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Information on EC 4.2.3.121 - (+)-alpha-pinene synthase
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EC Tree
4.2.3.121 (+)-alpha-pinene synthaseIUBMB Comments
Cyclase I of Salvia officinalis (sage) gives about equal parts (+)-alpha-pinene and (+)-camphene, whereas cyclase III gives about equal parts of (+)-alpha-pinene and (+)-beta-pinene. (3R)-Linalyl diphosphate can also be used by the enzyme in preference to (3S)-linalyl diphosphate. The 4-pro-R-hydrogen of geranyl diphosphate is lost. Requires Mg2+ (preferred to Mn2+) [1-4]. With synthase II of Pinus taeda (loblolly pine) (+)-alpha-pinene was the only product [5,6]. Requires Mn2+ (preferred to Mg2+). See also EC 4.2.3.122, (+)-beta-pinene synthase, and EC 4.2.3.116, (+)-camphene synthase.
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Word Map
The enzyme appears in viruses and cellular organisms
Synonyms
cyclase iii, (+)-alpha-pinene cyclase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(+)-alpha-pinene cyclase
-
-
-
-
cyclase I
PINS
TPS-(+)apin1
additional information
cyclase I
-
-
-
-
additional information
cf. EC 4.2.3.120, 4.2.3.119, and 4.2.3.122
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
geranyl diphosphate = (+)-alpha-pinene + diphosphate
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
geranyl-diphosphate diphosphate-lyase [cyclizing, (+)-alpha-pinene-forming]
Cyclase I of Salvia officinalis (sage) gives about equal parts (+)-alpha-pinene and (+)-camphene, whereas cyclase III gives about equal parts of (+)-alpha-pinene and (+)-beta-pinene. (3R)-Linalyl diphosphate can also be used by the enzyme in preference to (3S)-linalyl diphosphate. The 4-pro-R-hydrogen of geranyl diphosphate is lost. Requires Mg2+ (preferred to Mn2+) [1-4]. With synthase II of Pinus taeda (loblolly pine) (+)-alpha-pinene was the only product [5,6]. Requires Mn2+ (preferred to Mg2+). See also EC 4.2.3.122, (+)-beta-pinene synthase, and EC 4.2.3.116, (+)-camphene synthase.
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CAS REGISTRY NUMBER
COMMENTARY
11637-21-3
-
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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
(3S)-linalyl diphosphate
(+)-alpha-pinene + diphosphate
-
-
products are 9% (+)-alpha-pinene, 9% camphene, 34% limonene, 28%% terpinolene, 11% myrcene, 2% cis-ocimene, 6% trans-ocimene
-
?
(3S)-linalyl diphosphate
(-)-alpha-pinene + diphosphate
-
(3R)-enantiomer is preferred over (3S)-enantiomer
products are (-)-camphene and (-)alpha-pinene
-
?
(RS)-alpha-terpinyl diphosphate
limonene + diphosphate
-
-
about 90% limonene, 10% terpinolene
-
?
(3R)-linalyl diphosphate
(+)-alpha-pinene + diphosphate
-
-
products are 62% (+)-alpha-pinene, 6% camphene, 11% limonene, 7% terpinolene, 10% myrcene, 1% cis-ocimene, 4% trans-ocimene
-
?
(3R)-linalyl diphosphate
(+)-alpha-pinene + diphosphate
-
(3R)-enantiomer is preferred over (3S)-enantiomer
products are (+)-camphene and (+)alpha-pinene
-
?
geranyl diphosphate
(+)-alpha-pinene + diphosphate
-
products are 39% (R)-(+)-limonene, 22% terpinolene, 16% (1R,5S)-(+)-camphene, 14% (1R,5R)-(+)-alpha-pinene, 8% beta-myrcene and traces of alpha-phellandrene. Preferential formation of the (+)-enantiomers with 94% enantiomeric purity for (1R,5R)-(+)-alpha-pinene. Product pattern changes to 46% limonene, 9% terpinolene, 23% alpha-pinene, 5% beta-myrcene and 4% alpha-phellandrene, when Mn2+ is supplied instead of Mg2+
-
?
geranyl diphosphate
(+)-alpha-pinene + diphosphate
-
91.7% (+)-alpha-pinene
-
?
geranyl diphosphate
(+)-alpha-pinene + diphosphate
-
88.2% of products
-
?
geranyl diphosphate
(+)-alpha-pinene + diphosphate
-
products are 97% (+)-alpha-pinene, 3% (-)-alpha-pinene
-
?
geranyl diphosphate
(+)-alpha-pinene + diphosphate
-
-
31% (+)-alpha-pinene, 29% (+)-camphene, 36% (+)-alpha-pinene, 45% (+)beta-pinene
-
?
geranyl diphosphate
(+)-alpha-pinene + diphosphate
-
-
products are (+)-camphene and (+)alpha-pinene
-
?
geranyl diphosphate
(+)-alpha-pinene + diphosphate
-
-
products are (+)-camphene, (+)-alpha-pinene and (+)-limonene
-
?
geranyl diphosphate
(+)-alpha-pinene + diphosphate
-
-
products are 25% (+)-alpha-pinene, 25% (+)-camphene, 43% (+)-limonene, and 7% myrcene. Reaction in organic solvent gives the same olefin distribution as in aqueous buffer
-
?
geranyl diphosphate
(+)-alpha-pinene + diphosphate
-
-
products are 49% (+)-alpha-pinene, 30% camphene, 10% limonene, 5% terpinolene, 6% myrcene
-
?
geranyl diphosphate
(+)-alpha-pinene + diphosphate
-
-
products of cyclase I are (+)-alpha-pinene and (+)-camphene, products of cyclase III are (+)-alpha-pinene and (+)-beta-pinene
-
?
geranyl diphosphate
(+)-alpha-pinene + diphosphate
-
-
reaction proceeds stereoselectively to (+)-borneol, which is oxidised to (+)-camphor. Configuration at C1 of geranyl pyrophosphate is retained in the enzymatic transformations. The 1-proR-hydrogen of neryl diphosphate gives rise to the exo-alpha-hydrogen of (+)-camphor, and the 1-proS-hydrogen to the endo-alpha-hydrogen, whereas the 1-proS-hydrogen of this precursor gives rise to the exo-alpha-hydrogen of the enantiomeric (-)-camphor, and the 1-proR-hydrogen to the endo-alpha-hydrogen. The configuration at C1 of neryl pyrophosphate is inverted in the cyclizations to alpha- and beta-pinene, and fully consistent with the cyclization model
-
?
geranyl diphosphate
(+)-alpha-pinene + diphosphate
-
-
reaction proceeds via (3R)-linalyl diphosphate and the (4R)-alpha-terpinyl cation. Products are (+)-alpha-pinene, and lesser amounts of related olefins
-
?
geranyl diphosphate
alpha-pinene + diphosphate
-
93% alpha-pinene plus 4% limonene, 1.6% alpha-phellandrene, 1,1% alpha-terpinolene
-
?
geranyl diphosphate
alpha-pinene + diphosphate
-
90.6% alpha-pinene plus 6% limonene, 1.7% alpha-phellandrene, 1,6% alpha-terpinolene
-
?
neryl diphosphate
(+)-alpha-pinene + diphosphate
-
-
products are (+)-camphene and (+)alpha-pinene
-
?
neryl diphosphate
(+)-alpha-pinene + diphosphate
-
-
products are 14% (+)-alpha-pinene, 9% camphene, 62% limonene, 8% terpinolene, 6% myrcene
-
?
additional information
?
-
no substrate: geranylgeranyl diphosphate
-
-
?
additional information
?
-
no substrate: geranylgeranyl diphosphate
-
-
?
additional information
?
-
GC-MS analysis reaction product analysis. Enzyme PlPIN employs geranyl diphosphate as a specific substrate to produce alpha-pinene as a unique product
-
-
?
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-proR-hydrogen of the substrate, the C3 proton trans to the dimethyl bridge of the pinyl nucleus, with a stereoselectivity exceeding 94% 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
?
-
enzyme AvTPS1 (AvPS or pinene synthase) catalyzes geranyl diphosphate to form alpha-pinene and beta-pinene, the enzyme produces 63% beta-pinene as the major product
-
-
?
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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
K+
Mg2+
Mn2+
Mn2+
or Mg2+, required, optimum concentration 0.2 mM. 68% of the efficiency with Mg2+, with change in product pattern to 46% limonene, 9% terpinolene, 23% alpha-pinene, 5% beta-myrcene and 4% alpha-phellandrene, for Mn2+
Mn2+
-
or Mn2+, required. Mg2+ is preferred over Mn2+, Mn2+ shows 60-70% of the activity with Mg2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(+)-(1R)-N,N,4-trimethyl-3-cyclohexenamine
-
aza-analogue of terpenyl cation, uncompetitive
(+)-dimethyl-[(1R)-4-methylcyclohex-3-en-1-yl]sulfonium iodide
-
thia-analogue of terpenyl cation, uncompetitive/noncompetitive
(-)-(1S)-N,N,4-trimethyl-3-cyclohexenamine
-
aza-analogue of terpenyl cation, uncompetitive
(-)-dimethyl-[(1S)-4-methylcyclohex-3-en-1-yl]sulfonium iodide
-
thia-analogue of terpenyl cation, uncompetitive/noncompetitve
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.001
(+)-(1R)-N,N,4-trimethyl-3-cyclohexenamine
-
pH 5.8, 31°C, presence of diphosphate
0.0058
(+)-dimethyl-[(1R)-4-methylcyclohex-3-en-1-yl]sulfonium iodide
-
pH 5.8, 31°C, presence of diphosphate
0.0092
(+)-dimethyl-[(1R)-4-methylcyclohex-3-en-1-yl]sulfonium iodide
-
pH 5.8, 31°C
0.0007
(-)-(1S)-N,N,4-trimethyl-3-cyclohexenamine
-
pH 5.8, 31°C, presence of diphosphate
0.004
(-)-dimethyl-[(1S)-4-methylcyclohex-3-en-1-yl]sulfonium iodide
-
pH 5.8, 31°C, presence of diphosphate
0.0071
(-)-dimethyl-[(1S)-4-methylcyclohex-3-en-1-yl]sulfonium iodide
-
pH 5.8, 31°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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TEMPERATURE 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
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
sequence contains a chloroplast targeting signal of 50 amino acids
brenda
sequence contains a chloroplast targeting signal of 50 amino acids
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
physiological function
additional information
integrative volatile terpenoid profiling and transcriptomics analysis for mining the corresponding genes involved in volatile terpenoid biosynthesis, overview
evolution
the enzyme belongs to the TPS enzyme superfamily, clade TPS-b, where it is clustered with monoterpene synthases
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
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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). BPPS_SALOF
598
0
69292
Swiss-Prot
Chloroplast (Reliability: 2)
CAMPS_PINCO
619
0
71300
Swiss-Prot
Chloroplast (Reliability: 5)
TPS2_CANSA
615
0
71842
Swiss-Prot
Chloroplast (Reliability: 1)
RAPN1_PINBN
628
0
71327
Swiss-Prot
Chloroplast (Reliability: 4)
RAPN1_PINCO
628
0
71551
Swiss-Prot
Chloroplast (Reliability: 4)
PT30_PINTA
628
0
71496
Swiss-Prot
Mitochondrion (Reliability: 5)
A0A6C0QED6_TAICR
617
0
71428
TrEMBL
Chloroplast (Reliability: 2)
A0A2Z4K4P3_9LILI
600
0
68942
TrEMBL
Secretory Pathway (Reliability: 5)
PINS_LAVPL
600
0
69998
Swiss-Prot
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
modeling of structure against the tobacco sesquiterpene synthase 5-epi-aristolochene synthase and the monoterpene synthase bornyl diphosphate synthase from common sage
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diisopropyl ether
-
enzyme is active in hexane, hexadecane, diisopropyl ether, or distilled water, and gives rise to the same olefin distribution of 25% (+)-alpha-pinene, 25% (+)-camphene 43% (+)-limonene, 7% myrcene
hexadecane
-
enzyme is active in hexane, hexadecane, diisopropyl ether, or distilled water, and gives rise to the same olefin distribution of 25% (+)-alpha-pinene, 25% (+)-camphene 43% (+)-limonene, 7% myrcene
hexane
-
enzyme is active in hexane, hexadecane, diisopropyl ether, or distilled water, and gives rise to the same olefin distribution of 25% (+)-alpha-pinene, 25% (+)-camphene 43% (+)-limonene, 7% myrcene. Reactions run in hexane generate product at roughly one-third the rate of companion assays in which the lyophilized protein is rehydrated in distilled water. Relative proportion of alpha-pinene in product distribution is optimal in presence of 5-10% water
additional information
-
enzyme is active in hexane, hexadecane, diisopropyl ether, or distilled water, and gives rise to the same olefin distribution of 25% (+)-alpha-pinene, 25% (+)-camphene 43% (+)-limonene, 7% myrcene
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
lyophilization and rehydration in destilled water results in loss of about 10% of activity
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme PlPIN, cloned from roots, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis and tree, recombinant expression in Escherichia coli strain Transetta (DE3)
expression in Escherichi coli
expression in Escherichia coli
integrative volatile terpenoid profiling and transcriptomics analysis for mining the corresponding genes involved in volatile terpenoid biosynthesis, overview
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wagschal, K.C.; Pyun H.J.; Coates, R.M.; Croteau, R.
Monoterpene biosynthesis: Isotope effects associates with bicyclic olefin formation catalyzed by pinene synthases from sage (Salvia officinalis)
Arch. Biochem. Biophys.
308
477-487
1994
Salvia officinalis
brenda
Croteau, R.; Satterwhite, D.M.; Cane, D.E.; Chang, C.C.
Biosynthesis of monoterpenes: Enantioselectivity in the enzymatic cyclization of (+)- and (-)-linalyl pyrophospahte to (+)- and (-) pinene and (+)- and (-)-camphene
J. Biol. Chem.
263
10063-10071
1988
Salvia officinalis
brenda
Croteau, R.; Satterwhite, D.M.
Biosynthesis of monoterpenes: Stereochemical implications of acyclic and monocyclic olefin formation by (+)- and (-)-pinene cyclases from sage
J. Biol. Chem.
264
15309-15315
1989
Salvia officinalis
brenda
Croteau, R.; Satterwhite, D.M.; Wheeler, C.J.; Felton, N.M.
Biosynthesis of monoterpenes: Stereochemistry of the enzymatic cyclization of geranyl pyrophosphate to (+)-alpha- and (-)beta-pinene
J. Biol. Chem.
264
2075-2080
1989
Salvia officinalis
brenda
Pyun, H.J.; Wagschal, K.C.; Jung, D.; Coates, R.M.; Croteau, R.
Stereochemistry of the proton elimination in the formation of (+)- and (-)-alpha-pinene by monoterpene cyclases from sage (Salvia officinalis)
Arch. Biochem. Biophys.
308
488-496
1994
Salvia officinalis
brenda
Landmann, C.; Fink, B.; Festner, M.; Dregus, M.; Engel, K.H.; Schwab, W.
Cloning and functional characterization of three terpene synthases from lavender (Lavandula angustifolia)
Arch. Biochem. Biophys.
465
417-429
2007
Lavandula angustifolia (Q2XSC6)
brenda
Wheeler, C.J.; Croteau, R.
Terpene cyclase catalysis in organic solvent/minimal water media: demonstration and optimization of (+)-alpha-pinene cyclase activity
Arch. Biochem. Biophys.
248
429-434
1986
Salvia officinalis
brenda
McGeady, P.; Croteau, R.
Isolation and characterization of an active-site peptide from a monoterpene cyclase labeled with a mechanism-based inhibitor
Arch. Biochem. Biophys.
317
149-155
1995
Salvia officinalis
brenda
Phillips, M.; Savage, T.; Croteau, R.
Monoterpene synthases of loblolly pine (Pinus taeda) produce pinene isomers and enantiomers
Arch. Biochem. Biophys.
372
197-204
1999
Pinus taeda
brenda
Phillips, M.A.; Wildung, M.R.; Williams, D.C.; Hyatt, D.C.; Croteau, R.
cDNA isolation, functional expression, and characterization of (+)-alpha-pinene synthase and (-)-alpha-pinene synthase from loblolly pine (Pinus taeda): stereocontrol in pinene biosynthesis
Arch. Biochem. Biophys.
411
267-276
2003
Pinus taeda (Q84KL3), Pinus taeda
brenda
Gambliel, H.; Croteau, R.
Pinene cyclases I and II. Two enzymes from sage (Salvia officinalis) which catalyze stereospecific cyclizations of geranyl pyrophosphate to monoterpene olefins of opposite configuration
J. Biol. Chem.
259
740-748
1984
Salvia officinalis
brenda
Hall, D.; Yuen, M.; Jancsik, S.; Quesada, A.; Dullat, H.; Li, M.; Henderson, H.; Arango-Velez, A.; Liao, N.; Docking, R.; Chan, S.; Cooke, J.; Breuil, C.; Jones, S.; Keeling, C.; Bohlmann, J.
Transcriptome resources and functional characterization of monoterpene synthases for two host species of the mountain pine beetle, lodgepole pine (Pinus contorta) and jack pine (Pinus banksiana)
BMC Plant Biol.
13
80
2013
Pinus banksiana (R9QMR1), Pinus contorta (R9QMW2)
brenda
Benabdelkader, T.; Guitton, Y.; Pasquier, B.; Magnard, J.L.; Jullien, F.; Kameli, A.; Legendre, L.
Functional characterization of terpene synthases and chemotypic variation in three lavender species of section Stoechas
Physiol. Plant.
153
43-57
2015
Lavandula pedunculata (T1RR71), Lavandula viridis (T1RRI8)
brenda
Ma, X.; Guo, J.; Ma, Y.; Jin, B.; Zhan, Z.; Yuan, Y.; Huang, L.
Characterization of a monoterpene synthase from Paeonia lactiflora producing alpha-pinene as its single product
Biotechnol. Lett.
38
1213-1219
2016
Paeonia lactiflora (A0A0G3BIB7)
brenda
Wang, H.; Ma, D.; Yang, J.; Deng, K.; Li, M.; Ji, X.; Zhong, L.; Zhao, H.
An integrative volatile terpenoid profiling and transcriptomics analysis for gene mining and functional characterization of AvBPPS and AvPS involved in the monoterpenoid biosynthesis in Amomum villosum
Front. Plant Sci.
9
846
2018
Wurfbainia villosa (A0A2Z4K4P3)
brenda
