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 prenyl diphosphate and 3-methylbut-3-en-1-yl diphosphate, it also forms the regular monoterpene geranyl diphosphate . The enzyme from Artemisia tridentata (big sagebrush) forms both lavandulyl diphosphate and chrysanthemyl diphosphate (see EC 2.5.1.67, chrysanthemyl diphosphate synthase) when prenyl diphosphate is the sole substrate.
the two dimethylallyl diphosphate molecules, both allylic diphosphates, condense via a so-called head-to-middle condensation to form the (C10) monterpene, lavandulyl diphosphate. 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 catalytic mechanism, overview
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 prenyl diphosphate and 3-methylbut-3-en-1-yl 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 prenyl diphosphate is the sole substrate.
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
reaction of EC 2.5.1.1, chrysanthemyl diphosphate synthase is an inefficient promiscuous enzyme, which synthesizes the irregular monoterpenes chrysanthemyl diphosphate (CPP), lavandulyl diphosphate (LPP), and trace quantities of maconelliyl diphosphate (MPP) from two molecules of DMAPP, and couples IPP to DMAPP to give GPP
reaction of EC 2.5.1.67, chrysanthemyl diphosphate synthase is an inefficient promiscuous enzyme, which synthesizes the irregular monoterpenes chrysanthemyl diphosphate (CPP), lavandulyl diphosphate (LPP), and trace quantities of maconelliyl diphosphate (MPP) from two molecules of DMAPP, and couples IPP to DMAPP to give GPP
chrysanthemyl diphosphate synthase is an inefficient promiscuous enzyme, which synthesizes the irregular monoterpenes chrysanthemyl diphosphate (CPP), lavandulyl diphosphate (LPP), and trace quantities of maconelliyl diphosphate (MPP) from two molecules of DMAPP, and couples IPP to DMAPP to give GPP
Artemisia tridentata chrysanthemyl diphosphate synthase is an example of an enzyme that has evolved recently from a highly specialized parent. The origins of farnesyl diphosphate synthase date back to the very beginning of cellular life, and the enzyme has perfected its ability to catalyze chain-elongation. In contrast, Artemisia tridentata chrysanthemyl diphosphate synthase has recently evolved from Artemisia tridentata diphosphate synthase, presumably by gene duplication and random mutagenesis but is still a promiscuous inefficient catalyst in comparison with farnesyl diphosphate synthase
the enzyme catalyzes the formation of C10 mononterpene lavandulyl diphosphate, the precursor of the fragrances (R)-lavandulol and (R)-lavandulyl acetate
geranyl diphosphate synthase small subunit SSU1 can modify the chain-length specificity of geranylgeranyl diphosphate synthase GGPPS, but has no effect on lavandulyl diphosphate synthase LPPS activity
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
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
truncated protein with 55 N-terminal residues deleted (DELTA55 protein) is successfully expressed, and crystallized. Crystals diffract to 1.87 A resolution. The enzyme crystallizes in the orthorhombic space group C222(1)
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
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
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
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
The biosynthetic origin of irregular monoterpenes in Lavandula: isolation and biochemical characterization of a novel cis prenyl diphosphate synthase gene - lavandulyl diphosphate synthase
J. Biol. Chem.
288
6333-6341
2013
Lavandula x intermedia (M4QSY7), Lavandula x intermedia
Structure-function studies of Artemisia tridentata farnesyl diphosphate synthase and chrysanthemyl diphosphate synthase by site-directed mutagenesis and morphogenesis