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(3R)-linalyl diphosphate
(+)-alpha-pinene + diphosphate
-
(3S)-enantiomer is preferred over (3R)-enantiomer
products are (-)-camphene and (-)alpha-pinene
-
?
(3R)-linalyl diphosphate
(-)-alpha-pinene + diphosphate
(3S)-linalyl diphosphate
(+)-alpha-pinene + diphosphate
-
(3S)-enantiomer is preferred over (3R)-enantiomer
products are (+)-camphene and (+)alpha-pinene
-
?
(3S)-linalyl diphosphate
(-)-alpha-pinene + diphosphate
(RS)-alpha-terpinyl diphosphate
limonene + diphosphate
-
-
about 90% limonene, 10% terpinolene
-
?
geranyl diphosphate
(-)-alpha-pinene + diphosphate
geranyl diphosphate
alpha-pinene + diphosphate
neryl diphosphate
(-)-alpha-pinene + diphosphate
additional information
?
-
(3R)-linalyl diphosphate
(-)-alpha-pinene + diphosphate
-
-
products are (-)-alpha-pinene, (-)-beta-pinene, and (-)-camphene
-
?
(3R)-linalyl diphosphate
(-)-alpha-pinene + diphosphate
-
-
products are 17% (-)-alpha-pinene, 9% beta-pinene, 3% camphene, 28% limonene, 9% terpinolene, 23% myrcene, 3% cis-ocimene, 13% trans-ocimene
-
?
(3S)-linalyl diphosphate
(-)-alpha-pinene + diphosphate
-
-
products are (-)-alpha-pinene, (-)-beta-pinene, and (-)-camphene
-
?
(3S)-linalyl diphosphate
(-)-alpha-pinene + diphosphate
-
-
products are 15% (-)-alpha-pinene, 18% beta-pinene, 12% camphene, 11% limonene, 6% terpinolene, 23% myrcene, 3% cis-ocimene, 8% trans-ocimene
-
?
geranyl diphosphate
(-)-alpha-pinene + diphosphate
-
42% terpinolene, 18% (-)-alpha-pinene, 11% (-)-limonene, 10% (-)-beta-pinene plus several minor products
-
?
geranyl diphosphate
(-)-alpha-pinene + diphosphate
-
-
about 40% (-)-alpha-pinene and 60% (-)-beta-pinene
-
?
geranyl diphosphate
(-)-alpha-pinene + diphosphate
-
products are (-)-alpha-pinene and (-)-beta pinene
-
?
geranyl diphosphate
(-)-alpha-pinene + diphosphate
-
products are 20% (-)-alpha-pinene, 6% (-)-beta-pinene, 26% (-)-limonene, 37% (-)-9-beta-phellandrene, and about 11% other monoterpenes
-
?
geranyl diphosphate
(-)-alpha-pinene + diphosphate
-
products are 29% (-)-alpha-pinene, 63% (-)-beta-pinene, 1.8% myrcene, 3.6% limonene
-
?
geranyl diphosphate
(-)-alpha-pinene + diphosphate
-
-
products are 31.9% (-)-alpha-pinene and 63.9% (-)-beta-pinene, plus 4.2% myrcene
-
?
geranyl diphosphate
(-)-alpha-pinene + diphosphate
-
products are 54% (-)-(1S,4R)-camphene, followed by 32% (-)-(1S,5S)-alpha-pinene and 7% (-)-(4S)-limonene. (+)-alpha-pinene is produced to about 5% of (-)-alpha-pinene
-
?
geranyl diphosphate
(-)-alpha-pinene + diphosphate
-
products are (-)-alpha-pinene and (-)-beta-pinene, in a ratio of 6:94
-
?
geranyl diphosphate
(-)-alpha-pinene + diphosphate
-
products are (-)-alpha-pinene and (-)-beta-pinene, in a ratio of about 35:10
-
?
geranyl diphosphate
(-)-alpha-pinene + diphosphate
-
75.2% (-)-beta-pinene + 13.1% (-)-alpha-pinene
-
?
geranyl diphosphate
(-)-alpha-pinene + diphosphate
-
77.9% (-)-alpha-pinene + 9.6% (-)-beta-pinene
-
?
geranyl diphosphate
(-)-alpha-pinene + diphosphate
-
76.6% (-)-alpha-pinene + 9.9% (-)-beta-pinene
-
?
geranyl diphosphate
(-)-alpha-pinene + diphosphate
-
-
-
?
geranyl diphosphate
(-)-alpha-pinene + diphosphate
-
-
main product, plus lower amounts of (-)-beta-pinene
-
?
geranyl diphosphate
(-)-alpha-pinene + diphosphate
-
products are 79% (-)-alpha-pinene, 4.25 (-)-beta-pinene, almost racemic mixtures of camphene and limonene and small amounts of (+)-alpha-pinene and (+)-beta-pinene
-
?
geranyl diphosphate
(-)-alpha-pinene + diphosphate
-
main products (-)-alpha-pinene and (-)-camphene, plus minor products 3-carene, beta-pinene, limonene
-
?
geranyl diphosphate
(-)-alpha-pinene + diphosphate
-
-
25% (-)-alpha-pinene, 31% (-)-camphene, 24% (-)beta-pinene
-
?
geranyl diphosphate
(-)-alpha-pinene + diphosphate
-
-
main products are (-)-alpha-pinene, (-)-beta-pinene and camphene. Primary deuterium isotope effects suggest that (-)-alpha-pinene and (-)-beta-pinene derive from alternative deprotonation of a common enzymatic intermediate
-
?
geranyl diphosphate
(-)-alpha-pinene + diphosphate
-
-
products are (-)-alpha-pinene, (-)-beta-pinene, and (-)-camphene
-
?
geranyl diphosphate
(-)-alpha-pinene + diphosphate
-
-
products are (-)-camphene and (-)alpha-pinene
-
?
geranyl diphosphate
(-)-alpha-pinene + diphosphate
-
-
products are (-)-camphene, (-)-alpha-pinene, (-)-beta-pinene, (-)-limonene and myrcene
-
?
geranyl diphosphate
(-)-alpha-pinene + diphosphate
-
-
products are 28% (-)-alpha-pinene, 35% beta-pinene, 24% camphene, 5% limonene, 2% terpinolene, 6% myrcene
-
?
geranyl diphosphate
(-)-alpha-pinene + diphosphate
-
-
reaction proceeds via (3S)-linalyl diphosphate and the (4S)-alpha-terpinyl cation. Products are (-)-alpha-pinene, (-)-beta-pinene and lesser amounts of related olefins
-
?
geranyl diphosphate
alpha-pinene + diphosphate
-
products are 77% alpha-pinene + 14.7% beta-pinene + 5.5 beta-phellandrene
-
?
geranyl diphosphate
alpha-pinene + diphosphate
-
products are 90% alpha-pinene, 10% beta-pinene
-
?
geranyl diphosphate
alpha-pinene + diphosphate
-
-
-
?
geranyl diphosphate
alpha-pinene + diphosphate
stereochemistry of the product is not specified in the publication
-
-
?
geranyl diphosphate
alpha-pinene + diphosphate
-
-
-
?
geranyl diphosphate
alpha-pinene + diphosphate
stereochemistry of the product is not specified in the publication
-
-
?
neryl diphosphate
(-)-alpha-pinene + diphosphate
-
-
products are (-)-alpha-pinene, (-)-beta-pinene, and (-)-camphene, products are (-)-camphene and (-)alpha-pinene
-
?
neryl diphosphate
(-)-alpha-pinene + diphosphate
-
-
products are 18% (-)-alpha-pinene, 18% beta-pinene, 12% camphene, 42% limonene, 9% terpinolene, 9% myrcene
-
?
additional information
?
-
entire product set is derived in stereochemically consistent fashion via (-)-3S-linalyl diphosphate as intermediate
-
-
?
additional information
?
-
entire product set is derived in stereochemically consistent fashion via (-)-3S-linalyl diphosphate as intermediate
-
-
?
additional information
?
-
GC-MS analysis reaction product analysis. Enzyme PlPIN employs geranyl diphosphate as a specific substrate to produce a-pinene as a unique product
-
-
?
additional information
?
-
-
GC-MS analysis reaction product analysis. Enzyme PlPIN employs geranyl diphosphate as a specific substrate to produce a-pinene as a unique product
-
-
?
additional information
?
-
no substrates: farnesyl diphosphate, geranygeranyl diphosphate
-
-
?
additional information
?
-
-
each product exhibits the same absolute configuration at the center derived from C-6 of geranyl diphosphate, i e. the isopropylidene-substituted carbon
-
-
?
additional information
?
-
-
enzymes removes the C4-proS-hydrogen of the substrate, the C3 proton of the corresponding pinyl cation, with a stereoselectivity exceeding 78% in the formation of (-)-alpha-pinene
-
-
?
additional information
?
-
-
product distribution varies with deuterium substitution at C4 and C10 of substrate. Kinetic isotope effects strongly indicate multiple bicyclic olefin production through the partitioning of common carbocation intermediates
-
-
?
additional information
?
-
-
reaction follows a cisoid, anti-endo-pattern. In the case of geranyl diphosphate, a preassociation mechanism is suggested in which optimum folding of the terpenyl chain precedes the initial ionization step. The alternate substrates are ionized by the cyclases prior to their achieving the optimum orientation for bicyclization
-
-
?
additional information
?
-
-
substrates geranyl, neryl, and (3S)-linalyl diphosphate yield exclusively the (-)-isomer series, whereas (3R)-linalyl diphosphate affords the (+)-isomers at low rates
-
-
?
additional information
?
-
enzyme AvTPS1 (AvPS or pinene synthase) catalyzes GPP to form alpha-pinene and beta-pinene, the enzyme produces 63% beta-pinene as the major product
-
-
?
additional information
?
-
-
enzyme AvTPS1 (AvPS or pinene synthase) catalyzes GPP to form alpha-pinene and beta-pinene, the enzyme produces 63% beta-pinene as the major product
-
-
?
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evolution
the enzyme belongs to the TPS enzyme superfamily, clade TPS-b, where it is clustered with monoterpene synthases
evolution
the enzyme belongs to the TPS superfamily of enzymes
malfunction
mutation Q456L in the alpha-domain (catalytic domain) causes a reduction in pigmentation (PSmut)
malfunction
replacement of residue Q457 with three other amino acids I, K, and V, elevates the activity of the enzyme, while Q457P shows reduced activity
physiological function
in isoform TPS3-silenced plants, alpha-pinene, beta-pinene and beta-phellandrene contents decrease by more than 80%, whereas beta-myrcene is unchanged
physiological function
AvPS (AvTPS1) is not responsible for pinene biosynthesis in the seeds of Amomum villosum, no expression of this gene is detected in the seeds, and the expression of AvPS is not in accordance with the accumulation pattern of pinene in the leaves. But alpha-pinene is widely distributed throughout almost the whole plant, i.e. roots, creeping stems, leaves, pericarp, and seeds. beta-Pinene is found in all the tissues, except seeds. Pinene is a naturally occurring constituent of the essential oils in many plant species that has a relevant role in insect repellency and allelopathy (inhibiting root growth of the tested weed species). Gene AvPS is highly expressed in pericarp, the exterior tissue protecting the fruits against biotic stress, AvPS might be the gene involved in biotic defense in Amonum villosum
physiological function
the terpene synthase PlPIN from Paeonia lactiflora catalyzes the conversion of geranyl pyrophosphate to alpha-pinene and is involved in the biosynthesis of paeoniflorin
additional information
integrative volatile terpenoid profiling and transcriptomics analysis for mining the corresponding genes involved in volatile terpenoid biosynthesis, overview
additional information
-
integrative volatile terpenoid profiling and transcriptomics analysis for mining the corresponding genes involved in volatile terpenoid biosynthesis, overview
additional information
Q457 is located on helix F, which supports a part of the catalytic core and is proximate to the highly conserved residues Y455 and E458
additional information
Q457 is located on helix F, which supports a part of the catalytic core and is proximate to the highly conserved residues Y455 and E458. Residue Q457 is important for catalytic activity
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C372S
replacement with corresponding residue of (-)-camphene synthase, 97% of wild-type activity. Mutant produces an increased proportion of (-)-alpha-pinene and a correspondingly decreased proportion of (-)-beta-pinene, while the levels of total pinenes remains relatively constant
C372S/C480S
replacement with corresponding residue of (-)-camphene synthase, 72% of wild-type activity. Mutant produces an increased proportion of (-)-alpha-pinene and a correspondingly decreased proportion of (-)-beta-pinene
C372S/F597W
replacement with corresponding residue of (-)-camphene synthase, 100% of wild-type activity. Mutant produces an increased proportion of (-)-alpha-pinene and a correspondingly decreased proportion of (-)-beta-pinene
C372S/F597W/S485C/F597W
replacement with corresponding residue of (-)-camphene synthase, 99% of wild-type activity. Mutant produces about 80%(-)-alpha-pinene and 10% (-)-beta-pinene
C372S/S485C
replacement with corresponding residue of (-)-camphene synthase, 92% of wild-type activity. Mutant produces an increased proportion of (-)-alpha-pinene and a correspondingly decreased proportion of (-)-beta-pinene
C480S
replacement with corresponding residue of (-)-camphene synthase, 97% of wild-type activity. Mutant produces an increased proportion of (-)-alpha-pinene and a correspondingly decreased proportion of (-)-beta-pinene, while the levels of total pinenes remains relatively constant
C480S/F597W
replacement with corresponding residue of (-)-camphene synthase, 7% of wild-type activity. Mutant produces an increased proportion of (-)-alpha-pinene and a correspondingly decreased proportion of (-)-beta-pinene
C480S/S485C
replacement with corresponding residue of (-)-camphene synthase, 70% of wild-type activity. Mutant produces an increased proportion of (-)-alpha-pinene and a correspondingly decreased proportion of (-)-beta-pinene
F597W
replacement with corresponding residue of (-)-camphene synthase, 73% of wild-type activity. Mutant produces an increased proportion of (-)-alpha-pinene and a correspondingly decreased proportion of (-)-beta-pinene, while the levels of total pinenes remains relatively constant
S485C
replacement with corresponding residue of (-)-camphene synthase, 100% of wild-type activity. Mutant produces an increased proportion of (-)-alpha-pinene and a correspondingly decreased proportion of (-)-beta-pinene, while the levels of total pinenes remains relatively constant
S485C/F597W
replacement with corresponding residue of (-)-camphene synthase, 68% of wild-type activity. Mutant produces an increased proportion of (-)-alpha-pinene and a correspondingly decreased proportion of (-)-beta-pinene
H346Y
site-directed mutagenesis, mutation in the alpha-domain (catalytic domain), no phenotype, similar to wild-type
Q456K
site-directed mutagenesis, mutation in the alpha-domain (catalytic domain), the mutant shows increased catalytic activity compared to the wild-type
Q456P
site-directed mutagenesis, mutation in the alpha-domain (catalytic domain), the mutant shows 50% reduced catalytic activity compared to the wild-type
Q456V
site-directed mutagenesis, mutation in the alpha-domain (catalytic domain), the mutant shows increased catalytic activity compared to the wild-type
Q456L
site-directed mutagenesis, mutation in the alpha-domain (catalytic domain), the mutant shows a reduction in pigmentation (PSmut) but shows improved catalytic activity
Q456L
site-directed mutagenesis, mutation in the alpha-domain (catalytic domain), the mutant shows increased catalytic activity compared to the wild-type
additional information
replacement of selected amino acid residues in (-)-pinene synthase with the corresponding residues from (-)-camphene synthase in an effort to identify the amino acids responsible for the catalytic diVerences. The approach produces an enzyme in which more than half of the product is channeled through an alternative pathway. Several (-)-pinene synthase to (-)-camphene synthase amino acid substitutions are necessary before catalysis is significantly altered
additional information
to elucidate critical amino acids involved in determining monoterpene product distribution, a combination of domain swapping and reciprocal site-directed mutagenesis was carried out between (-)-(4S)-limonene synthase LS and (-)-(4S)-limonene/(-)-(1S, 5S)-alpha-pinene synthase LPS. Amino acids in the predicted D through F helix regions are critical for product determination. Chimera consisting of N-terminal 218 residues of LS plus corresponding C-terminus of LPS produces 20.7% alpha-pinene, 11.2% sabinene, 7.1% beta-pinene, 25.6% limonene, 35.4% beta-phellandrene, with 42.8% relative activity. Chimera consisting of N-terminal 518 residues of LS plus corresponding C-terminus of LPS produces 6.4% alpha-pinene, 1.5% sabinene, 11% beta-pinene, 64.1% limonene, 17% beta-phellandrene, with 101% relative activity. Chimera consisting of N-terminal 442 residues of LPS plus corresponding C-terminus of LS produces 11% alpha-pinene, 1.4% sabinene, 6.3% beta-pinene, 47.9% limonene, 33.3% beta-phellandrene, with 41.7% relative activity
additional information
-
to elucidate critical amino acids involved in determining monoterpene product distribution, a combination of domain swapping and reciprocal site-directed mutagenesis was carried out between (-)-(4S)-limonene synthase LS and (-)-(4S)-limonene/(-)-(1S, 5S)-alpha-pinene synthase LPS. Amino acids in the predicted D through F helix regions are critical for product determination. Chimera consisting of N-terminal 218 residues of LS plus corresponding C-terminus of LPS produces 20.7% alpha-pinene, 11.2% sabinene, 7.1% beta-pinene, 25.6% limonene, 35.4% beta-phellandrene, with 42.8% relative activity. Chimera consisting of N-terminal 518 residues of LS plus corresponding C-terminus of LPS produces 6.4% alpha-pinene, 1.5% sabinene, 11% beta-pinene, 64.1% limonene, 17% beta-phellandrene, with 101% relative activity. Chimera consisting of N-terminal 442 residues of LPS plus corresponding C-terminus of LS produces 11% alpha-pinene, 1.4% sabinene, 6.3% beta-pinene, 47.9% limonene, 33.3% beta-phellandrene, with 41.7% relative activity
additional information
estalishment of a pinene production system in recombinant Escherichia coli by coexpression of (-)-alpha-pinene synthase from Pinus paeda and Abies grandis GPPS, as well as farnesyl diphosphate synthase mutant IspA(S80F) from Escherichia coli. The isolated alpha-pinene synthase variant PSmut outperforms the wild-type (parent) enzyme in multiple contexts in Escherichia coli and cyanobacteria. The purified variant exhibits drastically altered metal dependency, enabling to keep the activity in the cytosol that is manganese-deficient. Coexpression of this variant with mevalonate pathway enzymes, isopentenyl diphosphate isomerase, and GPP synthase yield 140 mg/l pinene in a flask culture. Screening for PS mutants with higher cellular activity and production method optimization, overview
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Monoterpene synthases from grand fir (Abies grandis): cDNA isolation, characterization, and functional expression of myrcene synthase, (-)-(4S)-limonene synthase, and (-)-(1S,5S)-pinene synthase
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272
21784-21792
1997
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brenda
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Characterization of the constitutive and wound-inducible monoterpene cyclases of grand fir (Abies grandis)
Arch. Biochem. Biophys.
289
267-273
1991
Abies grandis
brenda
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Monoterpene biosynthesis: Isotope effects associates with bicyclic olefin formation catalyzed by pinene synthases from sage (Salvia officinalis)
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308
477-487
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Salvia officinalis
brenda
Croteau, R.; Wheeler, C.J.
Isotopically sensitive branching in the formation of cyclic monoterpenes: Proof that (-)-alpha-pinene and (-)-beta-pinene are synthesized by the same monoterpene cyclase via deprotonation of a common intermediate
Biochemistry
26
5383-5389
1987
Salvia officinalis
brenda
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Biosynthesis of monoterpenes: Enantioselectivity in the enzymatic cyclization of (+)- and (-)-linalyl pyrophospahte to (+)- and (-) pinene and (+)- and (-)-camphene
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263
10063-10071
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264
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Salvia officinalis
brenda
Lewinsohn, E.; Gijzen, M.; Croteau, R.
Wound-inducible pinene cyclase from grand fir: Purification, characterization, and renaturation after SDS-PAGE
Arch. Biochem. Biophys.
293
167-173
1992
Abies grandis
brenda
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Stereochemistry of the proton elimination in the formation of (+)- and (-)-alpha-pinene by monoterpene cyclases from sage (Salvia officinalis)
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308
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Katoh S.;Hyatt D.;Croteau R.
Altering product outcome in Abies grandis (-)-limonene synthase and (-)-limonene/(-)-alpha-pinene synthase by domain swapping and directed mutagenesis
Arch. Biochem. Biophys.
425
65-76
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Cloning and functional characterization of a beta-pinene synthase from Artemisia annua that shows a circadian pattern of expression
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130
477-486
2002
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brenda
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Mutational analysis of a monoterpene synthase reaction: altered catalysis through directed mutagenesis of (-)-pinene synthase from Abies grandis
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439
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2005
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brenda
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Characterization of four terpene synthase cDNAs from methyl jasmonate-induced Douglas-fir, Pseudotsuga menziesii
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66
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2005
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brenda
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cDNA cloning, characterization, and functional expression of four new monoterpene synthase members of the Tpsd gene family from grand fir (Abies grandis)
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368
232-243
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brenda
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Isolation and characterization of an active-site peptide from a monoterpene cyclase labeled with a mechanism-based inhibitor
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317
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Monoterpene synthases of loblolly pine (Pinus taeda) produce pinene isomers and enantiomers
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372
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cDNA isolation, functional expression, and characterization of (+)-alpha-pinene synthase and (-)-alpha-pinene synthase from loblolly pine (Pinus taeda): stereocontrol in pinene biosynthesis
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411
267-276
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Pinus taeda (Q84KL6), Pinus taeda
brenda
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Pinene cyclases I and II. Two enzymes from sage (Salvia officinalis) which catalyze stereospecific cyclizations of geranyl pyrophosphate to monoterpene olefins of opposite configuration
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259
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Insect attack and wounding induce traumatic resin duct development and gene expression of (-)-pinene synthase in Sitka spruce
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133
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brenda
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36
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