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(3R)-linalyl diphosphate
(+)-alpha-pinene + diphosphate
-
Substrates: (3S)-enantiomer is preferred over (3R)-enantiomer
Products: products are (-)-camphene and (-)alpha-pinene
?
(3R)-linalyl diphosphate
(-)-alpha-pinene + diphosphate
(3S)-linalyl diphosphate
(+)-alpha-pinene + diphosphate
-
Substrates: (3S)-enantiomer is preferred over (3R)-enantiomer
Products: products are (+)-camphene and (+)alpha-pinene
?
(3S)-linalyl diphosphate
(-)-alpha-pinene + diphosphate
(RS)-alpha-terpinyl diphosphate
limonene + diphosphate
-
Substrates: -
Products: about 90% limonene, 10% terpinolene
?
geranyl diphosphate
(-)-alpha-pinene + diphosphate
geranyl diphosphate
alpha-pinene + diphosphate
geranyl diphosphate
beta-pinene + diphosphate
-
Substrates: -
Products: -
?
neryl diphosphate
(-)-alpha-pinene + diphosphate
additional information
?
-
(3R)-linalyl diphosphate

(-)-alpha-pinene + diphosphate
-
Substrates: -
Products: products are (-)-alpha-pinene, (-)-beta-pinene, and (-)-camphene
?
(3R)-linalyl diphosphate
(-)-alpha-pinene + diphosphate
-
Substrates: -
Products: 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
-
Substrates: -
Products: products are (-)-alpha-pinene, (-)-beta-pinene, and (-)-camphene
?
(3S)-linalyl diphosphate
(-)-alpha-pinene + diphosphate
-
Substrates: -
Products: 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
-
Substrates: -
Products: about 40% (-)-alpha-pinene and 60% (-)-beta-pinene
?
geranyl diphosphate
(-)-alpha-pinene + diphosphate
Substrates: -
Products: products are 20% (-)-alpha-pinene, 6% (-)-beta-pinene, 26% (-)-limonene, 37% (-)-9-beta-phellandrene, and about 11% other monoterpenes
?
geranyl diphosphate
(-)-alpha-pinene + diphosphate
Substrates: -
Products: products are (-)-alpha-pinene and (-)-beta pinene
?
geranyl diphosphate
(-)-alpha-pinene + diphosphate
-
Substrates: -
Products: products are 31.9% (-)-alpha-pinene and 63.9% (-)-beta-pinene, plus 4.2% myrcene
?
geranyl diphosphate
(-)-alpha-pinene + diphosphate
Substrates: -
Products: 42% terpinolene, 18% (-)-alpha-pinene, 11% (-)-limonene, 10% (-)-beta-pinene plus several minor products
?
geranyl diphosphate
(-)-alpha-pinene + diphosphate
Substrates: -
Products: products are 29% (-)-alpha-pinene, 63% (-)-beta-pinene, 1.8% myrcene, 3.6% limonene
?
geranyl diphosphate
(-)-alpha-pinene + diphosphate
Substrates: -
Products: 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
Substrates: -
Products: products are (-)-alpha-pinene and (-)-beta-pinene, in a ratio of 6:94
?
geranyl diphosphate
(-)-alpha-pinene + diphosphate
Substrates: -
Products: -
?
geranyl diphosphate
(-)-alpha-pinene + diphosphate
Substrates: -
Products: products are (-)-alpha-pinene and (-)-beta-pinene, in a ratio of about 35:10
?
geranyl diphosphate
(-)-alpha-pinene + diphosphate
Substrates: -
Products: 77.9% (-)-alpha-pinene + 9.6% (-)-beta-pinene
?
geranyl diphosphate
(-)-alpha-pinene + diphosphate
Substrates: -
Products: 75.2% (-)-beta-pinene + 13.1% (-)-alpha-pinene
?
geranyl diphosphate
(-)-alpha-pinene + diphosphate
Substrates: -
Products: 76.6% (-)-alpha-pinene + 9.9% (-)-beta-pinene
?
geranyl diphosphate
(-)-alpha-pinene + diphosphate
Substrates: -
Products: 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
-
Substrates: -
Products: main product, plus lower amounts of (-)-beta-pinene
?
geranyl diphosphate
(-)-alpha-pinene + diphosphate
Substrates: -
Products: -
?
geranyl diphosphate
(-)-alpha-pinene + diphosphate
Substrates: -
Products: main products (-)-alpha-pinene and (-)-camphene, plus minor products 3-carene, beta-pinene, limonene
?
geranyl diphosphate
(-)-alpha-pinene + diphosphate
-
Substrates: -
Products: 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
-
Substrates: -
Products: 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
-
Substrates: -
Products: products are (-)-alpha-pinene, (-)-beta-pinene, and (-)-camphene
?
geranyl diphosphate
(-)-alpha-pinene + diphosphate
-
Substrates: -
Products: products are 28% (-)-alpha-pinene, 35% beta-pinene, 24% camphene, 5% limonene, 2% terpinolene, 6% myrcene
?
geranyl diphosphate
(-)-alpha-pinene + diphosphate
-
Substrates: -
Products: 25% (-)-alpha-pinene, 31% (-)-camphene, 24% (-)beta-pinene
?
geranyl diphosphate
(-)-alpha-pinene + diphosphate
-
Substrates: -
Products: products are (-)-alpha-pinene, (-)-beta-pinene, and (-)-camphene
?
geranyl diphosphate
(-)-alpha-pinene + diphosphate
-
Substrates: -
Products: products are (-)-camphene, (-)-alpha-pinene, (-)-beta-pinene, (-)-limonene and myrcene
?
geranyl diphosphate
(-)-alpha-pinene + diphosphate
-
Substrates: -
Products: products are (-)-camphene and (-)alpha-pinene
?
geranyl diphosphate

alpha-pinene + diphosphate
Substrates: -
Products: products are 77% alpha-pinene + 14.7% beta-pinene + 5.5 beta-phellandrene
?
geranyl diphosphate
alpha-pinene + diphosphate
Substrates: -
Products: products are 90% alpha-pinene, 10% beta-pinene
?
geranyl diphosphate
alpha-pinene + diphosphate
Substrates: -
Products: -
?
geranyl diphosphate
alpha-pinene + diphosphate
Substrates: stereochemistry of the product is not specified in the publication
Products: -
?
geranyl diphosphate
alpha-pinene + diphosphate
Substrates: -
Products: -
?
geranyl diphosphate
alpha-pinene + diphosphate
Substrates: stereochemistry of the product is not specified in the publication
Products: -
?
neryl diphosphate

(-)-alpha-pinene + diphosphate
-
Substrates: -
Products: products are (-)-alpha-pinene, (-)-beta-pinene, and (-)-camphene
?
neryl diphosphate
(-)-alpha-pinene + diphosphate
-
Substrates: -
Products: products are 18% (-)-alpha-pinene, 18% beta-pinene, 12% camphene, 42% limonene, 9% terpinolene, 9% myrcene
?
neryl diphosphate
(-)-alpha-pinene + diphosphate
-
Substrates: -
Products: products are (-)-camphene and (-)alpha-pinene
?
additional information

?
-
Substrates: entire product set is derived in stereochemically consistent fashion via (-)-3S-linalyl diphosphate as intermediate
Products: -
?
additional information
?
-
Substrates: entire product set is derived in stereochemically consistent fashion via (-)-3S-linalyl diphosphate as intermediate
Products: -
?
additional information
?
-
Substrates: GC-MS analysis reaction product analysis. Enzyme PlPIN employs geranyl diphosphate as a specific substrate to produce a-pinene as a unique product
Products: -
?
additional information
?
-
-
Substrates: GC-MS analysis reaction product analysis. Enzyme PlPIN employs geranyl diphosphate as a specific substrate to produce a-pinene as a unique product
Products: -
?
additional information
?
-
Substrates: no substrates: farnesyl diphosphate, geranygeranyl diphosphate
Products: -
?
additional information
?
-
-
Substrates: substrates geranyl, neryl, and (3S)-linalyl diphosphate yield exclusively the (-)-isomer series, whereas (3R)-linalyl diphosphate affords the (+)-isomers at low rates
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
?
additional information
?
-
-
Substrates: each product exhibits the same absolute configuration at the center derived from C-6 of geranyl diphosphate, i e. the isopropylidene-substituted carbon
Products: -
?
additional information
?
-
Substrates: 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
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
?
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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
F482A
47% of wild-type activity, products are 4.5% alpha-pinene, 93.2% sabinene, 1.6% limonene
F482A/S491A
18.7% of wild-type activity, products are 4.2% alpha-pinene, 88.4% sabinene, 3.4% limonene
F482I
50% of wild-type activity, products are 3% alpha-pinene, 92.4% sabinene, 0.7% limonene
F482I/S491A
28.7% of wild-type activity, products are 2.7% alpha-pinene, 92.9% sabinene, 2.4% limonene
F482L
18.4% of wild-type activity, products are 4.5% alpha-pinene, 93.2% sabinene, 1.6% limonene
F482R
1.3% of wild-type activity, products are 2.7% alpha-pinene, 31% sabinene, 63.6% limonene
F482T
52.7% of wild-type activity, products are 2.1% alpha-pinene, 94.5% sabinene, 0.3% limonene
F482V
29.5% of wild-type activity, products are 2% alpha-pinene, 94.3% sabinene, 0.3% limonene
F482W
1.5% of wild-type activity, products are 0% alpha-pinene, 19% sabinene, 131% limonene
F482Y
0.6% of wild-type activity, products are 3.5% alpha-pinene, 93.2% sabinene, 1.6% limonene
I335A
54.4% of wild-type activity, products are 78% alpha-pinene, 13% sabinene, 0.6% limonene
S491A
129% of wild-type activity, products are 97.3% alpha-pinene, 1.1% sabinene, 0.1% limonene
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
Q457I
150% of wild-type activity in the magnesium-bound state, while affinity to magnesium ions is not apparently different from wild-type. Mutant possesses higher affinity to manganese than wild-type. Mutation minimally impacts the calculated folding energy
Q457K
increase in catalytic activity, mutation minimally impacts the calculated folding energy
Q457L
130% of wild-type activity in the magnesium-bound state, while affinity to magnesium ions is not apparently different from wild-type. Mutant possesses higher affinity to manganese than wild-type
Q457V
increase in catalytic activity, mutation minimally impacts the calculated folding energy
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

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
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
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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Bohlmann, J.; Steele C.L.; Croteau, R.
Monoterpene synthases from grand fir (Abies grandis): cDNA isolation, characterization, and functional expression of myrcene synthase, (-)-(4S)-limonene synthase, and (-)-(1S,5S)-pinene synthase
J. Biol. Chem.
272
21784-21792
1997
Abies grandis (O24475)
brenda
Gijzen, M.; Lewinsohn, E.; Croteau, R
Characterization of the constitutive and wound-inducible monoterpene cyclases of grand fir (Abies grandis)
Arch. Biochem. Biophys.
289
267-273
1991
Abies grandis
brenda
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.; 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
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
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
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
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
2004
Abies grandis (Q9M7C9), Abies grandis
brenda
Lu, S.; Xu, R.; Jia, J.W.; Pang, J.; Matsuda, S.P.T.; Chen, X-Y.
Cloning and functional characterization of a beta-pinene synthase from Artemisia annua that shows a circadian pattern of expression
Plant Physiol.
130
477-486
2002
Artemisia annua (Q94G53)
brenda
Hyat, D.C.; Croteau, R.
Mutational analysis of a monoterpene synthase reaction: altered catalysis through directed mutagenesis of (-)-pinene synthase from Abies grandis
Arch. Biochem. Biophys.
439
222-233
2005
Abies grandis (O24475)
brenda
Huber, D.P.; Philippe, R.N.; Godard, K.A.; Sturrock, R.N.; Bohlmann, J.
Characterization of four terpene synthase cDNAs from methyl jasmonate-induced Douglas-fir, Pseudotsuga menziesii
Phytochemistry
66
1427-1439
2005
Pseudotsuga menziesii (Q4QSN3)
brenda
Bohlmann, J.; Phillips, M.; Ramachandiran, V.; Katoh, S.; Croteau, R.
cDNA cloning, characterization, and functional expression of four new monoterpene synthase members of the Tpsd gene family from grand fir (Abies grandis)
Arch. Biochem. Biophys.
368
232-243
1999
Abies grandis (Q9M7D0), Abies grandis (Q948Z0)
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 (Q84KL6), Pinus taeda
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Pinus taeda (Q84KL6)
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Gossypium hirsutum (U5N0S4)
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Gossypium hirsutum (U5N0S4)
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Pinus taeda (Q84KL6)
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Pinus taeda (Q84KL6)
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Wurfbainia villosa (A0A2Z4K4P3), Wurfbainia villosa
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Paeonia lactiflora (A0A0G3BIB7)
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Wurfbainia villosa
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