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Information on EC 5.4.99.41 - lupeol synthase
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5.4.99.41 lupeol synthaseIUBMB Comments
Also forms some beta-amyrin. The recombinant enzyme from Arabidopsis thaliana gives a 1:1 mixture of lupeol and lupan-3beta,20-diol with small amounts of beta-amyrin, germanicol, taraxasterol and psi-taraxasterol. See EC 4.2.1.128 (lupan-3beta,20-diol synthase).
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Word Map
- 5.4.99.41
-
triterpene
-
triterpenoids
- cycloartenol
- cyclases
- beta-amyrin
-
pentacyclic
-
betulinic
-
oleanolic
-
epoxidase
- mangrove
- glycyrrhizin
- lanosterol
- taraxacum
- phytosterols
- dandelion
-
oleanane
-
kandelia
- glabra
-
oleanane-type
-
soyasaponins
- taraxerol
-
bglus
- rhizophoraceae
- candel
-
bruguiera
- gymnorrhiza
The enzyme appears in viruses and cellular organisms
Synonyms
lupeol synthase, rclus, mdosc5, atlup1, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
lupeol synthase
LUS
OEW
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(3S)-2,3-epoxy-2,3-dihydrosqualene = lupeol
-
-
-
-
(3S)-2,3-epoxy-2,3-dihydrosqualene = lupeol
the C17 configuration of the tetracyclic intermediate dammarenyl cation can be deduced from the angular methyl configuration of the pentacyclic or 6-6-6-6 tetracyclic product
-
(3S)-2,3-epoxy-2,3-dihydrosqualene = lupeol
the final proton abstraction takes place from either of the two gem-dimethyl groups in a 1:1 ratio
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
(3S)-2,3-epoxy-2,3-dihydrosqualene mutase (cyclizing, lupeol-forming)
Also forms some beta-amyrin. The recombinant enzyme from Arabidopsis thaliana [3] gives a 1:1 mixture of lupeol and lupan-3beta,20-diol with small amounts of beta-amyrin, germanicol, taraxasterol and psi-taraxasterol. See EC 4.2.1.128 (lupan-3beta,20-diol synthase).
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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
(18E)-22,23-dihydro-20-oxa-oxidosqualene
3beta-hydroxy-22,23,24,25,26,27-hexanor-17beta-dammaran-20-one + ?
-
the 20-oxa substitution has negligible effect on substrate binding and on the activation energies
sole product
-
?
(3S,22S)-2,3:22,23-dioxidosqualene
(2R,4aR,6aS,6bS,10R,12aS,14aR,14bS)-2-(1-hydroxy-1-methylethyl)-4a,6a,6b,9,9,12a-hexamethylicosahydro-2H-phenanthro[1,2-h]chromen-10-ol + (3alpha,5xi,8alpha,9xi,10alpha,13aalpha,14beta,17xi,20R,24R)-20,24-epoxydammarane-3,25-diol + (3alpha,5xi,8alpha,9xi,10alpha,13alpha,14beta,17xi,24R)-20,24-epoxydammarane-3,25-diol
-
-
products 5_4_99.B3_11.8, 5_4_99.B3_11.9a and 5_4_99.B3_11.9b in ratio 3:4:2, almost complete consumption of substrate
-
?
(S)-2,3-oxidosqualene
beta-amyrin
via dammarenyl cation, low activity
-
-
r
2,3-oxidosqualene
lupeol + germanicol + beta-amyrin + taraxasterol + psi-taraxasterol + 3,20-dihydroxylupane
-
-
-
-
?
3-(omega-oxidogeranlygeranyl)indole
petromindole
-
substrate undergoes protonation, epoxide ring opening, and chair-chair bicyclization to cation. A Markovnikov intermediate is strongly favored, and its cyclization to indole forms the final product
-
-
?
(3S)-2,3-oxidosqualene
lupeol
-
beta-amyrin is a minor product
-
?
(3S)-2,3-oxidosqualene
lupeol
-
no discrimination of the terminal two methyl groups of substrate, proton abstraction occurs from both methyl groups in equal ratio. This is in contrast to Olea europea and Taraxacum officinale enzymes, which abstract the proton exclusively from (Z)-methyl of substrate
-
-
?
(3S)-2,3-oxidosqualene
lupeol
-
strict discrimination of the terminal two methyl groups of substrate, proton abstraction occurs exclusively from (Z)-methyl of 2,3-oxidosqualene. Mechanism is similar in Taraxacum officinale enzyme, but not in Arabidopsis thaliana LUP1 enzyme
-
-
?
(3S)-2,3-oxidosqualene
lupeol
-
strict discrimination of the terminal two methyl groups of substrate, proton abstraction occurs exclusively from (Z)-methyl of 2,3-oxidosqualene. Mechanism is similar in Olea europea enzyme, but not in Arabidopsis thaliana LUP1 enzyme
-
-
?
2,3-oxidosqualene
lupeol
-
-
enzyme additionally catalyzes the stereospecific addition of water to yield 3beta,20-dihydroxylupane without rotation of the C19-C20 bond
-
?
2,3-oxidosqualene
lupeol
-
sole product, no trace of other oxidosqualene derived products can be detected
-
?
2,3-oxidosqualene
lupeol
-
0.9% beta-amyrin and 0.1% alpha-amyrin beside lupeol
-
?
2,3-oxidosqualene
lupeol
lupeol is the main cuticular wax compound during early stages of hypocotyl development. Enzyme is responsible for formation of the cuticular lupeol and thus for the characteristic surface properties of Rhicinus communis stems
-
-
?
2,3-oxidosqualene
lupeol
-
sole product, no trace of other oxidosqualene derived products can be detected
-
?
additional information
?
-
MdOSC5 cyclizes 2,3-oxidosqualene into lupeol and beta-amyrin at a ratio of 95:5
-
-
?
additional information
?
-
-
MdOSC5 cyclizes 2,3-oxidosqualene into lupeol and beta-amyrin at a ratio of 95:5
-
-
?
additional information
?
-
-
the labeling profile of lupeol-3-(3'-hydroxy)-sterarate (procrim b) from a 13CO2 pulse/chase experiment using Pentalinon andrieuxii plants grown under quasi physiological conditions is reported. The 13C-pattern reveals the origin of the isopentyl diphosphate/demethylallyl diphosphate precursors, as well as important details on the cyclization processes occurring in the biosynthesis of lupeol-3-(3'-hydroxy)-sterarate
-
-
?
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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
(S)-2,3-oxidosqualene
beta-amyrin
via dammarenyl cation, low activity
-
-
r
2,3-oxidosqualene
lupeol
lupeol is the main cuticular wax compound during early stages of hypocotyl development. Enzyme is responsible for formation of the cuticular lupeol and thus for the characteristic surface properties of Rhicinus communis stems
-
-
?
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
hypocotyl portion of stem, high activity during early development
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
enzyme MdOSC5 contain the highly conserved DCTAE motif, which is implicated in substrate binding, and six repeats of the QW motifs, typical of the triterpene synthase superfamily. MdOSC5 is located in linkage group LG17, sequence comparisons and phylogenetic analysis
metabolism
physiological function
the enzyme is involved in the biosynthesis of pentacyclic triterpenes, which, in apple, account for 32-70% of the epicuticular waxes, depending on the cultivar
additional information
metabolism
MdOSC1 and MdOSC5 are key genes in apple fruit triterpene biosynthesis, analysis of biosynthetic pathway of triterpenic acids in apple, overview. The gene expression of MdOSC1 is linked to the concentrations of ursolic and oleanolic acid
metabolism
the enzyme is involved in the glycyrrhizin biosynthetic pathway. Controlled drought stress up-regulates the expression of key genes involved in the biosynthesis of triterpenoid saponins and directly enhances the production of secondary metabolites, including glycyrrhizin, in liquorice plants
additional information
analysis of triterpenes from apple fruits in a collection of 20 contrasting apple cultivars, expression patterns of triterpene-related genes in different apple cultivars, overview
additional information
-
analysis of triterpenes from apple fruits in a collection of 20 contrasting apple cultivars, expression patterns of triterpene-related genes in different apple cultivars, overview
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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). LUPS_BETPL
755
0
86473
Swiss-Prot
other Location (Reliability: 2)
LUPS_BRUGY
761
0
87314
Swiss-Prot
other Location (Reliability: 3)
LUPS_GLYGL
758
0
86688
Swiss-Prot
other Location (Reliability: 3)
LUPS_KALDA
765
0
87975
Swiss-Prot
other Location (Reliability: 2)
LUPS_RICCO
769
0
88321
Swiss-Prot
other Location (Reliability: 3)
LUP1_ARATH
757
0
87352
Swiss-Prot
other Location (Reliability: 2)
LUP2_ARATH
763
0
87515
Swiss-Prot
other Location (Reliability: 2)
A0A396HEJ3_MEDTR
172
0
19547
TrEMBL
Mitochondrion (Reliability: 3)
A0A396HCF1_MEDTR
253
0
28584
TrEMBL
other Location (Reliability: 3)
A0A396HCQ5_MEDTR
256
0
29527
TrEMBL
Secretory Pathway (Reliability: 5)
A0A396HGQ5_MEDTR
60
0
7224
TrEMBL
Mitochondrion (Reliability: 2)
A0A396HIQ4_MEDTR
60
0
6907
TrEMBL
other Location (Reliability: 3)
A0A396HIC8_MEDTR
136
1
15355
TrEMBL
Mitochondrion (Reliability: 5)
A0A396HEH0_MEDTR
193
0
22433
TrEMBL
other Location (Reliability: 3)
A0A396HJC1_MEDTR
68
0
8246
TrEMBL
Mitochondrion (Reliability: 4)
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
L256A
-
mutation in region responsible for product differentiation. Mutant produces 3.8% beta-amyrin, 69.5% lupeol, 10% butyrospermol and 13.5% of dammara-18(E),21-dien-3beta-ol, dammara-18(Z),21-dien-3beta-ol and dammara-18(28),21-dien-3beta-ol
L256F
-
mutation in region responsible for product differentiation. Mutant produces 9.8% beta-amyrin, 69.7% lupeol, 17.9% butyrospermol
L256H
-
mutation in region responsible for product differentiation. Mutant produces 3.8% beta-amyrin, 69.5% lupeol, 10% butyrospermol and 13.5% of dammara-18(E),21-dien-3beta-ol, dammara-18(Z),21-dien-3beta-ol and dammara-18(28),21-dien-3beta-ol
L256W
-
mutation in region responsible for product differentiation. Mutant produces 74.8% beta-amyrin, 6.9% lupeol, 9.9% butyrospermol and 8.4% germanicol
L256Y
-
mutation in region responsible for product differentiation. Mutant produces 1.6% beta-amyrin, 54.8% lupeol, 22.7% butyrospermol and 18.7% of dammara-18(E),21-dien-3beta-ol, dammara-18(Z),21-dien-3beta-ol and dammara-18(28),21-dien-3beta-ol
Y258H
-
mutation in region responsible for product differentiation. Mutant produces 43.6% lupeol, 6.2% butyrospermol and 42.4% of dammara-18(E),21-dien-3beta-ol, dammara-18(Z),21-dien-3beta-ol and dammara-18(28),21-dien-3beta-ol
yes
functional expression in Sacchaormyces cerevisiae results in production of lupeol
additional information
additional information
construction of chimera between Arabidopsis thaliana YUP8H12R.43 multifunctional triterpene synthase and LUP1 lupeol synthase. Mutant with N-terminal half of LUP1 and C-terminal half of YUP8H12R.43 gives a product pattern similar to native LUP1 with increased production of minor compounds. Mutant LUP1 containing amino acids corresponding to residues 184 to 398 from YUP8H12R.43 gives an almost identical product pattern with native LUP1. Mutant YUP8H12R.43 containing amino acids corresponding to residues 184 to 395 from LUP1 shows similar product multiplicity to that observed in YUP8H12R.43
additional information
construction of chimeric proteins using beta-amyrin synthase from Panax ginseng and lupeol synthase from Arabidopsis thaliana. Chimera with N-terminal half of beta-amyrin synthase and C-terminal half of lupeol synthase produces beta-amyrin and lupeol in ratio 3:1. Chimera with only the second quarter of the N-terminus from beta-amyrin synthase, produces beta-amyrin and lupeol in a 4:1 ratio, while another chimera created by mixed PCR produces beta-amyrin and lupeol in a 1:4 ratio
additional information
functional expression in Saccharomyces cerevisiae lacking lanosterol synthase activity results in production of lupeol
additional information
-
functional expression in Saccharomyces cerevisiae lacking lanosterol synthase activity results in production of lupeol
additional information
2,3-oxidosqualene production is implemented and subsequently combined with different cyclization reactions catalyzed by the representative oxidosqualene cyclases CAS1 (cycloartenol synthase), LUP1 (lupeol synthase), THAS1 (thalianol synthase) and MRN1 (marneral synthase), derived from model plant Arabidopsis thaliana, in the two alternative hosts for biosynthesis of cyclic plant triterpenes, the metabolically versatile photosynthetic alpha-proteobacterium Rhodobacter capsulatus strain SB1003 and cyanobacterium Synechocystis sp. PCC 6803, triterpene pathway design, overview. While successful accumulation of 2,3-oxidosqualene can be detected by LC-MS analysis in both hosts, cyclase expression results in differential production profiles. CAS1 catalyzes conversion to only cycloartenol, but expression of LUP1 yields lupeol and a triterpenoid matching an oxidation product of lupeol, lupX, in both hosts. In contrast, THAS1 expression does not lead to cyclic product formation in either host, whereas MRN1-dependent production of marnerol and hydroxymarnerol is observed in Synechocystis but not in Rhodobacter capsulatus. 2,3-Oxidosqualene cyclization in heterologous phototrophic bacteria is basically feasible but efficient conversion depends on both the respective cyclase enzyme and individual host properties
additional information
functional expression in Saccharomyces cerevisiae mutant lacking lanosterol synthase activity results in production of lupeol
additional information
functional expression in Saccharomyces cerevisiae results in production of lupeol
additional information
-
functional expression in Saccharomyces cerevisiae results in production of lupeol
additional information
-
functional expression in Saccharomyces cerevisiae mutant with disruption in oxidosqualene cyclase gene results in production of lupeol
additional information
transient expression of MdOSC1 and MdOSC5 together with CYP716A175 confirms the ratio between the different triterpene backbones observed after transient expression of MdOSC1 and MDOSC5 alone, overview
additional information
-
transient expression of MdOSC1 and MdOSC5 together with CYP716A175 confirms the ratio between the different triterpene backbones observed after transient expression of MdOSC1 and MDOSC5 alone, overview
additional information
expression in Saccharomyces cerevisiae lacking in lanosterol synthase activity results in production of lupeol
additional information
expression in Saccharomyces cerevisiae lacking in lanosterol synthase activity results in production of lupeol
additional information
-
expression in Saccharomyces cerevisiae lacking in lanosterol synthase activity results in production of lupeol
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Saccharomyces cerevisae
expression in Saccharomyces cerevisiae
expression in Saccharomyces cerevisiae lacking lanosterol and ergosterol synthase activities
-
expression in Saccharomyces cerevisiae lacking lanosterol synthase activity
-
gene LUP1, recombinant expression in Rhodobacter capsulatus strain SB1003. and Synechocystis sp. PCC 6803 using promoters Pnif and PcoaT, coexpression with CAS1, THAS1, and MRN1. Subcloning in Saccharomyces cerevisiae strain GIL77. Isolation of triterpenes, while cycloartenol and lupeol represent typical plant triterpenes with tetracyclic plant sterol and pentacyclic plant triterpene scaffolds, respectively, thalianol and marneral exhibit more unusual tri- and monocyclic structures. Expression of LUP1 yields lupeol and a triterpenoid matching an oxidation product of lupeol, in both hosts. In Rhodobacter capsulatus and Synechocystis, LUP1-mediated formation of oxidized lupeol derivatives appears to be favored
gene OSC1, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, quantitative real-time PCR expression analysis of the enzyme in apple fruits, functional recombinant expression in Nicotiana benthamiana leaves via transformation by Agrobacterium tumefaciens strain GV3101 resulting in production of alpha-amyrin, beta-amyrin, and lupeol. Cells transiently expressing MdOSC5 cDNA are found to generate lupeol as a major component and beta-amyrin as a minor product, in a ratio of 95:5
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
LUS gene expression is found to increase abruptly 10 h after Phomopsis induction
-
NaNO2 and L-arginine and NO donor sodium nitroprusside (SNP) are found to increase both NO production and LUS gene expression
-
semi-quantitative RT-PCR assays to evaluate the gene expression levels of sequalene synthase (SQS), beta-amyrin synthase (bAS), lupeol synthase (LUS) and cycloartenol synthase (CAS) during stress of seedlings. The expression of the LUS gene is not detectable. Due to osmotic stress, the gene expression levels of SQS and bAS are increased, whereas those of CAS are relatively unchanged at the seedling stage. At the adult plant stage, the expression levels of SQS and bAS are increased under drought stress conditions, whereas the gene expression level of CAS remain relatively constant. controlled drought stress up-regulates the expression of key genes involved in the biosynthesis of triterpenoid saponins and directly enhances the production of secondary metabolites, including glycyrrhizin, in liquorice plant
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Guhling, O.; Hobl, B.; Yeats, T.; Jetter, R.
Cloning and characterization of a lupeol synthase involved in the synthesis of epicuticular wax crystals on stem and hypocotyl surfaces of Ricinus communis
Arch. Biochem. Biophys.
448
60-72
2006
Ricinus communis (Q2XPU7), Ricinus communis
brenda
Sawai, S.; Shindo, T.; Sato, S.; Kaneko, T.; Tabata, S.; Ayabe, S.; Aoki, T.
Functional and structural analysis of genes encoding oxidosqualene cyclases of Lotus japonicus
Plant Sci.
170
247-257
2006
Lotus japonicus
brenda
Zhang, H.; Shibuya, M.; Yokota, S.; Ebizuka, Y.
Oxidosqualene cyclases from cell suspension cultures of Betula platyphylla var. japonica: molecular evolution of oxidosqualene cyclases in higher plants
Biol. Pharm. Bull.
26
642-650
2003
Betula platyphylla (Q8W3Z2)
brenda
Shibuya, M.; Zhang, H.; Endo, A.; Shishikura, K.; Kushiro, T.; Ebizuka, Y.
Two branches of the lupeol synthase gene in the molecular evolution of plant oxidosqualene cyclases
Eur. J. Biochem.
266
302-307
1999
Taraxacum officinale (Q9SLW1), Taraxacum officinale, Olea europaea (Q9SLW3)
brenda
Basyuni, M.; Oku, H.; Tsujimoto, E.; Kinjo, K.; Baba, S.; Takara, K.
Triterpene synthases from the Okinawan mangrove tribe, Rhizophoraceae
FEBS J.
274
5028-5042
2007
Bruguiera gymnorhiza (A8CDT3), Bruguiera gymnorhiza
brenda
Kushiro, T.; Shibuya, M.; Ebizuka, Y.
Chimeric triterpene synthase. A possible model for multifunctional triterpene synthase
J. Am. Chem. Soc.
121
1208-1216
1999
Arabidopsis thaliana (Q9C5M3)
-
brenda
Kushiro, T.; Shibuya, M.; Masuda, K.; Ebizuka, Y.
Mutational studies on triterpene synthases: engineering lupeol synthase into beta-amyrin synthase
J. Am. Chem. Soc.
122
6816-6824
2000
Olea europaea
-
brenda
Xiong, Q.; Zhu, X.; Wilson, W.K.; Ganesan, A.; Matsuda, S.P.
Enzymatic synthesis of an indole diterpene by an oxidosqualene cyclase: mechanistic, biosynthetic, and phylogenetic implications
J. Am. Chem. Soc.
125
9002-9003
2003
Arabidopsis thaliana
brenda
Shan, H.; Segura, M.J.; Wilson, W.K.; Lodeiro, S.; Matsuda, S.P.
Enzymatic cyclization of dioxidosqualene to heterocyclic triterpenes
J. Am. Chem. Soc.
127
18008-18009
2005
Arabidopsis thaliana
brenda
Xiong, Q.; Rocco, F.; Wilson, W.K.; Xu, R.; Ceruti, M.; Matsuda, S.P.
Structure and reactivity of the dammarenyl cation: configurational transmission in triterpene synthesis
J. Org. Chem.
70
5362-5375
2005
Arabidopsis thaliana
brenda
Segura, M.J.; Meyer, M.M.; Matsuda, S.P.
Arabidopsis thaliana LUP1 converts oxidosqualene to multiple triterpene alcohols and a triterpene diol
Org. Lett.
2
2257-2259
2000
Arabidopsis thaliana
brenda
Kushiro, T.; Hoshino, M.; Tsutsumi, T.; Kawai, K.i.; Shiro, M.; Shibuya, M.; Ebizuka, Y.
Stereochemical course in water addition during LUP1-catalyzed triterpene cyclization
Org. Lett.
8
5589-5592
2006
Arabidopsis thaliana
brenda
Herrera, J.B.; Bartel, B.; Wilson, W.K.; Matsuda, S.P.
Cloning and characterization of the Arabidopsis thaliana lupeol synthase gene
Phytochemistry
49
1905-1911
1998
Arabidopsis thaliana (Q9C5M3), Arabidopsis thaliana
brenda
Husselstein-Muller, T.; Schaller, H.; Benveniste, P.
Molecular cloning and expression in yeast of 2,3-oxidosqualene-triterpenoid cyclases from Arabidopsis thaliana
Plant Mol. Biol.
45
75-92
2001
Arabidopsis thaliana (Q9C5M3), Arabidopsis thaliana
brenda
Kushiro, T.; Shibuya, M.; Ebizuka, Y.
Cryptic regiospecificity in deprotonation step of triterpene biosynthesis catalyzed by new members of lupeol synthase
Tetrahedron Lett.
40
5553-5556
1999
Arabidopsis thaliana, Olea europaea, Taraxacum officinale
-
brenda
Kushiro, T.; Shibuya, M.; Masuda, K.; Ebizuka, Y.
A novel multifunctional triterpene synthase from Arabidopsis thaliana
Tetrahedron Lett.
41
7705-7710
2000
Arabidopsis thaliana (Q9C5M3)
-
brenda
Pena-Rodriguez, L.M.; Yam-Puc, A.; Knispel, N.; Schramek, N.; Huber, C.; Grassberger, C.; Ramirez-Torres, F.G.; Escalante-Erosa, F.; Garcia-Sosa, K.; Hiebert-Giesbrecht, M.R.; Chan-Bacab, M.J.; Godoy-Hernandez, G.; Bacher, A.; Eisenreich, W.
Isotopologue profiling of triterpene formation under physiological conditions. Biosynthesis of Lupeol-3-(3-R-hydroxy)-stearate in Pentalinon andrieuxii
J. Org. Chem.
79
2864-2873
2014
Pentalinon andrieuxii
brenda
Fan, G.; Zhai, Q.; Zhan, Y.
Gene expression of lupeol synthase and biosynthesis of nitric oxide in cell suspension cultures of Betula platyphylla in response to a Phomopsis elicitor
Plant Mol. Biol. Rep.
31
296-302
2013
Betula platyphylla
-
brenda
Andre, C.; Legay, S.; Deleruelle, A.; Nieuwenhuizen, N.; Punter, M.; Brendolise, C.; Cooney, J.; Lateur, M.; Hausman, J.; Larondelle, Y.; Laing, W.
Multifunctional oxidosqualene cyclases and cytochrome P450 involved in the biosynthesis of apple fruit triterpenic acids
New Phytol.
211
1279-1294
2016
Malus domestica (A0A142LT04), Malus domestica
brenda
Nasrollahi, V.; Mirzaie-Asl, A.; Piri, K.; Nazeri, S.; Mehrabi, R.
The effect of drought stress on the expression of key genes involved in the biosynthesis of triterpenoid saponins in liquorice (Glycyrrhiza glabra)
Phytochemistry
103
32-37
2014
Glycyrrhiza glabra (Q764T8), Glycyrrhiza glabra
brenda
Loeschcke, A.; Dienst, D.; Wewer, V.; Hage-Huelsmann, J.; Dietsch, M.; Kranz-Finger, S.; Hueren, V.; Metzger, S.; Urlacher, V.B.; Gigolashvili, T.; Kopriva, S.; Axmann, I.M.; Drepper, T.; Jaeger, K.E.
The photosynthetic bacteria Rhodobacter capsulatus and Synechocystis sp. PCC 6803 as new hosts for cyclic plant triterpene biosynthesis
PLoS ONE
12
e0189816
2017
Arabidopsis thaliana (Q9C5M3)
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