Information on EC 4.2.3.24 - amorpha-4,11-diene synthase

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The expected taxonomic range for this enzyme is: Artemisia annua

EC NUMBER
COMMENTARY
4.2.3.24
-
RECOMMENDED NAME
GeneOntology No.
amorpha-4,11-diene synthase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
(2E,6E)-farnesyl diphosphate = amorpha-4,11-diene + diphosphate
show the reaction diagram
-
-
-
-
(2E,6E)-farnesyl diphosphate = amorpha-4,11-diene + diphosphate
show the reaction diagram
enzyme first catalyzes a 1,6 ring closure with a subsequent 1,10 closure
-
(2E,6E)-farnesyl diphosphate = amorpha-4,11-diene + diphosphate
show the reaction diagram
mechanism involves isomerzation of farnesyl diphosphate to (R)-nerolidyl diphosphate, ionization, and C-1,C-6-ring closure to generate a bisabolyl cation, followed by a 1,3-hydride shift, 1,10-ring closure, and deprotonation at either C-12 or C-13
-
(2E,6E)-farnesyl diphosphate = amorpha-4,11-diene + diphosphate
show the reaction diagram
mechanism includes a bisabolyl carbocation and 1,3-hydride shift, detailed analysis
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
isomerization
-
-
PATHWAY
KEGG Link
MetaCyc Link
artemisinin biosynthesis
-
Biosynthesis of secondary metabolites
-
Sesquiterpenoid and triterpenoid biosynthesis
-
SYSTEMATIC NAME
IUBMB Comments
(2E,6E)-farnesyl diphosphate diphosphate-lyase (amorpha-4,11-diene-forming)
Requires Mg2+ and Mn2+ for activity. This is a key enzyme in the biosynthesis of the antimalarial endoperoxide artemisinin [3]. Catalyses the formation of both olefinic [e.g. amorpha-4,11-diene, amorpha-4,7(11)-diene, gamma-humulene and beta-sesquiphellandrene] and oxygenated (e.g. amorpha-4-en-7-ol) sesquiterpenes, with amorpha-4,11-diene being the major product. When geranyl diphosphate is used as a substrate, no monoterpenes are produced [2].
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
ADS3963
Q9AR04
-
amorpha-4,11-diene synthase
-
-
amorpha-4,11-diene synthase
Q9AR04
-
amorphadiene synthase
-
-
CAS REGISTRY NUMBER
COMMENTARY
259213-60-0
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
; expression in Escherichia coli with His-tag
-
-
Manually annotated by BRENDA team
Escherichia coli strain contains plasmid-borne copies of the mevalonate pathway from Saccharomyces cerevisiae, as well as the amorphadiene synthase(ADS) gene from Artemisia annua
-
-
Manually annotated by BRENDA team
expression in Escherichia coli
Swissprot
Manually annotated by BRENDA team
expression in Escherichia coli
-
-
Manually annotated by BRENDA team
expression in Escherichia coli and nicotiana tabacum
Swissprot
Manually annotated by BRENDA team
presence of conserved domain DDxxD and a motif SlwD, a casein kinase II phosphorylation domain site at position 104-107 in ADS3963 protein
Swissprot
Manually annotated by BRENDA team
sequence of wild-type enzyme; yeast-conform variant of the gene, production in a transformed yeast
Swissprot
Manually annotated by BRENDA team
the expression pattern of the GUS reporter gene, driven by the promoter of Artemisia annua ADS, is investigated in the model plant Arabidopsis thaliana
-
-
Manually annotated by BRENDA team
Artemisia annua L.
-
UniProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2E,6E)-farnesyl diphosphate
amorpha-4,11-diene + diphosphate
show the reaction diagram
-
-
-
-
?
(2E,6E)-farnesyl diphosphate
amorpha-4,11-diene + diphosphate
show the reaction diagram
-
-
dditionally production of 15 different sesquiterpenoids, detailed reaction scheme
-
-
2-trans,6-trans-farnesyl diphosphate
amorpha-4,11-diene + diphosphate
show the reaction diagram
-
-
-
-
?
2-trans,6-trans-farnesyl diphosphate
amorpha-4,11-diene + diphosphate
show the reaction diagram
Q9AR04
-
-
-
?
2-trans,6-trans-farnesyl diphosphate
amorpha-4,11-diene + diphosphate
show the reaction diagram
-
-
-
-
?
2-trans,6-trans-farnesyl diphosphate
amorpha-4,11-diene + diphosphate
show the reaction diagram
Q9AR04
-
amorpha-4,11-diene is a precursor of artemisin, a three-step oxidation is necessary
-
?
farnesyl diphosphate
amorpha-4,11-diene + diphosphate
show the reaction diagram
-
-
additionally production of 15 different sesquiterpenoids, detailed reaction scheme
-
?
farnesyl diphosphate
amorpha-4,7-diene + diphosphate
show the reaction diagram
Q9AR04
-
-
-
?
farnesyl diphosphate
amorpha-4,7-diene + diphosphate
show the reaction diagram
-
-
-
-
?
farnesyl diphosphate
amorpha-4,7-diene + diphosphate
show the reaction diagram
-
-
configuration is 1S,6R,7R,10R-amorpha-4,11-diene
-
?
farnesyl diphosphate
amorpha-4,7-diene + diphosphate
show the reaction diagram
Q9AR04
-
major product, minor product is beat-sesquiphellandrene
-
?
farnesyl diphosphate
amorpha-4,7-diene + diphosphate
show the reaction diagram
-
-
more than 90% of product, minor products are amorpha-4,7(11)-diene, gamma-humulene, amorpha-4-en-7-ol and others
-
?
Geranyl diphosphate
?
show the reaction diagram
-
-
-
-
-
geranyl diphosphate
alpha-terpineol + ocimene + myrcene + linalool
show the reaction diagram
-
alpha-terpineol (39%) + ocimene (24%) + myrcene (19%) + linalool (11%)
-
-
?
geranyl diphosphate + H2O
amorpha-4,11-diene + diphosphate
show the reaction diagram
-
substrate in the presence of Mn2+ but not with Mg2+ or Co2+
-
-
?
additional information
?
-
Q9AR04
key enzyme in the biosynthetic pathway of the antimalarial drug artemisinin
-
-
-
additional information
?
-
-
H-1si-proton of substrate is transferred during the cyclization reaction to carbon 10 of amorphadiene, as a result of a 1,3-hydride-shift follwing initial 1,6 ring closure, while the H-1re-proton of substrate is retained on C-6 of the product
-
-
-
additional information
?
-
-
no substrate: geranyl diphosphate
-
-
-
additional information
?
-
-
significant increased product selectivity in the presence of Mn2+ or Co2+
-
-
-
additional information
?
-
-
ADS is one of the two rate-limiting enzymes in the amorphadiene biosynthetic pathway
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2-trans,6-trans-farnesyl diphosphate
amorpha-4,11-diene + diphosphate
show the reaction diagram
-
-
-
-
?
2-trans,6-trans-farnesyl diphosphate
amorpha-4,11-diene + diphosphate
show the reaction diagram
Q9AR04
-
-
-
?
2-trans,6-trans-farnesyl diphosphate
amorpha-4,11-diene + diphosphate
show the reaction diagram
-
-
-
-
?
2-trans,6-trans-farnesyl diphosphate
amorpha-4,11-diene + diphosphate
show the reaction diagram
Q9AR04
-
amorpha-4,11-diene is a precursor of artemisin, a three-step oxidation is necessary
-
?
additional information
?
-
Q9AR04
key enzyme in the biosynthetic pathway of the antimalarial drug artemisinin
-
-
-
additional information
?
-
-
ADS is one of the two rate-limiting enzymes in the amorphadiene biosynthetic pathway
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Co2+
-
increase in product selectivity at pH 6.5, inhibitory above 0.5 mM
Mg2+
-
Km-value 0.07 mM
Mn2+
-
Km-value 0.013 mM
Mn2+
-
increase in product selectivity at pH 6.5, inhibitory above 0.5 mM
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Co2+
-
inhibitory above 0.5 mM
Cu2+
-
complete inhibition
Mn2+
-
inhibitory above 0.5 mM
Ni2+
-
inhibiton
Zn2+
-
complete inhibition
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0006
-
farnesyl diphosphate
-
presence of Co2+, pH 7.5, 30C
0.0006
-
farnesyl diphosphate
-
pH 7.0
0.0007
-
farnesyl diphosphate
-
presence of Co2+, pH 6.5, 30C
0.0016
-
farnesyl diphosphate
-
presence of Mg2+, pH 9.5, 30C
0.002
-
farnesyl diphosphate
-
presence of Mg2+, pH 7.5, 30C
0.0033
-
farnesyl diphosphate
-
presence of Mg2+, pH 6.5, 30C
0.0042
-
farnesyl diphosphate
-
presence of Mn2+, pH 7.5, 30C
0.008
-
farnesyl diphosphate
-
presence of Mn2+, pH 6.5, 30C
0.0169
-
geranyl diphosphate
-
presence of Mn2+, pH 6.5, 30C
0.0282
-
geranyl diphosphate
-
presence of Mn2+, pH 7.5, 30C
additional information
-
additional information
-
the apparent Km value is 3.4 mmol/l
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00078
-
(2E,6E)-farnesyl diphosphate
-
presence of Co2+, pH 7.5, 30C
0.0013
-
(2E,6E)-farnesyl diphosphate
-
presence of Co2+, pH 6.5, 30C
0.0043
-
(2E,6E)-farnesyl diphosphate
-
presence of Mg2+, pH 7.5, 30C
0.0068
-
(2E,6E)-farnesyl diphosphate
-
presence of Mg2+, pH 6.5, 30C
0.0108
-
(2E,6E)-farnesyl diphosphate
-
presence of Mn2+, pH 7.5, 30C
0.015
-
(2E,6E)-farnesyl diphosphate
-
presence of Mn2+, pH 6.5, 30C
0.0154
-
(2E,6E)-farnesyl diphosphate
-
presence of Mg2+, pH 9.5, 30C
0.00034
-
geranyl diphosphate
-
presence of Mn2+, pH 7.5, 30C
0.0007
-
geranyl diphosphate
-
presence of Mn2+, pH 6.5, 30C
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.3
-
(2E,6E)-farnesyl diphosphate
-
presence of Co2+, pH 7.5, 30C
263972
1.9
-
(2E,6E)-farnesyl diphosphate
-
presence of Mn2+, pH 6.5, 30C
263972
2.1
-
(2E,6E)-farnesyl diphosphate
-
presence of Co2+, pH 6.5, 30C; presence of Mg2+, pH 6.5, 30C
263972
2.2
-
(2E,6E)-farnesyl diphosphate
-
presence of Mg2+, pH 7.5, 30C
263972
2.6
-
(2E,6E)-farnesyl diphosphate
-
presence of Mn2+, pH 7.5, 30C
263972
9.7
-
(2E,6E)-farnesyl diphosphate
-
presence of Mg2+, pH 9.5, 30C
263972
0.012
-
geranyl diphosphate
-
presence of Mn2+, pH 7.5, 30C
10850
0.042
-
geranyl diphosphate
-
presence of Mn2+, pH 6.5, 30C
10850
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.000002
-
-
strain BL21DE3 pLysS Tuner, 6 g/l Inducer, sorbitol, betaine; strain BL21DE3 pLysS Tuner, no Inducer; strain BL21DE3 pLysS, without IPTG, sorbitol, betaine
0.000003
-
-
strain BL21DE3 pLysS Tuner, 1 g/l Inducer, sorbitol, betaine; strain BL21DE3 pLysS Tuner, 3 g/l Inducer, sorbitol, betaine; strain BL21DE3 pLysS Tuner, no Inducer, sorbitol, betaine
0.000008
-
-
strain BL21DE3 pLysS Tuner, 6 g/l Inducer; strain BL21DE3 pLysS Tuner, without IPTG; strain BL21DE3 pLysS Tuner, without IPTG, sorbitol, betaine
0.000013
-
-
strain BL21DE3 pLysS Tuner, 1 g/l Inducer; strain BL21DE3 pLysS Tuner, 3 g/l Inducer
0.00002
-
-
strain BL21DE3 pLysS, 6 g/l Inducer; strain BL21DE3 pLysS, no Inducer; strain BL21DE3 pLysS, no Inducer, sorbitol, betaine; strain BL21DE3 pLysS Tuner, 0.1 mM IPTG; strain BL21DE3 pLysS Tuner, 0.2 mM IPTG; strain BL21DE3 pLysS Tuner, 0.5 mM IPTG; strain BL21DE3 pLysS, without IPTG
0.00003
-
-
strain BL21DE3, 0.1 mM IPTG; strain BL21DE3, 0.2 mM IPTG; strain BL21DE3, 0.5 mM IPTG; strain BL21DE3, 1 g/l Inducer; strain BL21DE3, 3 g/l Inducer; strain BL21DE3, 6 g/l Inducer; strain BL21DE3 pLysS, 0.1 mM IPTG; strain BL21DE3 pLysS, 0.2 mM IPTG; strain BL21DE3 pLysS, 0.5 mM IPTG; strain BL21DE3 pLysS, 1 g/l Inducer; strain BL21DE3 pLysS, 1 g/l Inducer, sorbitol, betaine; strain BL21DE3 pLysS, 3 g/l Inducer; strain BL21DE3 pLysS, 3 g/l Inducer, sorbitol, betaine; strain BL21DE3 pLysS, 6 g/l Inducer, sorbitol, betaine; strain BL21DE3 Tuner, 0.1 mM IPTG; strain BL21DE3 Tuner, 0.2 mM IPTG; strain BL21DE3 Tuner, 0.5 mM IPTG; strain BL21DE3 Tuner, no Inducer; strain BL21DE3 Tuner, without IPTG
0.00005
-
-
strain BL21DE3, no Inducer; strain BL21DE3 Tuner, 1 g/l Inducer; strain BL21DE3 Tuner, 3 g/l Inducer; strain BL21DE3 Tuner, 6 g/l Inducer; strain BL21DE3, without IPTG
0.00006
-
-
strain BL21DE3, without IPTG, sorbitol, betaine
0.00008
-
-
strain BL21DE3 Tuner, without IPTG, sorbitol, betaine
0.0001
-
-
strain BL21DE3 Tuner, 1 g/l Inducer, sorbitol, betaine
0.00012
-
-
strain BL21DE3, 1 g/l Inducer, sorbitol, betaine; strain BL21DE3, no Inducer, sorbitol, betaine; strain BL21DE3 Tuner, 3 g/l Inducer, sorbitol, betaine
0.00013
-
-
strain BL21DE3, 3 g/l Inducer, sorbitol, betaine; strain BL21DE3 Tuner, 6 g/l Inducer, sorbitol, betaine; strain BL21DE3 Tuner, no Inducer, sorbitol, betaine
0.00015
-
-
strain BL21DE3, 0.2 mM IPTG, sorbitol, betaine; strain BL21DE3, 6 g/l Inducer, sorbitol, betaine
0.0002
-
-
strain BL21DE3, 0.1 mM IPTG, sorbitol, betaine; strain BL21DE3, 0.5 mM IPTG, sorbitol, betaine; strain BL21DE3 pLysS, 0.1 mM IPTG, sorbitol, betaine; strain BL21DE3 pLysS, 0.2 mM IPTG, sorbitol, betaine; strain BL21DE3 pLysS, 0.5 mM IPTG, sorbitol, betaine; strain BL21DE3 pLysS Tuner, 0.1 mM IPTG, sorbitol, betaine; strain BL21DE3 Tuner, 0.1 mM IPTG, sorbitol, betaine; strain BL21DE3 Tuner, 0.2 mM IPTG, sorbitol, betaine; strain BL21DE3 Tuner, 0.5 mM IPTG, sorbitol, betaine
0.00025
-
-
strain BL21DE3 pLysS Tuner, 0.2 mM IPTG, sorbitol, betaine; strain BL21DE3 pLysS Tuner, 0.5 mM IPTG, sorbitol, betaine
3.53
-
Q9AR04
pH 7.5, 35C, recombinant enzyme
additional information
-
Q9AR04
Strains transformed with the yeast-conform allele (ADSm) are more efficient in terms of production of amorpha-4,11-diene than those transformed with the plant gene. Production of amorpha-4,11-diene in the engineered yeasts containing ADSm gene is 10-20fold higher than the control
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
7
-
broad
6.5
-
-
activity assay
7
-
-
activity assay
7.5
9
-
broad
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.5
-
-
pH-minimum, increasing enzyme activity with increasing pH above 7.5
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
-
activity assay
37
-
-
activity assay
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.3
-
Q9AR04
calculated
5.59
-
Q9AR04
calculated
5.66
-
Q9AR04
calculated
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
young flower
Manually annotated by BRENDA team
-
juvenile leaf
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
56000
-
-
gel filtration
69300
-
-
detemined by SDS-PAGE, recombinant protein extended with 17 amino acids after fusion to the His-tag
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
Q9AR04
x * 63900, calculated, x * 63500, SDS-PAGE
?
-
x * 65000, SDS-PAGE, recombinant enzyme with His-tag
?
-
x * 61000, SDS-PAGE of recombinant protein with His6-tag
?
-
x * 63900, calculated
?
Q9AR04
x 62200, calculated
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
Q9AR04
sequence contains no plastidial targeting sequence
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
3D-modeling of structure. Predicted model shows that the putative ADS3963 protein contains 72% of alpha-helices, 23% beta-turns and 26% of random coils. Based on docking studies with substrate farnesyl diphosphate, the stretches Ala321-Ala324-Lys-398, Ala234-Val237-Phe283-Thr286-Tyr-287, Ser94-Met95-Trp141-Trp430-Asn434, Ser94-Arg96-Glu104-Leu107-Lys142-Lys431, Lys137-Arg143-Ile147-Ala150-Gln151-Leu478 and Ser218-Gly219-Tyr224-Arg228-Cys352-Met356-Aln450 may constitute to substrate binding
Q9AR04
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
purified by immobilized metal affinity chromatography on a column loaded with Co2+
-
purified by immobilized metal affinity chromatography on a column loaded with Ni2+
-
recombinant enzyme with his-tag
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
; expression in Escherichia coli with His-tag
-
Escherichia coli DH10B is used for cloning and strain DH1 is used for expression, developing and optimizing of a simple cloning system for expression of the amorphadiene biosynthetic pathway. The pathway genes are originally constructed by assembly of the operons onto three different plasmids, each with a different copy number and Escherichia coli promoter. Escherichia coli DH1 harboring pAM45MevT and pADS exhibits a significant increase in amorphadiene production (21 mg/l at 75 h), which is 3fold higher than the original base-strain DH1 pMevTpMBISpADS. To increase ADS expression, transforming of DH1pAM92 with pADS is done, resulting in a combined ADS gene dosage of 30-45 copies/cell. The strain exhibits an increase in amorphadiene production over DH1pAM92, but still does not approach the peak titers obtained with DH1pAM45pADS
-
expression of a synthetic Artemesia annua amorphadiene synthase gene under control of a strong constitutive promoter ((p)gpdA) in Aspergillus nidulans yields altered product distribution. The transformants produces only small amounts of amorphadiene, but much larger amounts of similar sesquiterpenes normally produced as minor by-products in plants. Expression of ADS in Escherichia coli produces almost exclusively amorpha-4,11-diene. The host environment can greatly impact the terpenes produced from terpene synthases.
-
into the pET28 vector for expression in Escherichia coli BL21DE3, BL21DE3 Tuner, BL21DE3 pLysS and BL21DE3 pLysS Tuner cells using different inducing agents
-
into the pET30a+ vector for expression in Escherichia coli
-
into the pYeDP60 vector for expression in Saccharomyces cerevisiae, and, in addition, introduced into the yeast genome by homologous recombination
-
The ADS gene is mutated to the yeast-conform variant ADSm (based on the original DNA sequence of the wild-type gene, the plant gene codons are modified to Saccharomyces cerevisiae preferred with the intact protein primary structure, production in a transformed yeast.) The 8 low-usage codons, AGG (Arg), CGA (Arg), CGG (Arg), CGC (Arg), CCG (Pro), CTC (Leu), GCG (Ala) and ACG (Thr) in ADSm gene are changed with bias codons in Saccharomyces cerevisiae. The synonymous codons of 5 amino acids are changed into one preferred codon in ADSm gene, such as Gln (CAA), Glu (GAA), Cys (TGT), Arg (AGA) and Gly (GGT), which can improve the abundance of cognate tRNA when translated. Three genes, encoding the FPP synthase, HMG-CoA reductase and ADS, are plasmid-transformed together.
Q9AR04
the open reading frame of amorpha-4,11-diene synthase is fused to the green fluorescent proten reporter gene for introducing into the Arabidopsis protoplasts
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
strongly induced by methyl jasmonate and chitosan
-
temporary peak in expression after salicylic acid treatment
-
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
protein is recovered from the inclusion body fraction
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
agriculture
C5HG79
overexpression of HMG-Co A reductase gene from Catharanthus roseus G. Don and amorpha-4,11-diene synthase gene from Artemisia annua in Artemisia annua L. plants to study their effects on artemisinin yields. The artemisinin contents are up to 7.7fold increased in the transgenics
agriculture
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growth of self-pollinated F2 plants under optimized growth conditions, consisting of long day, i.e. 16 h of light, and short day, i.e.9 h of light exposures in a phytotron. The leaves on the main stems exhibit obvious morphological changes, from indented single leaves to odd, pinnately compound leaves. Leaves and flowers form glandular and T-shaped trichomes on their surfaces. The glandular trichome densities increased from the bottom to the top leaves. Leaves, flowers, and young seedlings of F2 plants produce artemisinin. In leaves, the levels of artemisinin increases from the bottom to the top of the plants, showing a positive correlation to the density increase of glandular trichomes. Progeny of self-pollinated plants express the amorpha-4, 11-diene synthase and cytochrome P450 monooxygenase 71 AV1 genes
drug development
Q9AR04
amorpha-4,11-diene is a precursor of artemisinin, an endoperoxide sesquiterpene lactone produced in plant Artemisia annua L., one of the most important agents in the treatment of malaria, particularly in the form of artemisinin-based combination therapies
drug development
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amorpha-4,11-diene is an anti-malarial drug precursor
medicine
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amorpha-4,11-diene is a presursor of artemisinin, artemisinin and derivates are used for the treatment of malaria
pharmacology
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amorpha-4,11-diene is a precursor of artemisinin, an important agent in the treatment of malaria, produced via oxidation
synthesis
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expression of enzyme plus mevalonate isoprenoid pathway genes from Saccharomyces cerevisiae in Escherichia coli results in synthesis of amorpha-4,11-diene up to 0.024 mg caryophyllene per ml
synthesis
Q9AR04
production of amorpha-4,11-diene, expression in Nicotiana tabacum gives 0.2 to 1.7 ng per g fresh weight
agriculture
Artemisia annua L.
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overexpression of HMG-Co A reductase gene from Catharanthus roseus G. Don and amorpha-4,11-diene synthase gene from Artemisia annua in Artemisia annua L. plants to study their effects on artemisinin yields. The artemisinin contents are up to 7.7fold increased in the transgenics
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