Information on EC 2.5.1.69 - lavandulyl diphosphate synthase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.5.1.69
-
RECOMMENDED NAME
GeneOntology No.
lavandulyl diphosphate synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 dimethylallyl diphosphate = diphosphate + lavandulyl diphosphate
show the reaction diagram
SYSTEMATIC NAME
IUBMB Comments
dimethylallyl-diphosphate:dimethylallyl-diphosphate dimethylallyltransferase (lavandulyl-diphosphate-forming)
Lavandulyl diphosphate is a monoterpene with a non-head-to-tail linkage. It is unlike most monoterpenoids, which are derived from geranyl diphosphate and have isoprene units that are linked head-to-tail. When this enzyme is incubated with dimethylallyl diphosphate and isopentenyl diphosphate, it also forms the regular monoterpene geranyl diphosphate [2]. The enzyme from Artemisia tridentata (big sagebrush) forms both lavandulyl diphosphate and chrysanthemyl diphosphate (see EC 2.5.1.67, chrysanthemyl diphosphate synthase) when dimethylally diphosphate is the sole substrate.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
ssp. spiciformis
-
-
Manually annotated by BRENDA team
big sagebrush
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
the enzyme catalyzes the formation of C10 mononterpene lavandulyl diphosphate, the precursor of the fragrances (R)-lavandulol and (R)-lavandulyl acetate
additional information
-
enzyme structure comparisons, ligand binding structure analysis, residue H78 is essential for catalysis, modelling, overview; the enzyme structure is similar to that of the bacterial cis-prenyl synthase, undecaprenyl diphosphate synthase, and contains an allylic site (S1) in which dimethylallyl diphosphate ionizes and a second site (S2) which houses the dimethylallyl diphosphate nucleophile. Both S-thiolo-dimethylallyl diphosphate and S-thiolo-isopentenyl diphosphate bind intact to S2, but are cleaved to (thio)diphosphate, in S1. His78 is essential for catalysis and is proposed to facilitate diphosphate release in S1, while the P1 phosphate in S2 abstracts a proton from the lavandulyl carbocation to form the LPP product, structure-based mechanism, overview
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 dimethylallyl diphosphate
diphosphate + lavandulyl diphosphate
show the reaction diagram
dimethylallyl diphosphate
(R)-lavandulol + (R)-maconelliol + diphosphate
show the reaction diagram
-
-
in presence of alkaline phosphatase, chimera c98f produces a 6:5 mixture of (R)-lavandulol and (R)-maconelliol and a small amount of planococcyl alcohol
-
?
dimethylallyl diphosphate
diphosphate + chrysanthemyl diphosphate
show the reaction diagram
-
reaction of EC 2.5.1.67, chrysanthemyl diphosphate synthase, a cyclopropanation
an irregular monoterpene product
-
?
dimethylallyl diphosphate
diphosphate + lavandulyl diphosphate
show the reaction diagram
-
a branching reaction
-
-
?
isopentenyl diphosphate + dimethylallyl diphosphate
diphosphate + geranyl diphosphate
show the reaction diagram
-
reaction of EC 2.5.1.10, geranyltranstransferase, a chain elongation
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2 dimethylallyl diphosphate
diphosphate + lavandulyl diphosphate
show the reaction diagram
-
-
-
-
?
dimethylallyl diphosphate
diphosphate + lavandulyl diphosphate
show the reaction diagram
-
a branching reaction
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.208
dimethylallyl diphosphate
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pH 8.0, 30°C
additional information
additional information
-
enzyme displays a sigmoidal saturation curve and Hill coefficient of 2.7, pH 8.0, 30°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1
dimethylallyl diphosphate
Lavandula x intermedia
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pH 8.0, 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9
-
pH profile
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
34500
-
x * 34500, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 34500, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
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the pre-enzyme contains an N-terminal plastidial targeting sequence
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinat DELTA55 LPPS enzyme mutant as dimeric apo-protein and with ligands bound, soaking of LPPS crystals with S-thiolo-dimethylallyl diphosphate and with S-thiolo-isopentenyldiphosphate, X-ray diffraction structure determination and analysis at 1.87 A resolution
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant N-terminally His6-tagged enzyme from Escherichia coli strain XA90 by nickel affinity chromatography to over 95% purity
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recombinant protein
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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gene FDS-5, cDNA library screening, DNA and amino acid sequence determination and analysis, phylogenetic tree, functional expression of N-terminally His6-tagged enzyme in Escherichia coli strain XA90, expression of the fusion FDS-5 transit peptide-GFP protein in Nicotiana tabacum cv. xanthi cells with plastidial localization
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recombinant expression of truncated mutant enzymes with 30, 50, or 55 N-terminal residues deleted. The DELTA30 and DELTA50 proteins are unstable but the DELTA55 protein is successfully expressed
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H78N
-
site-directed mutagenesis, inactive mutant
W100V
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site-directed mutagenesis, the mutant shows 15% of wild-type activity
Y139F
-
site-directed mutagenesis, the mutant shows 62% of wild-type activity
additional information
-
chimera c98f, constructed by replacing the first 98 residues in Artemisia tridentata ssp. spiciformis farnesyl diphosphate synthase with the corresponding sequence from Artemisia tridentata chrysanthemyl diphosphate synthase is able to produce a 6:5 mixture of (R)-lavandulol and (R)-maconelliol and a small amount of planococcyl alcohol in presence of alkaline phosphatase. Chimeric proteins constructed from farnesyl diphosphate synthase, which catalyzes chain elongation, and chrysanthemyl diphosphate synthase, which catalyzes cyclopropanation, catalyze all four of the known isoprenoid coupling reactions to give a mixture of geranyl diphosphate by chain elongation, chrysanthemyl diphosphate by cyclopropanation, lavandulyl diphosphate by branching, and maconelliyl and planococcyl diphosphate by cyclobutanation