd2+ generates active enzyme
Zn2+
-
10mM, relative activity 0.2%
Zn2+
-
0.92 mol per mol of enzyme. Reconstitution of metal-free enzyme with Mg2+, Mn2+, Zn2+, Co2+, Ni2+ or Cd2+ generates active enzyme
Zn2+
-
IDI-1 is a zinc-metalloprotein
additional information
-
not activated by Zn2+
additional information
-
no effects of other divalent cations such as Co2+, Cu2+, Zn2+ at 5mM
additional information
no effects of other divalent cations such as Co2+, Cu2+, Zn2+ at 5mM
additional information
-
not activated by Zn2*, Fe2*, or Cu2+
additional information
-
not activated by Zn2+, Fe2+, or Cu2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(+/-)-cis/trans-Chrysanthemyl diphosphate
-
-
(+/-)-cis/trans-Chrysanthemyl monophosphate
-
-
(2Z)-3-methylhept-2-en-1-yl trihydrogen diphosphate
(2Z)-3-methylhex-2-en-1-yl trihydrogen diphosphate
(2Z)-3-methyloct-2-en-1-yl trihydrogen diphosphate
(E/Z)-3-cyclopropyl-2-buten-1-yl diphosphate
-
-
(N,N-dimethylamino)-1-ethyl diphosphate
-
transition state analogue
(Z)-3-difluoromethyl-2-buten-1-yl diphosphate
-
reversible
(Z)-3-fluoromethyl-2-buten-1-yl diphosphate
-
reversible
(Z)-4-Fluoro-3-methyl-2-buten-1-yl diphosphate
-
inactivates through an active-site-directed covalent modification
2,2-Diphenyl-1-(beta-dimethylaminoethoxy)pentane hydrochloride
-
-
2,3-butadien-1-yl diphosphate
2,3-cis,6,7-trans-farnesyl diphosphate
-
-
2-(dimethylamino)ethyl diphosphate
-
weak competitive inhibitor
-
2-(dimethylamino)ethyl phosphate
2-[ethyl(methyl)amino]ethyl trihydrogen diphosphate
2-[ethyl(propyl)amino]ethyl trihydrogen diphosphate
3,4-Epoxy-1-butenyl diphosphate
-
active-site directed irreversible inhibitor
3,4-epoxy-3-methyl-1-butyl diphosphate
-
-
3,4-epoxy-3-methylbutyl diphosphate
3,4-oxido-3-methyl-1-butyl diphosphate
-
inactivation through formation of covalent adducts with the reduced flavin, modification of the isoalloxazine ring at position N5
3-(Fluoromethyl)-3-buten-1-yl diphosphate
3-Bromo-3-butenyl diphosphate
-
competitive
3-cyclopropyl-3-buten-1-yl diphosphate
3-cyclopropylbut-3-en-1-yl trihydrogen diphosphate
-
cyclopropyl-derivative of isopentenyl diphosphate, mechanism-based inhibitor
3-Methyl-3,4-epoxybutyl diphosphate
3-methyl-5-oxo-hexyl diphosphate
-
-
3-methyl-5-oxo-hexyl diphosphate ethylene glycol acetal
-
-
3-methylene-4-penten-1-yl diphosphate
3-oxiran-2-ylbut-3-en-1-yl trihydrogen diphosphate
-
epoxy-derivative of isopentenyl diphosphate, mechanism-based inhibitor. The enzyme catalyzes formation of a stable covalent adduct between the inhibitor and FMNH2 in a reaction catalyzed by protonation of the epoxide moiety followed by nucleophilic addition of the cofactor
3-oxiranyl-3-buten-1-yl diphosphate
4-aminophenyl-2-ethane-1,1-bisphosphonic acid
-
weak. Due to inhibition of more than one enzyme in the mevalonate pathway may lead to an increase in antiresorptive potency compared to bisphosphonates that only inhibit farnesyl diphosphate synthase
beta-Diethylaminoethyldiphenylpropylacetate hydrochloride
-
i.e. SKF-525A
dimethylallyl diphosphate
Dimethylallyl diphosphate containing fluorine, epoxy, and ammonium function groups
-
-
-
dimethylammonium diphosphate
EDTA
addditon of 5mM EDTA results in almost complete loss of activity
epoxide of isopentenyl diphosphate
-
-
geranyl monophosphate
-
-
homodimethylallyl diphosphate
homoisopentenyl diphosphate
Isoamyl diphosphate
-
competitive
isopentenyl diphosphate
-
-
Isopentenyl diphosphates containing fluorine, epoxy, and ammonium functional groups
-
-
-
linaloyl monophosphate
-
-
Methyl diphosphate
-
competitive
Mg2+
Cinchona robusta
-
isomerase I is activated by concentrations below 1 mM of Mn2+ or Mg2+, increasing concentrations are inhibitory
N,N-dimethyl-2-amino-1-ethyl diphosphate
-
transition state analogue, competitive
N,N-dimethylaminoethyl diphosphate
-
-
O2
-
the overall reaction is sensitive to O2
p-hydroxymercuribenzoate
-
-
Terpene diphosphate esters
-
-
-
Terpene monophosphate esters
-
-
-
additional information
-
not inhibited by 2-[ethyl(propyl)amino]ethyl trihydrogen diphosphate
-
(2Z)-3-methylhept-2-en-1-yl trihydrogen diphosphate
-
-
(2Z)-3-methylhept-2-en-1-yl trihydrogen diphosphate
-
-
(2Z)-3-methylhept-2-en-1-yl trihydrogen diphosphate
-
-
(2Z)-3-methylhex-2-en-1-yl trihydrogen diphosphate
-
-
(2Z)-3-methylhex-2-en-1-yl trihydrogen diphosphate
-
-
(2Z)-3-methylhex-2-en-1-yl trihydrogen diphosphate
-
-
(2Z)-3-methyloct-2-en-1-yl trihydrogen diphosphate
-
-
(2Z)-3-methyloct-2-en-1-yl trihydrogen diphosphate
-
-
(2Z)-3-methyloct-2-en-1-yl trihydrogen diphosphate
-
-
2,3-butadien-1-yl diphosphate
-
competitive inhibitor
2,3-butadien-1-yl diphosphate
-
competitive inhibitor
2-(dimethylamino)ethyl phosphate
Cinchona robusta
-
-
2-(dimethylamino)ethyl phosphate
-
may function as a transition state or reactive intermediate analogue of a carbocation that binds extremely tightly
2-(dimethylamino)ethyl phosphate
-
competitive
2-[ethyl(methyl)amino]ethyl trihydrogen diphosphate
-
-
2-[ethyl(methyl)amino]ethyl trihydrogen diphosphate
-
-
2-[ethyl(methyl)amino]ethyl trihydrogen diphosphate
-
-
2-[ethyl(propyl)amino]ethyl trihydrogen diphosphate
-
-
2-[ethyl(propyl)amino]ethyl trihydrogen diphosphate
-
-
3,4-epoxy-3-methylbutyl diphosphate
-
i.e. EIPP, mechanism-based inhibitor of type I enzyme, covalent modification of reduced FMN in N5 position
3,4-epoxy-3-methylbutyl diphosphate
-
irreversible inhibition
3-(Fluoromethyl)-3-buten-1-yl diphosphate
-
-
3-(Fluoromethyl)-3-buten-1-yl diphosphate
-
inactivates through an active-site-directed covalent modification
3-(Fluoromethyl)-3-buten-1-yl diphosphate
-
active site-directed inhibitor
3-(Fluoromethyl)-3-buten-1-yl diphosphate
-
active site-directed inhibitor; irreversible
3-(Fluoromethyl)-3-buten-1-yl diphosphate
-
inactivation through formation of covalent adducts with the reduced flavin
3-butyn-1-yl diphosphate
-
competitive inhibitor
3-butyn-1-yl diphosphate
-
competitive inhibitor
3-cyclopropyl-3-buten-1-yl diphosphate
-
reversible
3-cyclopropyl-3-buten-1-yl diphosphate
-
-
3-Methyl-3,4-epoxybutyl diphosphate
-
-
3-Methyl-3,4-epoxybutyl diphosphate
-
time-dependent first-order loss of activity
3-methylene-4-penten-1-yl diphosphate
-
irreversible inhibition; the covalent adduct formed between irreversible mechanism based inhibitors, 3-methylene-4-penten-1-yl diphosphate or 3-oxiranyl-3-buten-1-yl diphosphate, and the flavin cofactor are investigated by X-ray crystallography and UV-visible spectroscopy. Both the crystal structures of enzyme binding the flavin-inhibitor adduct and the UV-visible spectra of the adducts indicate that the covalent bond is formed at C4a of flavin rather than at N5
3-methylene-4-penten-1-yl diphosphate
-
inactivation through formation of covalent adducts with the reduced flavin
3-oxiranyl-3-buten-1-yl diphosphate
-
irreversible inhibition; the covalent adduct formed between irreversible mechanism based inhibitors, 3-methylene-4-penten-1-yl diphosphate or 3-oxiranyl-3-buten-1-yl diphosphate, and the flavin cofactor are investigated by X-ray crystallography and UV-visible spectroscopy. Both the crystal structures of enzyme binding the flavin-inhibitor adduct and the UV-visible spectra of the adducts indicate that the covalent bond is formed at C4a of flavin rather than at N5
3-oxiranyl-3-buten-1-yl diphosphate
-
irreversible
dimethylallyl diphosphate
-
-
dimethylallyl diphosphate
-
-
dimethylallyl diphosphate
-
-
dimethylallyl diphosphate
-
-
dimethylallyl diphosphate
-
-
dimethylammonium diphosphate
-
-
dimethylammonium diphosphate
-
-
dimethylammonium diphosphate
-
-
diphosphate
-
-
diphosphate
-
inhibitory effect decreases in the order of isomerases I, II, III, and IV
farnesyl diphosphate
-
-
geranyl diphosphate
Cinchona robusta
-
-
homodimethylallyl diphosphate
-
-
homodimethylallyl diphosphate
-
-
homodimethylallyl diphosphate
-
-
homoisopentenyl diphosphate
-
-
homoisopentenyl diphosphate
-
-
homoisopentenyl diphosphate
-
-
iodoacetamide
-
70% inhibition at 0.001 mM, complete inhibition at 0.1 mM
iodoacetamide
Cucurbita sp.
-
-
iodoacetamide
-
inhibitory effect decreases in the order of isomerases I, II, III, no inhibition of isomerase IV
iodoacetic acid
-
-
Mn2+
Cinchona robusta
-
isomerase I is activated by concentrations below 1 mM of Mn2+ or Mg2+, increasing concentrations are inhibitory
Mn2+
inhibitory at high concentrations
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FMN
-
required as cofactor. The enzyme requires the combined presence of FMN, NADPH and Mg2+
L-Cysteine hydrochloride
-
activates
mevalonic acid
-
activates
Mevalonic acid lactone
-
weakly activates
NADPH
-
required as cofactor. The enzyme requires the combined presence of FMN, NADPH and Mg2+
2-mercaptoethanol
-
activates isomerase III and IV
2-mercaptoethanol
-
activates
dithiothreitol
-
activates
dithiothreitol
-
activates
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Amyotrophic Lateral Sclerosis
Segmental copy-number gain within the region of isopentenyl diphosphate isomerase genes in sporadic amyotrophic lateral sclerosis.
Bacterial Infections
Characterization and mechanistic studies of type II isopentenyl diphosphate:dimethylallyl diphosphate isomerase from Staphylococcus aureus.
isopentenyl-diphosphate delta-isomerase deficiency
Isopentenyl diphosphate isomerase deficiency in Synechocystis sp. strain PCC6803.
Neoplasms
Proliferation of NS0 cells in protein-free medium: the role of cell-derived proteins, known growth factors and cellular receptors.
Paralysis
Isopentenyl-diphosphate isomerase is essential for viability of Caenorhabditis elegans.
Zellweger Syndrome
Cholesterol biosynthesis in Zellweger syndrome: normal activity of mevalonate kinase, mevalonate-5'-pyrophosphate decarboxylase and IPP-isomerase in patients' fibroblasts but deficient mevalonate kinase activity in liver.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.017
dimethylallyl diphosphate
Cinchona robusta
-
isomerase I
0.0008 - 15.3
isopentenyl diphosphate
additional information
additional information
-
substrate binds to the inactive oxidized and active reduced form of enzyme with similar affinities
-
0.0008
isopentenyl diphosphate
-
mutant enzyme W161F
0.001
isopentenyl diphosphate
Cinchona robusta
-
isomerase II
0.0013
isopentenyl diphosphate
-
isomerase II and III
0.0015
isopentenyl diphosphate
-
pH 6.0, 60°C, mutant enzyme Q160L
0.00152
isopentenyl diphosphate
-
mutant enzyme Q160L, in 50 mM MOPS-NaOH, pH 6.0, at 60°C
0.0017
isopentenyl diphosphate
-
isomerase I
0.0025
isopentenyl diphosphate
-
isomerase IV
0.0027
isopentenyl diphosphate
-
-
0.003
isopentenyl diphosphate
-
mutant enzyme R83K
0.0032
isopentenyl diphosphate
-
pH 6.0, 60°C, mutant enzyme Q160N
0.00323
isopentenyl diphosphate
-
mutant enzyme Q160N, in 50 mM MOPS-NaOH, pH 6.0, at 60°C
0.0033
isopentenyl diphosphate
-
wild type enzyme, in 25 mM Tris-HCl, pH 7.0, at 37°C
0.0035
isopentenyl diphosphate
-
wild-type enzyme
0.004
isopentenyl diphosphate
-
-
0.0048
isopentenyl diphosphate
-
aerobic, presence of NADPH, pH 7.0, 37°C
0.0051
isopentenyl diphosphate
Cinchona robusta
-
isomerase I
0.0054
isopentenyl diphosphate
-
-
0.0056
isopentenyl diphosphate
-
pH 7.0, 37°C
0.0057
isopentenyl diphosphate
-
-
0.00595
isopentenyl diphosphate
-
wild type enzyme, at anaerobic conditions, at pH 7.0 and 37°C
0.006
isopentenyl diphosphate
-
-
0.006
isopentenyl diphosphate
-
mutant enzyme E169Q, in 25 mM Tris-HCl, pH 7.0, at 37°C; mutant enzyme Y105F, in 25 mM Tris-HCl, pH 7.0, at 37°C
0.0071
isopentenyl diphosphate
-
pH 6.0, 60°C, mutant enzyme Q160H
0.00713
isopentenyl diphosphate
-
mutant enzyme Q160H, in 50 mM MOPS-NaOH, pH 6.0, at 60°C
0.00714
isopentenyl diphosphate
-
pH 6.0, 60°C, mutant enzyme E13R/R235E
0.00739
isopentenyl diphosphate
-
wild type enzyme, in 50 mM MOPS-NaOH, pH 6.0, at 60°C
0.0074
isopentenyl diphosphate
-
pH 6.0, 60°C, wild-type enzyme
0.0076
isopentenyl diphosphate
-
-
0.00826
isopentenyl diphosphate
-
mutant enzyme Q160E, in 50 mM MOPS-NaOH, pH 6.0, at 60°C
0.0083
isopentenyl diphosphate
-
pH 6.0, 60°C, mutant enzyme Q160E
0.0095
isopentenyl diphosphate
-
wild-type, pH 7.4, 37°C
0.0115
isopentenyl diphosphate
-
mutant enzyme E87Q
0.0116
isopentenyl diphosphate
-
mutant enzyme W216F, in 25 mM Tris-HCl, pH 7.0, at 37°C
0.012
isopentenyl diphosphate
-
aerobic, presence of dithionite, pH 7.0, 37°C
0.0128
isopentenyl diphosphate
-
mutant enzyme Y159F, in 25 mM Tris-HCl, pH 7.0, at 37°C
0.014
isopentenyl diphosphate
-
mutant enzyme K55A
0.0142
isopentenyl diphosphate
-
mutant Y104F, pH 7.4, 37°C
0.015
isopentenyl diphosphate
-
mutant enzyme K55R
0.0168
isopentenyl diphosphate
-
anaerobic, presence of NADPH, pH 7.0, 37°C
0.0185
isopentenyl diphosphate
-
mutant enzyme R51K
0.02
isopentenyl diphosphate
-
-
0.021
isopentenyl diphosphate
-
mutant enzyme E116Q
0.0225
isopentenyl diphosphate
-
mutant Y104A, pH 7.4, 37°C
0.0228
isopentenyl diphosphate
-
pH 8.0
0.033
isopentenyl diphosphate
-
-
0.035
isopentenyl diphosphate
-
-
0.036
isopentenyl diphosphate
-
-
0.0376
isopentenyl diphosphate
mutant enzyme L141H/Y195F/W256C, at pH 7.5 and 30°C
0.04
isopentenyl diphosphate
at pH 7.0 and 37°C
0.0408
isopentenyl diphosphate
-
wild type enzyme, at aerobic conditions, at pH 7.0 and 37°C
0.0415
isopentenyl diphosphate
wild type enzyme, at pH 7.5 and 30°C
0.043
isopentenyl diphosphate
-
-
0.046
isopentenyl diphosphate
-
pH 8.0, 50°C
0.0463
isopentenyl diphosphate
-
pH 6.0, 60°C, wild-type enzyme
0.047
isopentenyl diphosphate
-
pH 8.0, 55°C
0.063
isopentenyl diphosphate
pH 6.0, 60°C
0.063
isopentenyl diphosphate
-
pH 8.0, 60°C
0.064
isopentenyl diphosphate
-
-
0.065
isopentenyl diphosphate
-
pH 8.0, 70°C
0.071
isopentenyl diphosphate
-
pH 8.0, 65°C
0.077
isopentenyl diphosphate
-
pH 8.0, 75°C
0.084
isopentenyl diphosphate
-
pH 8.0, 80°C
0.0841
isopentenyl diphosphate
-
pH 6.0
0.093
isopentenyl diphosphate
-
pH 8.0, 90°C
0.187
isopentenyl diphosphate
-
pH 8.0, 82.5°C
0.199
isopentenyl diphosphate
-
pH 8.0, 87.5°C
0.211
isopentenyl diphosphate
-
pH 8.0, 85°C
0.2768
isopentenyl diphosphate
-
in 0.4 M Tris, 1 mM dithiothreitol, 10 mM MgCl2, pH 8.0, at 50°C
0.572
isopentenyl diphosphate
-
mutant enzyme N37A, at aerobic conditions, at pH 7.0 and 37°C
15.3
isopentenyl diphosphate
-
pH 7.0, 85°C
0.0874
NADH
dehydrogenase reaction without isopentenyl diphosphate
0.0904
NADH
isomerase reaction
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.000197 - 29900
isopentenyl diphosphate
0.000197
isopentenyl diphosphate
-
pH 6.0, 60°C, mutant enzyme Q160N
0.00022
isopentenyl diphosphate
-
pH 6.0, 60°C, mutant enzyme Q160L
0.001
isopentenyl diphosphate
-
pH 6.0, 60°C, mutant enzyme Q160H
0.003
isopentenyl diphosphate
-
pH 6.0, 60°C, mutant enzyme Q160E
0.03
isopentenyl diphosphate
-
pH 6.0, 60°C, wild-type enzyme
0.065
isopentenyl diphosphate
-
aerobic, presence of NADPH, pH 7.0, 37°C
0.141
isopentenyl diphosphate
at pH 7.0 and 37°C
0.2
isopentenyl diphosphate
pH 6.0, 60°C
0.57
isopentenyl diphosphate
-
aerobic, presence of dithionite, pH 7.0, 37°C
0.69
isopentenyl diphosphate
-
anaerobic, presence of NADPH, pH 7.0, 37°C
0.875
isopentenyl diphosphate
-
wild type enzyme, at anaerobic conditions, at pH 7.0 and 37°C
0.983
isopentenyl diphosphate
-
wild type enzyme, at aerobic conditions, at pH 7.0 and 37°C
1.31
isopentenyl diphosphate
-
mutant enzyme N37A, at aerobic conditions, at pH 7.0 and 37°C
1.6
isopentenyl diphosphate
-
-
8.27
isopentenyl diphosphate
wild type enzyme, at pH 7.5 and 30°C
10.57
isopentenyl diphosphate
mutant enzyme L141H/Y195F/W256C, at pH 7.5 and 30°C
17.9
isopentenyl diphosphate
-
pH 7.0, 37°C
191
isopentenyl diphosphate
-
pH 7.0, 85°C
197
isopentenyl diphosphate
-
mutant enzyme Q160N, in 50 mM MOPS-NaOH, pH 6.0, at 60°C
221
isopentenyl diphosphate
-
mutant enzyme Q160L, in 50 mM MOPS-NaOH, pH 6.0, at 60°C
1210
isopentenyl diphosphate
-
mutant enzyme Q160H, in 50 mM MOPS-NaOH, pH 6.0, at 60°C
3280
isopentenyl diphosphate
-
mutant enzyme Q160E, in 50 mM MOPS-NaOH, pH 6.0, at 60°C
29900
isopentenyl diphosphate
-
wild type enzyme, in 50 mM MOPS-NaOH, pH 6.0, at 60°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.031 - 280
isopentenyl diphosphate
0.031
isopentenyl diphosphate
-
mutant enzyme Q160K, in 50 mM MOPS-NaOH, pH 6.0, at 60°C
0.061
isopentenyl diphosphate
-
mutant enzyme Q160N, in 50 mM MOPS-NaOH, pH 6.0, at 60°C
0.145
isopentenyl diphosphate
-
mutant enzyme Q160L, in 50 mM MOPS-NaOH, pH 6.0, at 60°C
0.17
isopentenyl diphosphate
-
mutant enzyme Q160H, in 50 mM MOPS-NaOH, pH 6.0, at 60°C
0.397
isopentenyl diphosphate
-
mutant enzyme Q160E, in 50 mM MOPS-NaOH, pH 6.0, at 60°C
4.05
isopentenyl diphosphate
-
wild type enzyme, in 50 mM MOPS-NaOH, pH 6.0, at 60°C
200
isopentenyl diphosphate
wild type enzyme, at pH 7.5 and 30°C
280
isopentenyl diphosphate
mutant enzyme L141H/Y195F/W256C, at pH 7.5 and 30°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.383
(Z)-3-difluoromethyl-2-buten-1-yl diphosphate
-
pH 7.0, 37°C
0.012
(Z)-3-fluoromethyl-2-buten-1-yl diphosphate
-
pH 7.0, 37°C
0.031 - 0.036
2,3-butadien-1-yl diphosphate
0.0565
3,4-epoxy-3-methylbutyl diphosphate
-
pH 7.0, 85°C
0.0486
3,4-oxido-3-methyl-1-butyl diphosphate
-
pH 7.0, 37°C
0.0074
3-(Fluoromethyl)-3-buten-1-yl diphosphate
-
pH 7.0, 37°C
0.048 - 0.049
3-butyn-1-yl diphosphate
0.054
3-cyclopropyl-3-buten-1-yl diphosphate
-
pH 7.0, 37°C
0.008
3-methylene-4-penten-1-yl diphosphate
-
pH 7.0, 37°C
0.0014
3-oxiranyl-3-buten-1-yl diphosphate
-
pH 7.0, 37°C
0.292
isopentenyl diphosphate
0.031
2,3-butadien-1-yl diphosphate
-
in 50 mM HEPES (pH 7.2) containing 10 mM MgCl2, 200 mM KCl, 1 mg/ml bovine serum albumin, 0.5 mM dithiothreitol, at 37°C
0.036
2,3-butadien-1-yl diphosphate
-
in 200 mM HEPES (pH 7.0) containing 2 mM MgCl2, 0.04 mM FMN, 2 mM NADPH, at 37°C
0.048
3-butyn-1-yl diphosphate
-
in 200 mM HEPES (pH 7.0) containing 2 mM MgCl2, 0.04 mM FMN, 2 mM NADPH, at 37°C
0.049
3-butyn-1-yl diphosphate
-
in 50 mM HEPES (pH 7.2) containing 10 mM MgCl2, 200 mM KCl, 1 mg/ml bovine serum albumin, 0.5 mM dithiothreitol, at 37°C
0.0064
FMN
-
wild type enzyme, at anaerobic conditions, at pH 7.0 and 37°C
0.0064
FMN
at pH 7.0 and 37°C
0.292
isopentenyl diphosphate
-
wild type enzyme, at aerobic conditions, at pH 7.0 and 37°C
0.292
isopentenyl diphosphate
at pH 7.0 and 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.158
(2Z)-3-methylhept-2-en-1-yl trihydrogen diphosphate
Choristoneura fumiferana
-
in 25 mM Tris-HCl, pH 7.0, at 37°C
0.156
(2Z)-3-methylhex-2-en-1-yl trihydrogen diphosphate
Choristoneura fumiferana
-
in 25 mM Tris-HCl, pH 7.0, at 37°C
0.234
(2Z)-3-methyloct-2-en-1-yl trihydrogen diphosphate
Choristoneura fumiferana
-
in 25 mM Tris-HCl, pH 7.0, at 37°C
0.278
(E/Z)-3-cyclopropyl-2-buten-1-yl diphosphate
Thermus thermophilus
-
25°C, pH 8.6
0.003 - 0.0055
2-[ethyl(methyl)amino]ethyl trihydrogen diphosphate
0.007
2-[ethyl(propyl)amino]ethyl trihydrogen diphosphate
Choristoneura fumiferana
-
in 25 mM Tris-HCl, pH 7.0, at 37°C
0.1
3-cyclopropyl-3-buten-1-yl diphosphate
Thermus thermophilus
-
25°C, pH 8.6
0.00114
3-oxiranyl-3-buten-1-yl diphosphate
Thermus thermophilus
-
pH 7.0, 37°C
0.092
dimethylallyl diphosphate
Choristoneura fumiferana
-
in 25 mM Tris-HCl, pH 7.0, at 37°C
0.0008
dimethylammonium diphosphate
Sus scrofa
-
in 50 mM Tris-HCl (pH 7.0), at 37°C
0.131
homodimethylallyl diphosphate
Choristoneura fumiferana
-
in 25 mM Tris-HCl, pH 7.0, at 37°C
0.066
homoisopentenyl diphosphate
Choristoneura fumiferana
-
in 25 mM Tris-HCl, pH 7.0, at 37°C
0.003
2-[ethyl(methyl)amino]ethyl trihydrogen diphosphate
Choristoneura fumiferana
-
in 25 mM Tris-HCl, pH 7.0, at 37°C
0.0055
2-[ethyl(methyl)amino]ethyl trihydrogen diphosphate
Sus scrofa
-
in 50 mM Tris-HCl (pH 7.0), at 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.001
-
pyruvate, C13-labeled at positions 2 and 3, aerobic, pH 8, 37°C
0.046
Cinchona robusta
-
-
0.08
-
dimethylallyl diphosphate, C13-labeled at positions 3, 4 and 5, aerobic, pH 8, 37°C
0.19
-
dimethylallyl diphosphate, anaerobic, pH 8, 37°C
0.23
-
dimethylallyl diphosphate, aerobic, pH 8, 37°C
0.62
-
isopentenyl diphosphate, anaerobic, pH 8, 37°C
0.63
-
isopentenyl diphosphate, aerobic, pH 8, 37°C
52
-
isoenzyme type II, isopentenyl diphosphate, pH 7.0, 37 °C
additional information
-
-
additional information
-
-
additional information
-
mutant D216A, relative IPP isomerase activity 35%, wild-type enzyme 100%; mutant E161A, relative IPP isomerase activity 0.5%, wild-type enzyme 100%; mutant E194A, relative IPP isomerase activity 15%, wild-type enzyme 100%; mutant E229A, relative IPP isomerase activity 6.5%, wild-type enzyme 100%; mutant H11A, relative IPP isomerase activity 4%, wild-type enzyme 100%; mutant H155A, relative IPP isomerase activity 3%, wild-type enzyme 100%; mutant K193A, relative IPP isomerase activity 1%, wild-type enzyme 100%; mutant K8A, relative IPP isomerase activity 0.1%, wild-type enzyme 100%; mutant N125A, relative IPP isomerase activity 5%, wild-type enzyme 100%; mutant N157A, relative IPP isomerase activity 0.5%, wild-type enzyme 100%; mutant Q160A, relative IPP isomerase activity 0.1%, wild-type enzyme 100%; mutant R232A, relative IPP isomerase activity 2%, wild-type enzyme 100%; mutant R7A, relative IPP isomerase activity 0.1%, wild-type enzyme 100%; mutant S96A, relative IPP isomerase activity 3%, wild-type enzyme 100%; mutant T68A, relative IPP isomerase activity 6%, wild-type enzyme 100%
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
6 - 8.5
-
in presence of Mg2+. A sharper maximum is observed in presence of Mn2+
7
-
in presence of Mg2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
4.5 - 9.5
-
pH 4.5: about 39% of maximal activity, pH 9.5: about 60% of maximal activity
5.5 - 7.5
-
pH 5.5: about 35% of maximal activity, pH 7.5: about 30% of maximal activity
7 - 8.5
Cinchona robusta
-
pH 7.0-7.8: maximal activity, pH 8.5: 20% of maximal activity, isomerase I
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
6
-
calculated from amino acid sequence
6.4
-
calculated from amino acid sequence
5.9
-
isoelectric focusing
6.1
-
-
6.1
calculated from amino acid sequence
6.1
calculated from amino acid sequence
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
UniProt
brenda
-
-
-
brenda
-
-
-
brenda
Cinchona robusta
-
-
-
brenda
Citrus sp.
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
Cucurbita sp.
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
UniProt
brenda
-
A0A067K3N5
UniProt
brenda
-
UniProt
brenda
-
-
-
brenda
-
Uniprot
brenda
type II isopentenyl diphosphate isomerase
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
isoform IDI2
UniProt
brenda
-
-
-
brenda
-
UniProt
brenda
-
-
-
brenda
-
-
-
brenda
type II enzyme
-
-
brenda
-
UniProt
brenda
-
-
-
brenda
strain PCC 6803 ORF sll 1556
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
Vitis vinifera x Vitis vinifera
-
-
-
brenda
isoform Idi1
UniProt
brenda
isoform IDI2
UniProt
brenda
isoform Ipi1
UniProt
brenda
isoform Ipi2
UniProt
brenda
-
SwissProt
brenda
-
-
-
brenda
type II isopentenyl diphosphate:dimethylallyl diphosphate isomerase
SwissProt
brenda
-
-
-
brenda
cultivar Pacifica Pink
-
-
brenda
-
-
-
brenda
-
UniProt
brenda
type I enzyme
-
-
brenda
type I isopentenyl-diphosphate D-isomerase
-
-
brenda
wild type and strain Y104F
UniProt
brenda
-
-
-
brenda
4 enzyme forms: I, II, III, and IV
-
-
brenda
-
-
-
brenda
-
SwissProt
brenda
isoform 1 and isoform 2
SwissProt
brenda
isoform IDI2
-
-
brenda
type I enzyme
SwissProt
brenda
-
-
-
brenda
type II enzyme, isoform IDI-2
-
-
brenda
-
-
-
brenda
-
Uniprot
brenda
-
-
-
brenda
-
SwissProt
brenda
type 2 isopentenyl diphosphate isomerase
SwissProt
brenda
-
-
-
brenda
-
UniProt
brenda
expressed in Escherichia coli
-
-
brenda
-
A9LRT7
UniProt
brenda
cultivar M82
-
-
brenda
tomato
-
-
brenda
-
-
-
brenda
type II enzyme
-
-
brenda
type II isopentenyl diphosphate/dimethylallyl diphosphate isomerase
-
-
brenda
-
-
-
brenda
-
UniProt
brenda
-
-
-
brenda
isoform IDI-2
-
-
brenda
isoform IDI2
-
-
brenda
type II enzyme, recombinant protein
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-
brenda
-
-
brenda
Cinchona robusta
-
-
brenda
-
-
brenda
-
developing
brenda
-
in normal fibroblasts and Zellweger fibroblasts, in which the synthesis of cholesterol is impaired
brenda
-
-
brenda
-
-
brenda
Citrus sp.
-
-
brenda
-
-
brenda
-
-
brenda
A0A067K3N5
-
brenda
-
isoform IDI2 is only expressed in skeletal muscle
brenda
-
highest expression
brenda
in mature and tender leaf, expression is higher than in tubers
brenda
-
-
brenda
-
highly abundant in the corpora allata
brenda
-
-
brenda
-
high expression
brenda
A0A067K3N5
highest expression
brenda
highest expression
brenda
A9LRT7
-
brenda
-
-
brenda
Cucurbita sp.
-
-
brenda
-
brenda
-
-
brenda
-
-
brenda
expression in stem is much higher than in root and tender leaf, no expression in mature leaf
brenda
-
highest expression in young leaf
brenda
-
expression is highest in stems, followed by leaf, and is lowest in root
brenda
in mature and tender leaf, expression is higher than in tubers
brenda
A0A067K3N5
-
brenda
lowest expression
brenda
highest expression
brenda
-
-
brenda
A9LRT7
cDNA clone of the tomato IPI gene is amplified using cDNA from young leaves as template
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
-
brenda
-
-
brenda
expression in stem is much higher than in root and tender leaf
brenda
-
high expression
brenda
-
expression is highest in stems, followed by leaf, and is lowest in root
brenda
-
brenda
-
brenda
A9LRT7
highest expression level
brenda
-
-
brenda
expression is much higher than in root and tender leaf
brenda
-
expression is highest in stems, followed by leaf, and is lowest in root
brenda
-
brenda
-
brenda
A9LRT7
-
brenda
additional information
-
no expression in mature leaf and fruit
brenda
additional information
no expression in mature leaf and fruit
brenda
additional information
-
expression may be induced by Verticillium dahliae kleb, by methyl jasmonate and salicylic acid
brenda
additional information
no expression in veins
brenda
additional information
-
no activity in heart muscle
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
A0A067K3N5
-
brenda
A9LRT7
-
brenda
-
-
brenda
-
stroma
brenda
-
stroma
brenda
-
-
brenda
;
brenda
-
-
brenda
enhanced green fluorescent protein fusions are found mainly in the mitochondrion
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
enhanced green fluorescent protein fusions are found mainly in the plastid
brenda
-
-
brenda
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
metabolism
-
IPP isomerase activity is a rate-limiting step in terpenoid synthesis
metabolism
IPP isomerase activity is a rate-limiting step in terpenoid synthesis
metabolism
the enzyme plays a critical role in terpenoid metabolic pathways
metabolism
-
the plastidial enzyme plays an important function in carotenoid biosynthesis
physiological function
A9LRT7
isopentenyl diphosphate and dimethylallyl diphosphate are essential precursors for terpenoid biosynthesis
physiological function
-
involved in terpenoid metabolism
physiological function
Vitis vinifera x Vitis vinifera
-
involved in terpenoid metabolism
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Bacillus subtilis (strain 168)
Escherichia coli (strain K12)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
Streptococcus pneumoniae (strain CGSP14)
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
21760
-
x * 21760, selenomethionyl form of the enzyme, mass spectrometry
24500
-
x * 24500, SDS-PAGE
26300
x * 26300, SDS-PAGE
26864
-
x * 26864, calculation from nucleotide sequence
28500
-
x * 28500, calculated from amino acid sequence
29000
Cinchona robusta
-
x * 29000, isomerase I, SDS-PAGE
30000
A9LRT7
determined by SDS-PAGE
33350
-
x * 33350, calculation from nucleotide sequence
33800
x * 33800, calculated
34390
-
x * 34390, calculated
38460
-
calculated; mass spectrometry
39897
-
x * 39897, mass spectrometry
40000
-
x * 40000, SDS-PAGE
41492
-
8 * 41492, calculated
43000
4 * 43000, SDS-PAGE
48000
-
4 * 48000, SDS-PAGE
345000
-
gel filtration chromatography
29200
-
x * 29200, calculated from amino acid sequence
29200
-
x * 29200, calculated from amino acid sequence
34000
-
gel filtration
34000
Cinchona robusta
-
x * 34000, isomerase II, SDS-PAGE
35000
-
gel filtration
35000
-
x * 35000, SDS-PAGE
35000
-
x * 35000, SDS-PAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
?
-
x * 28500, calculated from amino acid sequence
?
-
x * 29200, calculated from amino acid sequence
?
Cinchona robusta
-
x * 29000, isomerase I, SDS-PAGE; x * 34000, isomerase II, SDS-PAGE
?
-
x * 21760, selenomethionyl form of the enzyme, mass spectrometry
?
-
x * 34390, calculated
?
x * 33680, calculated from amino acid sequence; x * 35000, SDS-PAGE
?
-
x * 29200, calculated from amino acid sequence
?
-
x * 39897, mass spectrometry
?
-
x * 33350, calculation from nucleotide sequence; x * 39000-40000, SDS-PAGE
?
x * 34100, calculated from amino acid sequence
?
-
x * 26864, calculation from nucleotide sequence
homotetramer
-
-
homotetramer
4 * 39868, calculated from amino acid sequence; 4 * 39874, purified His-tagged enzyme, electrospray ionization mass spectrometry
homotetramer
-
4 * 39868, calculated from amino acid sequence; 4 * 39874, purified His-tagged enzyme, electrospray ionization mass spectrometry
-
monomer
-
1 * 33500, SDS-PAGE
monomer
-
1 * 35000, SDS-PAGE
octamer
8 * 45000
octamer
-
substrate binding causes the dissociation of an octamer into tetramers. The mutant enzyme E13R/R235E is in the tetrameric state even at a concentration where the wild-type enzyme dominantly forms an octamer
octamer
-
8 * 41492, calculated
tetramer
-
4 * 48000, SDS-PAGE
tetramer
4 * 43000, SDS-PAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
sitting drop vapor diffusion method, ligand-free form of the FMN-bound enzyme form at 2.8 A resolution. The octamer forms a D4 symmetrical open, cage-like structure. The monomers of 45000 Da display a classical TIM barrel fold
comparison of orthorhombic, monoclinic and trigonal crystal forms, up to 2.2 A resolution. Crystallization of free enzyme and in complex wih transition-state analogue N,N-dimethyl-2-amino-1-ethyl diphosphate
-
crystal structure of free and metal-bound C67A mutant enzyme
-
crystal structure of the isomerase-bromohydrin complex
-
crystallographic investigation of phosphoantigen binding
crystals soaked with transition state analogue (N,N-dimethylamino)-1-ethyl diphosphate
-
hanging drop vapor diffusion method, crystal structure of the C67A mutant of isopentenyl diphosphate isomerase complexed with the mechanism-based irreversible inhibitor 3,4-epoxy-3-methyl-1-butyl diphosphate
-
hanging drop vapor diffusion method, crystal structures of complexes with transition state analogue N,N-dimethyl-2-amino-1-ethyl diphosphate and the covalently attached irreversible inhibitors 3,4-epoxy-3-methyl-1-butyl diphosphate at 1.96 A resolution
-
hanging drop vapour diffusion method, selenomethionyl form, crystals display trigonal symmetry, with unit-cell parameters, a = b = 71.3 A, c = 61.7 A, and diffract to 1.45 A resolution
-
of wild-type and mutants Y104A, Y104F
-
enzyme shows a flexible N-terminal alpha-helix covering the active pocket and blocking the entrance. Substrate binding induces conformational change in the active site. A water molecule is the direct proton donor for the substrate
native enzyme at 1.7 A and in complex with substrate at 1.9 A resolution. comparison with Escherichia coli enzyme structure
sitting drop vapor diffusion method, using 0.6 M calcium acetate and 50 mM HEPES pH 7.5
-
molecular modeling of structure and comparison with structures of Streptococcus pneumoniae and Thermus thermophilus enzymes
crystallized at 20°C using the hanging-drop vapor diffusion method with a reservoir solution containing 0.1 M Tris-HCl (pH 8.0), 0.2 M sodium citrate, and 30% (vol/vol) polyethylene glycol 400 (PEG 400)
-
the covalent adduct formed between irreversible mechanism based inhibitors, 3-methylene-4-penten-1-yl diphosphate or 3-oxiranyl-3-buten-1-yl diphosphate, and the flavin cofactor are investigated by X-ray crystallography and UV-visible spectroscopy. Both the crystal structures of enzyme binding the flavin-inhibitor adduct and the UV-visible spectra of the adducts indicate that the covalent bond is formed at C4a of flavin rather than at N5. The high-resolution crystal structures of enzyme-substrate complexes and the kinetic studies of new mutants confirm that only the flavin cofactor can catalyze protonation of the substrates and suggest that N5 of flavin is most likely to be involved in proton transfer
-
the crystal structures of the substrate-free enzyme and of the substrate-enzyme complexes, in the oxidized and reduced states, are solved to resolutions between 1.99 and 3.1 A, six distinct types of type 2 IDI crystals are obtained
-
sitting drop vapor diffusion method, using HEPES buffer (100 mM, pH 7.5 with 2 M (NH4)2SO4)
in complex with diphosphate. The diphosphate moiety is located near the conserved residues H10, R97, H152, Q157, E158, and W219, and the flavin cofactor. The putative active site may stabilize a carbocationic intermediate
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W216F
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10% activity compared to the wild type enzyme
Y105F
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115% activity compared to the wild type enzyme
C67A
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inactive mutant enzyme
K55A
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the ratio of maximal velocity to turnover number is 66% of that of the wild-type enzyme
K55R
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the ratio of maximal velocity to turnover number is 28% of that of the wild-type enzyme
R51K
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the ratio of maximal velocity to turnover number is 4.2% of that of the wild-type enzyme
R83K
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the ratio of maximal velocity to turnover number is 104% of that of the wild-type enzyme
W161F
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the ratio of maximal velocity to turnover number is 0.8% of that of the wild-type enzyme
Y104A
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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
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0.1% of wild-type activity. Crystallization data. General fold of enzyme is similar to wild-type
D216A
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mutation of highly conserved residue
E13R/R235E
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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
E161A
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mutation of highly conserved residue
E194A
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mutation of highly conserved residue
E229A
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mutation of highly conserved residue
H11A
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mutation of highly conserved residue
H155A
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mutation of highly conserved residue
K193A
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mutation of highly conserved residue
K8A
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mutation of highly conserved residue
N125A
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mutation of highly conserved residue
N157A
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mutation of highly conserved residue
Q160A
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mutation of highly conserved residue
Q160E
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10-fold decrease in kcat/Km; the mutant shows a 10fold decrease in kcat/Km
Q160H
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23-fold decrease in kcat/Km; the mutant shows a 23fold decrease in kcat/Km
Q160K
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130-fold decrease in kcat/Km; the mutant shows a 130fold decrease in kcat/Km
Q160L
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28-fold decrease in kcat/Km; the mutant shows a 28fold decrease in kcat/Km
Q160N
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150-fold decrease in kcat, kcat/Km decreases 66-fold; the mutant shows a 150fold decrease in kcat, although kcat/Km only decreases 66fold
R232A
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mutation of highly conserved residue
R7A
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mutation of highly conserved residue
S96A
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mutation of highly conserved residue
T68A
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mutation of highly conserved residue
L141H
the mutation enhances the enzyme activity 1.1fold
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
W256C
the mutation enhances the enzyme activity 0.47fold
Y195F
the mutation enhances the enzyme activity 0.71fold
Y195F/W256C
the mutations enhance the enzyme activity 1.14fold
Q154N
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active site mutant
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
E116Q
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the ratio of maximal velocity to turnover number is 0.09%% of that of the wild-type enzyme
E116Q
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inactive mutant enzyme
E87Q
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the ratio of maximal velocity to turnover number is 0.07% of that of the wild-type enzyme
E87Q
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inactive mutant enzyme
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; 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 idi1 activity have no major morphological or chemical differences from the wild-type. Mutants lacking both isoforms idi1 and idi2 are non-viable; 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; 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 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; 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
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functional expression in engineered Escherichia coli restores the carotenoid pathway
additional information
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
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37
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half-life in dilute solution: 30 min. In more concentrated solutions of the protein or dilute enzyme in the presence of 0.01% bovine serum albumin, little loss of activity after 1 h
48
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melting temperature of mutant Y104A
55
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melting temperature of mutant Y104F
69
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melting temperature of wild-type
70
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1h, IDI retained 50% of the activity
80
10 min, more than 90% residual activity
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high susceptibility to proteolysis
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unstable in dilute solutions
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-15°C, stable for several months
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-20°C, 0.1 M potassium phosphate buffer, pH 7.0, 2 mM dithiothreitol, stable for several weeks
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-80°C, 0.05 M Tris/HCl, pH 7.5, containing 0.01 mM leupeptin, 2 mM dithiothreitol, 5% glycerol, 55% of the activity is recovered after 3 months
Cinchona robusta
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2 isoforms: I and II
Cinchona robusta
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by affinity chromatography on Ni-NTA resin
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Co2+ column chromatography, and gel filtration
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cobalt column chromatography
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DEAE Sepharose column chromatography and Resource Phe column chromatograpyh
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His-Trap column chromatography
Ni-NTA agarose column chromatography
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Ni-NTA agarose resin column chromatography
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Ni-NTA column chromatography
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nickel-nitrilotriacetic acid affinity chromatography
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on a HisTrap column, for crystallisation, the enzyme is loaded on a HiLoad 16/60 Superdex 200 column
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partial. Dye-ligand and immobilized metal ion interaction chromatography are efficient techniques for the rapid batchwise fractionation, from crude plant extracts, of a series of enzymes of prenyl diphosphate metabolism
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recombinant protein, enzyme purified under aerobic conditions is inactive until the flavin cofactor is reduced by NADPH or dithionite or photochemically
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TALON metal affinity resin column chromatography
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recombinant enzyme
TALON metal affinity resin column chromatography
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TALON metal affinity resin column chromatography
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expressed in Escherichia coli
expressed in Escherichia coli BL21 cells
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) pLysS cells
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expressed in Escherichia coli M15pREP4 cells
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expressed in Escherichia coli M15[pREP4] cells
expressed in Escherichia coli Rosetta cells
expressed in Nicotiana benthamiana
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expressed in Nicotiana tabacum and Escherichia coli BL-21 (DE3) cells
A0A067K3N5
expressed in Synechocystis sp.
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expression in Escherichia coli
expression in Escherichia coli strain BL21(DE3)
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expression in Escherichia coli strain JMSB0373a
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expression in Escherichia coli, His6-tagged type II enzyme
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for expression in Escherichia coli BL21DE3 cells
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into a pET-vector for expression in Escherichia coli Bl21DE3 cells
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into the vector pMD18-T for sequencing, and subsequently into pET-28a+ for expression in Escherichia coli BL21DE3 cells
A9LRT7
overexpressed in Escherichia coli
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overexpression in Escherichia coli
recombinantly expressed with a polyhistidine tag at its N terminus in Escherichia coli BL21
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the plasmid pDL11, which contains the genes idi, gps and egsA, is constructed by inserting idi and egsA into pCW3, derived from pCL1920, pDL11 is transformed into Escherichia coli TOP10 cells
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expressed in Escherichia coli
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expressed in Escherichia coli
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expressed in Escherichia coli
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expressed in Escherichia coli BL21 cells
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expressed in Escherichia coli BL21 cells
expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli Rosetta cells
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expressed in Escherichia coli Rosetta cells
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expression in Escherichia coli
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expression in Escherichia coli
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expression in Escherichia coli
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expression in Escherichia coli
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expression in Escherichia coli
expression in Escherichia coli
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expression in Escherichia coli
expression in Escherichia coli
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expression in Escherichia coli
expression in Escherichia coli
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expression in Escherichia coli
overexpression in Escherichia coli
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overexpression in Escherichia coli
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enzyme expression is increased about 4fold at 4°C, about 2.5fold at 0.1 mM NaCl, about 6fold at 0.15 mM mannitol, and about 7.5fold at 0.03 mM methyl jasmonate
A0A067K3N5
enzyme expression is induced 6 and 24 h after treatment with 30 mM Ag+
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enzyme purified under aerobic conditions is inactive until the flavin cofactor is reduced by NADPH or dithionite or photochemically
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reconstitution of apo-enzyme with 5-deaza-FMN results in an inactive enzyme, whereas reconstitution with 1-deaza-FMN leads to full recovery of activity
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reconstitution of metal-free enzyme with Mg2+, Mn2+, Zn2+, Co2+, Ni2+ or Cd2+ generates active enzyme
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