The enzyme reacts with (3S)-linalyl diphosphate twice as rapidly as geranyl diphosphate, but 25 times as rapidly as (3R)-linalyl diphosphate. It is assumed that (3S)-linalyl diphosphate is normally formed as an enzyme bound intermediate in the reaction. In the reaction the 5-pro-R hydrogen of geranyl diphosphate is eliminated during cyclopropane ring formation [1,2]. In Picea abies (Norway spruce) and Picea sitchensis (Sitka spruce) terpinolene is also formed [4,6]. See EC 4.2.3.113 terpinolene synthase. (+)-Car-3-ene is associated with resistance of Picea sitchensis (Sitka spruce) to white pine weevil .
The enzyme reacts with (3S)-linalyl diphosphate twice as rapidly as geranyl diphosphate, but 25 times as rapidly as (3R)-linalyl diphosphate. It is assumed that (3S)-linalyl diphosphate is normally formed as an enzyme bound intermediate in the reaction. In the reaction the 5-pro-R hydrogen of geranyl diphosphate is eliminated during cyclopropane ring formation [1,2]. In Picea abies (Norway spruce) and Picea sitchensis (Sitka spruce) terpinolene is also formed [4,6]. See EC 4.2.3.113 terpinolene synthase. (+)-Car-3-ene is associated with resistance of Picea sitchensis (Sitka spruce) to white pine weevil [6].
the velocity of the reaction with the (3S)-linalyl enantiomer is 25fold greater than the velocity with the (3R)-enantiomer and twice that of the natural substrate, geranyl diphosphate. Cyclization of the linalyl intermediate is faster than the coupled isomerization and cyclization of the geranyl substrate
the velocity of the reaction with the (3S)-linalyl enantiomer is 25fold greater than the velocity with the (3R)-enantiomer and twice that of the natural substrate, geranyl diphosphate. Cyclization of the linalyl intermediate is faster than the coupled isomerization and cyclization of the geranyl substrate
low activity, neryl diphosphate is transformed into limonene (33%), alpha-terpinolene (29%) and alpha-thujene (20%) as main products, and minor amounts of a few other monoterpenes including 3-carene (8.5%)
the H located at C1 in the geranyl substrate resides at C5 of product (+)-car-3-ene. The 5-proR hydrogen is eliminated during cyclopropyl ring closure. Cyclopropyl ring formation occurs via a (4S)-alpha-terpinyl cation derived from the anti-endo-cyclization of a (3S)-linalyl diphosphate intermediate
the recombinant Li3CARS converted geranyl diphosphate (GPP) into 3-carene as the major product, Li3CARS also accepts neryl diphosphate (NPP) as a substrate to produce multiple products including a small amount of 3-carene. The catalytic efficiency of Li3CARS to produce 3-carene is about 13fold higher for GPP than NPP. Ligand identification by GC-MS analysis
the recombinant Li3CARS converted geranyl diphosphate (GPP) into 3-carene as the major product, Li3CARS also accepts neryl diphosphate (NPP) as a substrate to produce multiple products including a small amount of 3-carene. The catalytic efficiency of Li3CARS to produce 3-carene is about 13fold higher for GPP than NPP. Ligand identification by GC-MS analysis
evolutionary inference from Lavandula TPS genes, Li3CARS is highly homologous to the Lavandula angustifolia limonene synthase (LaLIMS), and is clustered with this gene under angiosperm mTPSs (TPS-b) subfamily
biosynthesis of monoterpenes catalyzed by recombinant Li3CARS from geranyl diphosphate (GPP, derived from plastidial 2-C-methyl-D-erythritol-4-phosphate pathway) and neryl diphosphate (NPP)
(+)-3-carene is associated with resistance of Sitka spruce to white pine weevil, Pissodes strobi. Variation of the (+)-3-carene phenotype is controlled by copy number variation of TPS-3car genes, variation of gene and protein expression, and variation in catalytic efficiencies
lavenders produce essential oils consisting mainly of monoterpenes, including the potent antimicrobial and insecticidal monoterpene 3-carene. Gene Li3CARS encodes a leaf-specific, methyl jasmonate (MeJA)-responsive monoterpene synthase from Lavandula x intermedia. The transcriptional activity of Li3CARS correlates with 3-carene production. enzyme Li3CARS may play a defensive role in lavenders
homology-based molecular modeling of Li3CARS using the crystal structure of Salvia officinalis bornyl pyrophosphate synthase (SoBPPS) (PDB ID 1N1Z), containing the substrate analogue diphosphate (POP), as template
homology-based molecular modeling of Li3CARS using the crystal structure of Salvia officinalis bornyl pyrophosphate synthase (SoBPPS) (PDB ID 1N1Z), containing the substrate analogue diphosphate (POP), as template
construction of a series of domain swaps and site-directed substitutions between (-)-sabinene synthase and (+)-3-carene synthase isoforms to explore which regions and specific amino acids of these enzymes affect the differences of their product profiles. The amino acid in position 596 is critical for product profiles dominated by (+)-3-carene in (+)-3-carene synthase isoforms. A leucine in this position promotes formation of (+)-3-carene, whereas phenylalanine promotes (-)-sabinene
construction of a series of domain swaps and site-directed substitutions between (-)-sabinene synthase and (+)-3-carene synthase isoforms to explore which regions and specific amino acids of these enzymes affect the differences of their product profiles. The amino acid in position 596 is critical for product profiles dominated by (+)-3-carene in (+)-3-carene synthase isoforms. A leucine in this position promotes formation of (+)-3-carene, whereas phenylalanine promotes (-)-sabinene
construction of a series of domain swaps and site-directed substitutions between (-)-sabinene synthase and (+)-3-carene synthase isoforms to explore which regions and specific amino acids of these enzymes affect the differences of their product profiles. The amino acid in position 596 is critical for product profiles dominated by (+)-3-carene in (+)-3-carene synthase isoforms. A leucine in this position promotes formation of (+)-3-carene, whereas phenylalanine promotes (-)-sabinene
construction of a series of domain swaps and site-directed substitutions between (-)-sabinene synthase and (+)-3-carene synthase isoforms to explore which regions and specific amino acids of these enzymes affect the differences of their product profiles. The amino acid in position 596 is critical for product profiles dominated by (+)-3-carene in (+)-3-carene synthase isoforms. A leucine in this position promotes formation of (+)-3-carene, whereas phenylalanine promotes (-)-sabinene
gene Li3CARS, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of His-tagged enzyme in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme 3-carene synthase from Lavandula intermedia hybrid is methyl jasmonate (MeJA) responsive, the 3CARS expression is upregulated 1.18 to 3.8fold with MeJA 8-72 h post-treatment
transcript levels are increased following methyl jasmonate treatment, with transcripts detected at significantly higher abundance in resistant trees compared to susceptible trees
PCR-based approach to identify BAC clones for two target genes, 3-carene synthase and a cytochrome P450 from a non-arrayed genomic BAC library. Shotgun genomic fragments isolated from the BAC clones were sequenced to a depth of 15.6- and 16.0fold coverage, respectively. Assembly and manual curation yielded sequence scaffolds of 172 kbp long for 3CAR. Inspection of the genomic sequences reveals the intron-exon structures, the putative promoterregions and putative cis-regulatory elements. Sequences related to transposable elements, high complexity repeats and simple repeats are prevalent and comprise approximately 40% of the sequenced genomic DNA
An integrated genomic, proteomic and biochemical analysis of (+)-3-carene biosynthesis in Sitka spruce (Picea sitchensis) genotypes that are resistant or susceptible to white pine weevil
Hamberger, B.; Hall, D.; Yuen, M.; Oddy, C.; Hamberger, B.; Keeling, C.; Ritland, C.; Ritland, K.; Bohlmann, J.
Targeted isolation, sequence assembly and characterization of two white spruce (Picea glauca) BAC clones for terpenoid synthase and cytochrome P450 genes involved in conifer defence reveal insights into a conifer genome
Plasticity and evolution of (+)-3-carene synthase and (-)-sabinene synthase functions of a Sitka spruce monoterpene synthase gene family associated with weevil resistance