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Information on EC 4.2.3.107 - (+)-car-3-ene synthase
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EC Tree
4.2.3.107 (+)-car-3-ene synthaseIUBMB Comments
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 .
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Word Map
The enzyme appears in viruses and cellular organisms
Synonyms
(+)-3-carene synthase, 3-carene synthase, li3cars, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(+)-3-carene synthase
3-carene cyclase
-
-
-
-
3-carene synthase
3CAR
(+)-3-carene synthase
-
-
-
-
3-carene synthase
-
-
-
-
3CAR
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
geranyl diphosphate = (+)-car-3-ene + diphosphate
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
-
,
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SYSTEMATIC NAME
IUBMB Comments
geranyl-diphosphate diphosphate-lyase [cyclizing, (+)-car-3-ene-forming]
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].
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CAS REGISTRY NUMBER
COMMENTARY
153190-33-1
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(3R)-linalyl diphosphate
? + diphosphate
-
-
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
-
?
(3S)-linalyl diphosphate
(+)-car-3-ene + diphosphate
-
-
more than 99.9% optically pure
-
?
(3S)-linalyl diphosphate
? + diphosphate
-
-
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
-
?
neryl diphosphate
limonene + diphosphate
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%)
-
-
?
geranyl diphosphate
(+)-car-3-ene + diphosphate
geranyl diphosphate is converted mainly to 3-carene
-
-
?
geranyl diphosphate
(+)-car-3-ene + diphosphate
-
78% (+)-car-3-ene plus 11% terpinolene plus minor products. No detection of (-)-car-3-ene
-
?
geranyl diphosphate
(+)-car-3-ene + diphosphate
-
major product, plus some terpinolene
-
?
geranyl diphosphate
(+)-car-3-ene + diphosphate
-
wild-type produces 46.2% (+)-car-3-ene, 8.8% (-)-sabinene, 29.7% terpinolene
-
?
geranyl diphosphate
(+)-car-3-ene + diphosphate
-
wild-type produces 49% (+)-car-3-ene, 8.7% (-)-sabinene, 24.7% terpinolene
-
?
geranyl diphosphate
(+)-car-3-ene + diphosphate
-
wild-type produces 67.5% (+)-car-3-ene, 6.9% (-)-sabinene, 15.4% terpinolene
-
?
geranyl diphosphate
(+)-car-3-ene + diphosphate
-
reaction proceeds via an enzyme-bound (3S)-linalyl diphosphate intermediate
more than 99.9% optically pure
-
?
geranyl diphosphate
(+)-car-3-ene + diphosphate
-
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
-
-
?
geranyl diphosphate
(+)-car-3-ene + diphosphate
-
73% (+)-3-carene, 13% (-)-limonene, 6% myrcene, 4% 4-carene and 1% beta-phellandrene
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
no oxygenated or phosphorylated monoterpenes are found in detectable amounts
-
-
?
additional information
?
-
-
no oxygenated or phosphorylated monoterpenes are found in detectable amounts
-
-
?
additional information
?
-
poor substrate: neryl diphosphate. No substrates: farnesyl diphosphate, geranylgeranyl diphosphate
-
-
?
additional information
?
-
poor substrate: neryl diphosphate. No substrates: farnesyl diphosphate, geranylgeranyl diphosphate
-
-
?
additional information
?
-
poor substrate: neryl diphosphate. No substrates: farnesyl diphosphate, geranylgeranyl diphosphate
-
-
?
additional information
?
-
-
poor substrate: neryl diphosphate. No substrates: farnesyl diphosphate, geranylgeranyl diphosphate
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
diethyl dicarbonate
-
formation of a substrate-metal ion complex does not protect against inhibition
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
methyl jasmonate
protein is detected at significantly higher levels in susceptible trees compared to resistant trees at day 7 after methyl jasmonate treatment
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0143
neryl diphosphate
recombinant His-tagged enzyme, pH 7.2, temperature not specified in the publication
0.00369
geranyl diphosphate
recombinant His-tagged enzyme, pH 7.2, temperature not specified in the publication
0.00688
geranyl diphosphate
pH 7.4, 30°C, proteins from both susceptible and resistant plants have similar kinetic parameters
0.0153
geranyl diphosphate
mutant L596F, 30°C, pH not specified in the publication
0.0158
geranyl diphosphate
wild-type, 30°C, pH not specified in the publication
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
isoform 3car3 has an extremely low activity
-
additional information
additional information
isoform 3car3 has an extremely low activity
-
additional information
additional information
isoform 3car3 has an extremely low activity
-
additional information
additional information
-
isoform 3car3 has an extremely low activity
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.636
neryl diphosphate
recombinant His-tagged enzyme, pH 7.2, temperature not specified in the publication
0.098
geranyl diphosphate
wild-type, 30°C, pH not specified in the publication
0.643
geranyl diphosphate
mutant L596F, 30°C, pH not specified in the publication
2.07
geranyl diphosphate
recombinant His-tagged enzyme, pH 7.2, temperature not specified in the publication
2.21
geranyl diphosphate
pH 7.4, 30°C, proteins from both susceptible and resistant plants have similar kinetic parameters
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
44.5
neryl diphosphate
recombinant His-tagged enzyme, pH 7.2, temperature not specified in the publication
0.0062
geranyl diphosphate
wild-type, 30°C, pH not specified in the publication
0.042
geranyl diphosphate
mutant L596F, 30°C, pH not specified in the publication
561
geranyl diphosphate
recombinant His-tagged enzyme, pH 7.2, temperature not specified in the publication
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isoform TPS-3car1, expressed both in trees susceptible and resistant to white pine weevil
UniProt
brenda
isoform TPS-3car2, only expressed in trees resistant to white pine weevil
UniProt
brenda
isoform TPS-3car3, only expressed in trees susceptilble to white pine weevil
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
Li3CARS transcripts are highly abundant in leaves (16fold) as compared to flower tissues
brenda
additional information
-
Li3CARS transcripts are highly abundant in leaves (16fold) as compared to flower tissues
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
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
metabolism
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)
physiological function
additional information
physiological function
(+)-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
physiological function
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
additional information
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
additional information
-
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
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). 3CAR1_PICGL
627
0
71920
Swiss-Prot
Chloroplast (Reliability: 1)
3CAR1_PICSI
627
0
72037
Swiss-Prot
Chloroplast (Reliability: 1)
3CAR1_PICXS
627
0
72078
Swiss-Prot
Chloroplast (Reliability: 1)
3CAR1_PINBN
626
0
71190
Swiss-Prot
Chloroplast (Reliability: 2)
3CAR1_PINCO
626
0
71412
Swiss-Prot
Chloroplast (Reliability: 2)
3CAR2_PICSI
627
0
71645
Swiss-Prot
Chloroplast (Reliability: 3)
3CAR2_PINBN
626
0
71417
Swiss-Prot
Chloroplast (Reliability: 2)
3CAR3_PICSI
627
0
71661
Swiss-Prot
Chloroplast (Reliability: 2)
3CAR1_PICAB
627
0
71913
Swiss-Prot
Chloroplast (Reliability: 3)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 64900, about, sequence calculation from enzyme sequence excluding transit peptides, x * 69600, about, full-length enzyme, sequence calculation
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
sequence contains a N-terminal transit peptide
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
G595A/L596F/F599L
L596F
additional information
G595A/L596F/F599L
shift in product profile, mutant produces 1.8% (+)-car-3-ene, 23.3% (-)-sabinene, 55.2% terpinolene
G595A/L596F/F599L
shift in product profile, mutant produces 4.7% (+)-car-3-ene, 47.4% (-)-sabinene, 35.2% terpinolene
G595A/L596F/F599L
shift in product profile, mutant produces 5.4% (+)-car-3-ene, 29.0% (-)-sabinene, 26.4% terpinolene
L596F
shift in product profile, mutant produces 12.3% (+)-car-3-ene, 37.4% (-)-sabinene, 35.4% terpinolene
L596F
shift in product profile, mutant produces 5% (+)-car-3-ene, 20.9% (-)-sabinene, 53.5% terpinolene
L596F
shift in product profile, mutant produces 9.2% (+)-car-3-ene, 20.2% (-)-sabinene, 32.2% terpinolene
additional information
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
additional information
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
additional information
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
additional information
-
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
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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
treatment with methyl jasmonate induces transient transcript accumulation in stem tissues
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
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
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Savage, T.J.; Hatch, M.W.; Croteau, R.
Monoterpene synthases of Pinus contorta and related conifers. A new class of terpenoid cyclase
J. Biol. Chem.
269
4012-4020
1994
Pinus contorta
brenda
Savage, T.J.; Croteau, R.
Biosynthesis of monoterpenes: regio- and stereochemistry of (+)-3-carene biosynthesis
Arch. Biochem. Biophys.
305
581-587
1993
Pinus contorta
brenda
Hoelscher, D.J.; Williams, D.C.; Wildung, M.R.; Croteau, R.
A cDNA clone for 3-carene synthase from Salvia stenophylla
Phytochemistry
62
1081-1086
2003
Salvia stenophylla (Q8L5J7), Salvia stenophylla
brenda
Hall, D.E.; Robert, J.A.; Keeling, C.I.; Domanski, D.; Quesada, A.L.; Jancsik, S.; Kuzyk, M.A.; Hamberger, B.; Borchers, C.H.; Bohlmann, J.
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
Plant J.
65
936-948
2011
Picea sitchensis (F1CKI6), Picea sitchensis (F1CKI8), Picea sitchensis (F1CKI9), Picea sitchensis
brenda
Fldt, J.; Martin, D.; Miller, B.; Rawat, S.; Bohlmann, J.
Traumatic resin defense in Norway spruce (Picea abies): methyl jasmonate-induced terpene synthase gene expression, and cDNA cloning and functional characterization of (+)-3-carene synthase
Plant Mol. Biol.
51
119-133
2003
Picea abies (Q84SM8), Picea abies
brenda
Savage, T.J.; Ichii, H.; Hume, S.D.; Little, D.B.; Croteau, R.
Monoterpene synthases from Gymnosperms and Angiosperms: stereospecificity and inactivation by cysteinyl- and arginyl-directed modifying reagents
Arch. Biochem. Biophys.
269
4012-4020
1994
Pinus contorta
-
brenda
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
BMC Plant Biol.
9
106
2009
Picea glauca
brenda
Roach, C.R.; Hall, D.E.; Zerbe, P.; Bohlmann, J.
Plasticity and evolution of (+)-3-carene synthase and (-)-sabinene synthase functions of a Sitka spruce monoterpene synthase gene family associated with weevil resistance
J. Biol. Chem.
289
23859-23869
2014
Picea sitchensis (F1CKI6), Picea sitchensis (F1CKI8), Picea sitchensis (F1CKI9), Picea sitchensis
brenda
Adal, A.M.; Sarker, L.S.; Lemke, A.D.; Mahmoud, S.S.
Isolation and functional characterization of a methyl jasmonate-responsive 3-carene synthase from Lavandula x intermedia
Plant Mol. Biol.
93
641-657
2017
Lavandula x intermedia (A0A1V0D8Y5), Lavandula x intermedia
brenda
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