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(25R)-3beta-hydroxycholest-5-en-27-oate
?
-
-
-
-
?
(2E,6E)-farnesyl diphosphate
amorpha-4,11-diene + diphosphate
2-trans,6-trans-farnesyl diphosphate
amorpha-4,11-diene + diphosphate
farnesyl diphosphate
amorpha-4,11-diene + diphosphate
-
-
additionally production of 15 different sesquiterpenoids, detailed reaction scheme
-
?
farnesyl diphosphate
amorpha-4,7-diene + diphosphate
Geranyl diphosphate
?
-
-
-
-
?
geranyl diphosphate
alpha-terpineol + ocimene + myrcene + linalool
-
alpha-terpineol (39%) + ocimene (24%) + myrcene (19%) + linalool (11%)
-
-
?
geranyl diphosphate + H2O
amorpha-4,11-diene + diphosphate
-
substrate in the presence of Mn2+ but not with Mg2+ or Co2+
-
-
?
additional information
?
-
(2E,6E)-farnesyl diphosphate
amorpha-4,11-diene + diphosphate
-
-
-
-
?
(2E,6E)-farnesyl diphosphate
amorpha-4,11-diene + diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate
amorpha-4,11-diene + diphosphate
A2TEY7
-
-
-
?
(2E,6E)-farnesyl diphosphate
amorpha-4,11-diene + diphosphate
-
-
dditionally production of 15 different sesquiterpenoids, detailed reaction scheme
-
?
2-trans,6-trans-farnesyl diphosphate
amorpha-4,11-diene + diphosphate
-
-
-
-
?
2-trans,6-trans-farnesyl diphosphate
amorpha-4,11-diene + diphosphate
-
-
-
?
2-trans,6-trans-farnesyl diphosphate
amorpha-4,11-diene + diphosphate
-
-
-
-
?
2-trans,6-trans-farnesyl diphosphate
amorpha-4,11-diene + diphosphate
-
amorpha-4,11-diene is a precursor of artemisin, a three-step oxidation is necessary
-
?
farnesyl diphosphate
amorpha-4,7-diene + diphosphate
-
-
-
-
?
farnesyl diphosphate
amorpha-4,7-diene + diphosphate
-
-
-
?
farnesyl diphosphate
amorpha-4,7-diene + diphosphate
-
-
configuration is 1S,6R,7R,10R-amorpha-4,11-diene
-
?
farnesyl diphosphate
amorpha-4,7-diene + diphosphate
-
major product, minor product is beat-sesquiphellandrene
-
?
farnesyl diphosphate
amorpha-4,7-diene + diphosphate
-
-
more than 90% of product, minor products are amorpha-4,7(11)-diene, gamma-humulene, amorpha-4-en-7-ol and others
-
?
additional information
?
-
key enzyme in the biosynthetic pathway of the antimalarial drug artemisinin
-
-
?
additional information
?
-
-
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
-
-
?
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0.0009
(25R)-3beta-hydroxycholest-5-en-27-oate
-
pH 7.5
0.00191 - 0.033
(2E,6E)-farnesyl diphosphate
0.0006 - 0.008
farnesyl diphosphate
0.0169 - 0.0282
geranyl diphosphate
additional information
additional information
-
the apparent Km value is 3.4 mmol/l
-
0.00191
(2E,6E)-farnesyl diphosphate
-
mutant enzyme T447S, at pH 7.0 and 30°C
0.00203
(2E,6E)-farnesyl diphosphate
-
wild type enzyme, at pH 7.0 and 30°C
0.00256
(2E,6E)-farnesyl diphosphate
-
mutant enzyme T399S, at pH 7.0 and 30°C
0.00366
(2E,6E)-farnesyl diphosphate
-
mutant enzyme T296V, at pH 7.0 and 30°C
0.00792
(2E,6E)-farnesyl diphosphate
-
mutant enzyme T399S/T447S, at pH 7.0 and 30°C
0.0108
(2E,6E)-farnesyl diphosphate
mutant enzyme T296A, at pH 7.2 and 30°C
0.0153
(2E,6E)-farnesyl diphosphate
wild type enzyme, at pH 7.2 and 30°C
0.0198
(2E,6E)-farnesyl diphosphate
mutant enzyme T296I, at pH 7.2 and 30°C
0.0282
(2E,6E)-farnesyl diphosphate
mutant enzyme T296V, at pH 7.2 and 30°C
0.033
(2E,6E)-farnesyl diphosphate
mutant enzyme T296S, at pH 7.2 and 30°C
0.0006
farnesyl diphosphate
-
pH 7.0
0.0006
farnesyl diphosphate
-
presence of Co2+, pH 7.5, 30°C
0.0007
farnesyl diphosphate
-
presence of Co2+, pH 6.5, 30°C
0.0016
farnesyl diphosphate
-
presence of Mg2+, pH 9.5, 30°C
0.002
farnesyl diphosphate
-
presence of Mg2+, pH 7.5, 30°C
0.0033
farnesyl diphosphate
-
presence of Mg2+, pH 6.5, 30°C
0.0042
farnesyl diphosphate
-
presence of Mn2+, pH 7.5, 30°C
0.008
farnesyl diphosphate
-
presence of Mn2+, pH 6.5, 30°C
0.0169
geranyl diphosphate
-
presence of Mn2+, pH 6.5, 30°C
0.0282
geranyl diphosphate
-
presence of Mn2+, pH 7.5, 30°C
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0.00078 - 0.518
(2E,6E)-farnesyl diphosphate
0.00034 - 0.0007
geranyl diphosphate
0.00078
(2E,6E)-farnesyl diphosphate
-
presence of Co2+, pH 7.5, 30°C
0.0013
(2E,6E)-farnesyl diphosphate
-
presence of Co2+, pH 6.5, 30°C
0.0013
(2E,6E)-farnesyl diphosphate
mutant enzyme T296I, at pH 7.2 and 30°C
0.0015
(2E,6E)-farnesyl diphosphate
mutant enzyme T296V, at pH 7.2 and 30°C
0.0043
(2E,6E)-farnesyl diphosphate
-
presence of Mg2+, pH 7.5, 30°C
0.0059
(2E,6E)-farnesyl diphosphate
mutant enzyme T296A, at pH 7.2 and 30°C
0.0068
(2E,6E)-farnesyl diphosphate
-
presence of Mg2+, pH 6.5, 30°C
0.0075
(2E,6E)-farnesyl diphosphate
mutant enzyme T296S, at pH 7.2 and 30°C
0.0108
(2E,6E)-farnesyl diphosphate
-
presence of Mn2+, pH 7.5, 30°C
0.015
(2E,6E)-farnesyl diphosphate
-
presence of Mn2+, pH 6.5, 30°C
0.0154
(2E,6E)-farnesyl diphosphate
-
presence of Mg2+, pH 9.5, 30°C
0.0162
(2E,6E)-farnesyl diphosphate
-
mutant enzyme T296V, at pH 7.0 and 30°C
0.0163
(2E,6E)-farnesyl diphosphate
wild type enzyme, at pH 7.2 and 30°C
0.186
(2E,6E)-farnesyl diphosphate
-
wild type enzyme, at pH 7.0 and 30°C
0.321
(2E,6E)-farnesyl diphosphate
-
mutant enzyme T399S, at pH 7.0 and 30°C
0.334
(2E,6E)-farnesyl diphosphate
-
mutant enzyme T447S, at pH 7.0 and 30°C
0.518
(2E,6E)-farnesyl diphosphate
-
mutant enzyme T399S/T447S, at pH 7.0 and 30°C
0.00034
geranyl diphosphate
-
presence of Mn2+, pH 7.5, 30°C
0.0007
geranyl diphosphate
-
presence of Mn2+, pH 6.5, 30°C
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0.05 - 174
(2E,6E)-farnesyl diphosphate
0.012 - 0.042
geranyl diphosphate
0.05
(2E,6E)-farnesyl diphosphate
mutant enzyme T296V, at pH 7.2 and 30°C
0.07
(2E,6E)-farnesyl diphosphate
mutant enzyme T296I, at pH 7.2 and 30°C
0.23
(2E,6E)-farnesyl diphosphate
mutant enzyme T296S, at pH 7.2 and 30°C
0.55
(2E,6E)-farnesyl diphosphate
mutant enzyme T296A, at pH 7.2 and 30°C
1.06
(2E,6E)-farnesyl diphosphate
wild type enzyme, at pH 7.2 and 30°C
1.3
(2E,6E)-farnesyl diphosphate
-
presence of Co2+, pH 7.5, 30°C
1.9
(2E,6E)-farnesyl diphosphate
-
presence of Mn2+, pH 6.5, 30°C
2.1
(2E,6E)-farnesyl diphosphate
-
presence of Co2+, pH 6.5, 30°C
2.1
(2E,6E)-farnesyl diphosphate
-
presence of Mg2+, pH 6.5, 30°C
2.2
(2E,6E)-farnesyl diphosphate
-
presence of Mg2+, pH 7.5, 30°C
2.6
(2E,6E)-farnesyl diphosphate
-
presence of Mn2+, pH 7.5, 30°C
4.4
(2E,6E)-farnesyl diphosphate
-
mutant enzyme T296V, at pH 7.0 and 30°C
9.7
(2E,6E)-farnesyl diphosphate
-
presence of Mg2+, pH 9.5, 30°C
65
(2E,6E)-farnesyl diphosphate
-
mutant enzyme T399S/T447S, at pH 7.0 and 30°C
92
(2E,6E)-farnesyl diphosphate
-
wild type enzyme, at pH 7.0 and 30°C
125
(2E,6E)-farnesyl diphosphate
-
mutant enzyme T399S, at pH 7.0 and 30°C
174
(2E,6E)-farnesyl diphosphate
-
mutant enzyme T447S, at pH 7.0 and 30°C
0.012
geranyl diphosphate
-
presence of Mn2+, pH 7.5, 30°C
0.042
geranyl diphosphate
-
presence of Mn2+, pH 6.5, 30°C
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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
3.53
pH 7.5, 35°C, recombinant enzyme
0.000002
strain BL21DE3 pLysS Tuner, 6 g/l Inducer, sorbitol, betaine
0.000002
strain BL21DE3 pLysS Tuner, no Inducer
0.000002
strain BL21DE3 pLysS, without IPTG, sorbitol, betaine
0.000003
strain BL21DE3 pLysS Tuner, 1 g/l Inducer, sorbitol, betaine
0.000003
strain BL21DE3 pLysS Tuner, 3 g/l Inducer, sorbitol, betaine
0.000003
strain BL21DE3 pLysS Tuner, no Inducer, sorbitol, betaine
0.000008
strain BL21DE3 pLysS Tuner, 6 g/l Inducer
0.000008
strain BL21DE3 pLysS Tuner, without IPTG
0.000008
strain BL21DE3 pLysS Tuner, without IPTG, sorbitol, betaine
0.000013
strain BL21DE3 pLysS Tuner, 1 g/l Inducer
0.000013
strain BL21DE3 pLysS Tuner, 3 g/l Inducer
0.00002
strain BL21DE3 pLysS Tuner, 0.1 mM IPTG
0.00002
strain BL21DE3 pLysS Tuner, 0.2 mM IPTG
0.00002
strain BL21DE3 pLysS Tuner, 0.5 mM IPTG
0.00002
strain BL21DE3 pLysS, 6 g/l Inducer
0.00002
strain BL21DE3 pLysS, no Inducer
0.00002
strain BL21DE3 pLysS, no Inducer, sorbitol, betaine
0.00002
strain BL21DE3 pLysS, without IPTG
0.00003
strain BL21DE3 pLysS, 0.1 mM IPTG
0.00003
strain BL21DE3 pLysS, 0.2 mM IPTG
0.00003
strain BL21DE3 pLysS, 0.5 mM IPTG
0.00003
strain BL21DE3 pLysS, 1 g/l Inducer
0.00003
strain BL21DE3 pLysS, 1 g/l Inducer, sorbitol, betaine
0.00003
strain BL21DE3 pLysS, 3 g/l Inducer
0.00003
strain BL21DE3 pLysS, 3 g/l Inducer, sorbitol, betaine
0.00003
strain BL21DE3 pLysS, 6 g/l Inducer, sorbitol, betaine
0.00003
strain BL21DE3 Tuner, 0.1 mM IPTG
0.00003
strain BL21DE3 Tuner, 0.2 mM IPTG
0.00003
strain BL21DE3 Tuner, 0.5 mM IPTG
0.00003
strain BL21DE3 Tuner, no Inducer
0.00003
strain BL21DE3 Tuner, without IPTG
0.00003
strain BL21DE3, 0.1 mM IPTG
0.00003
strain BL21DE3, 0.2 mM IPTG
0.00003
strain BL21DE3, 0.5 mM IPTG
0.00003
strain BL21DE3, 1 g/l Inducer
0.00003
strain BL21DE3, 3 g/l Inducer
0.00003
strain BL21DE3, 6 g/l Inducer
0.00005
strain BL21DE3 Tuner, 1 g/l Inducer
0.00005
strain BL21DE3 Tuner, 3 g/l Inducer
0.00005
strain BL21DE3 Tuner, 6 g/l Inducer
0.00005
strain BL21DE3, no Inducer
0.00005
strain BL21DE3, without IPTG
0.00012
strain BL21DE3 Tuner, 3 g/l Inducer, sorbitol, betaine
0.00012
strain BL21DE3, 1 g/l Inducer, sorbitol, betaine
0.00012
strain BL21DE3, no Inducer, sorbitol, betaine
0.00013
strain BL21DE3 Tuner, 6 g/l Inducer, sorbitol, betaine
0.00013
strain BL21DE3 Tuner, no Inducer, sorbitol, betaine
0.00013
strain BL21DE3, 3 g/l Inducer, sorbitol, betaine
0.00015
strain BL21DE3, 0.2 mM IPTG, sorbitol, betaine
0.00015
strain BL21DE3, 6 g/l Inducer, sorbitol, betaine
0.0002
strain BL21DE3 pLysS Tuner, 0.1 mM IPTG, sorbitol, betaine
0.0002
strain BL21DE3 pLysS, 0.1 mM IPTG, sorbitol, betaine
0.0002
strain BL21DE3 pLysS, 0.2 mM IPTG, sorbitol, betaine
0.0002
strain BL21DE3 pLysS, 0.5 mM IPTG, sorbitol, betaine
0.0002
strain BL21DE3 Tuner, 0.1 mM IPTG, sorbitol, betaine
0.0002
strain BL21DE3 Tuner, 0.2 mM IPTG, sorbitol, betaine
0.0002
strain BL21DE3 Tuner, 0.5 mM IPTG, sorbitol, betaine
0.0002
strain BL21DE3, 0.1 mM IPTG, sorbitol, betaine
0.0002
strain BL21DE3, 0.5 mM IPTG, sorbitol, betaine
0.00025
strain BL21DE3 pLysS Tuner, 0.2 mM IPTG, sorbitol, betaine
0.00025
strain BL21DE3 pLysS Tuner, 0.5 mM IPTG, sorbitol, betaine
additional information
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
additional information
-
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
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G400A
the mutant accumulates more alpha-bisabolol compared to the wild type enzyme
H392A
the mutant displays 3-4fold increase in activity compared to the wild type enzyme
H392I
the mutant displays 3-4fold increase in activity compared to the wild type enzyme
H392N
the mutant displays 3-4fold increase in activity compared to the wild type enzyme
H448A
the mutant shows about 4fold increase in catalytic efficiency compared to the wild type enzyme
H448C
the mutant displays 4fold increase in activity compared to the wild type enzyme
H448F
the mutant displays 4fold increase in activity compared to the wild type enzyme
H448G
the mutant displays 2fold increase in activity compared to the wild type enzyme
H448M
the mutant displays 2fold increase in activity compared to the wild type enzyme
H448N
the mutant displays 3fold increase in activity compared to the wild type enzyme
H448Q
the mutant displays 3fold increase in activity compared to the wild type enzyme
H448R
the mutant displays 2fold increase in activity compared to the wild type enzyme
H448S
the mutant displays 3fold increase in activity compared to the wild type enzyme
H448T
the mutant displays 2fold increase in activity compared to the wild type enzyme
H448V
the mutant displays 2fold increase in activity compared to the wild type enzyme
K449M
the mutant displays 3-4fold increase in activity compared to the wild type enzyme
L374Y
-
the mutant enzyme is inactive toward 1,10 closure
L374Y/G439S
-
the mutant produces 51.9% bisabolyl-type compounds, including alpha-bisabolol (4.7%), beta-bisabolol (7.4%), and cis-gamma-bisabolene (38.6%)
L374Y/L404V/L405I/G439S
-
the mutations lead to an enzyme generating 80% monocyclic bisabolyltype sesquiterpenes
L515A
the mutant accumulates more alpha-bisabolol compared to the wild type enzyme
L515C
the mutant accumulates more alpha-bisabolol compared to the wild type enzyme
L515G
the mutant accumulates more alpha-bisabolol compared to the wild type enzyme
L515S
the mutant accumulates more alpha-bisabolol compared to the wild type enzyme
L515T
the mutant accumulates more alpha-bisabolol compared to the wild type enzyme
Q518A
the mutant displays 3-4fold increase in activity compared to the wild type enzyme
Q518L
the mutant displays 3-4fold increase in activity compared to the wild type enzyme
T296I
the mutant converts (2E,6E)-farnesyl diphosphate to 100% (E)-beta-farnesene
T296Y
the mutant loses its cyclization ability producing the acyclic beta-farnesene instead of amorpha-4,11-diene
T399A
the mutant exhibits an increase in the level of amorpha-4,7-diene
T399G
the mutant exhibits an increase in the level of amorpha-4,7-diene
T399I
the mutant exhibits an increase in the level of amorpha-4,7-diene
T399L/T447G
-
the mutant shows compromised activity in regioselective deprotonation to yield 34.7 and 37.7% normal and aberrant deprotonation products, respectively
T399N
the mutant exhibits an increase in the level of amorpha-4,7-diene
T399S
-
the mutant with increased catalytic efficiency produces 87.4% amorpha-4,11-diene compared to the wild type enzyme (90%)
T399S/H448A
the mutations improve the kcat value by 5times but at the expense of a raised Km making its catalytic efficiency about 3 times higher compared to the wild type enzyme
T399S/T447S
-
the mutant with reduced catalytic efficiency produces 72.1% amorpha-4,11-diene compared to the wild type enzyme (90%)
T399V
the mutant exhibits an increase in the level of amorpha-4,7-diene
T447S
-
the mutant with increased catalytic efficiency produces 76.9% amorpha-4,11-diene compared to the wild type enzyme (90%)
V396A
the mutant displays 3-4fold increase in activity compared to the wild type enzyme
V396I
the mutant displays 3-4fold increase in activity compared to the wild type enzyme
G439A
the mutant accumulates more alpha-bisabolol compared to the wild type enzyme
G439A
the mutant displays 3-4fold increase in activity compared to the wild type enzyme
T296A
the mutant predominantly retains amorphadiene synthase activity by converting (2E,6E)-farnesyl diphosphate to 78% amorpha-4,11-diene and 5% (E)-beta-farnesene
T296A
the mutant retains its cyclization ability producing amorpha-4,11-diene
T296L
the mutant converts (2E,6E)-farnesyl diphosphate to 35.24% amorpha-4,11-diene and 54.05% (E)-beta-farnesene
T296L
the mutant loses its cyclization ability producing the acyclic beta-farnesene instead of amorpha-4,11-diene
T296S
the mutant converts (2E,6E)-farnesyl diphosphate to 90.32% amorpha-4,11-diene and 1.57% (E)-beta-farnesene
T296S
the mutant retains its cyclization ability producing amorpha-4,11-diene
T296V
the mutant is defective in allylic diphosphate isomerization but retains the ability to cyclize the intermediate (3R,6E)-nerolidyl diphosphate to amorpha-4,11-diene. The mutant catalyzes the abortive conversion of (2E,6E)-farnesyl diphosphate mainly into the acyclic product (E)-beta-farnesene (88%)
T296V
the mutant loses its cyclization ability producing the acyclic beta-farnesene instead of amorpha-4,11-diene
T296V
-
the mutation impairs the ring closure activity almost completely. The mutant produces 93.7% linear (E)-beta-farnesene and 6.3% bicyclical amorpha-4,11-diene compared to the wild type enzyme (90% amorpha-4,11-diene)
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Mercke, P.; Bengtsson, M.; Bouwmeester, H.J.; Posthumus, M.A.; Brodelius, P.E.
Molecular cloning, expression, and characterization of amorpha-4,11-diene synthase, a key enzyme of artemisinin biosynthesis in Artemisia annua L.
Arch. Biochem. Biophys.
381
173-180
2000
Artemisia annua
brenda
Chang, Y.J.; Song, S.H.; Park, S.H.; Kim, S.U.
Amorpha-4,11-diene synthase of Artemisia annua: cDNA isolation and bacterial expression of a terpene synthase involved in artemisinin biosynthesis
Arch. Biochem. Biophys.
383
178-184
2000
Artemisia annua (Q9AR04), Artemisia annua
brenda
Picaud, S.; Olofsson, L.; Brodelius, M.; Brodelius, P.E.
Expression, purification, and characterization of recombinant amorpha-4,11-diene synthase from Artemisia annua L
Arch. Biochem. Biophys.
436
215-226
2005
Artemisia annua
brenda
Picaud, S.; Mercke, P.; He, X.; Sterner, O.; Brodelius, M.; Cane, D.E.; Brodelius, P.E.
Amorpha-4,11-diene synthase: mechanism and stereochemistry of the enzymatic cyclization of farnesyl diphosphate
Arch. Biochem. Biophys.
448
150-155
2006
Artemisia annua
brenda
Kim, S.H.; Heo, K.; Chang, Y.J.; Park, S.H.; Rhee, S.K.; Kim, S.U.
Cyclization mechanism of amorpha-4,11-diene synthase, a key enzyme in artemisinin biosynthesis
J. Nat. Prod.
69
758-762
2006
Artemisia annua
brenda
Martin, V.J.; Pitera, D.J.; Withers, S.T.; Newman, J.D.; Keasling, J.D.
Engineering a mevalonate pathway in Escherichia coli for production of terpenoids
Nat. Biotechnol.
21
796-802
2003
Artemisia annua
brenda
Bouwmeester, H.J.; Wallaart, T.E.; Janssen, M.H.A.; Van Loo, B.; Jansen, B.J.M.; Posthumus, M.A.; Schmidt, C.O.; De Kraker, J.W.; Konig, W.A.; Franssen, M.C.R.
Amorpha-4,11-diene synthase catalyzes the first probable step in artemisinin biosynthesis
Phytochemistry
52
843-854
1999
Artemisia annua
brenda
Wallaart, T.E.; Bouwmeester, H.J.; Hille, J.; Poppinga, L.; Maijers, N.C.A.
Amorpha-4,11-diene synthase: cloning and functional expression of a key enzyme in the biosynthetic pathway of the novel antimalarial drug artemisinin
Planta
212
460-465
2001
Artemisia annua (Q9AR04), Artemisia annua
brenda
Lindahl, A.L.; Olsson, M.E.; Mercke, P.; Tollbom, O.; Schelin, J.; Brodelius, M.; Brodelius, P.E.
Production of the artemisinin precursor amorpha-4,11-diene by engineered Saccharomyces cerevisiae
Biotechnol. Lett.
28
571-580
2006
Artemisia annua (Q9AR04), Artemisia annua
brenda
Li, Z.; Liu, Y.; Liu, B.; Wang, H.; Ye, H.; Li, G.
Cloning, E. coli expression and molecular analysis of amorpha-4,11-diene synthase from a high-yield strain of Artemisia annua L
J. Integr. Plant Biol.
48
1486-1492
2006
Artemisia annua
-
brenda
Kim, S.H.; Chang, Y.J.; Kim, S.U.
Tissue specificity and developmental pattern of amorpha-4,11-diene synthase (ADS) proved by ADS promoter-driven GUS expression in the heterologous plant, Arabidopsis thaliana
Planta Med.
74
188-193
2008
Artemisia annua
brenda
Picaud, S.; Olsson, M.E.; Brodelius, P.E.
Improved conditions for production of recombinant plant sesquiterpene synthases in Escherichia coli
Protein Expr. Purif.
51
71-79
2007
Artemisia annua (Q9AR04), Artemisia annua
brenda
Jiang-Qiang, K.; Wei, W.; Li-Na, W.; Xiao-Dong, Z.; Ke-Di, C.; Ping, Z.
The improvement of amorpha-4,11-diene production by a yeast-conform variant
J. Appl. Microbiol.
106
941-951
2009
Artemisia annua (Q9AR04), Artemisia annua
brenda
Lubertozzi, D.; Keasling, J.D.
Expression of a synthetic Artemesia annua amorphadiene synthase in Aspergillus nidulans yields altered product distribution
J. Ind. Microbiol. Biotechnol.
35
1191-1198
2008
Artemisia annua
brenda
Anthony, J.R.; Anthony, L.C.; Nowroozi, F.; Kwon, G.; Newman, J.D.; Keasling, J.D.
Optimization of the mevalonate-based isoprenoid biosynthetic pathway in Escherichia coli for production of the anti-malarial drug precursor amorpha-4,11-diene
Metab. Eng.
11
13-19
2008
Artemisia annua
brenda
Olsson, M.E.; Olofsson, L.M.; Lindahl, A.L.; Lundgren, A.; Brodelius, M.; Brodelius, P.E.
Localization of enzymes of artemisinin biosynthesis to the apical cells of glandular secretory trichomes of Artemisia annua L
Phytochemistry
70
1123-1128
2009
Artemisia annua
brenda
Ma, D.; Pu, G.; Lei, C.; Ma, L.; Wang, H.; Guo, Y.; Chen, J.; Du, Z.; Wang, H.; Li, G.; Ye, H.; Liu, B.
Isolation and characterization of AaWRKY1, an Artemisia annua transcription factor that regulates the amorpha-4,11-diene synthase gene, a key gene of artemisinin biosynthesis
Plant Cell Physiol.
50
2146-2161
2009
Artemisia annua
brenda
Pu, G.B.; Ma, D.M.; Chen, J.L.; Ma, L.Q.; Wang, H.; Li, G.F.; Ye, H.C.; Liu, B.Y.
Salicylic acid activates artemisinin biosynthesis in Artemisia annua L
Plant Cell Rep.
28
1127-1135
2009
Artemisia annua
brenda
Alam, P.; Kiran, U.; Ahmad, M.M.; Kamaluddin, M.M.; Khan, M.A.; Jhanwar, S.; Abdin, M.
Isolation, characterization and structural studies of amorpha - 4, 11-diene synthase (ADS(3963)) from Artemisia annua L
Bioinformation
4
421-429
2010
Artemisia annua (Q9AR04), Artemisia annua
brenda
Alam, P.; Abdin, M.Z.
Over-expression of HMG-CoA reductase and amorpha-4,11-diene synthase genes in Artemisia annua L. and its influence on artemisinin content
Plant Cell Rep.
30
1919-1928
2011
Artemisia annua (C5HG79), Artemisia annua, Artemisia annua L. (C5HG79)
brenda
Alejos-Gonzalez, F.; Qu, G.; Zhou, L.L.; Saravitz, C.H.; Shurtleff, J.L.; Xie, D.Y.
Characterization of development and artemisinin biosynthesis in self-pollinated Artemisia annua plants
Planta
234
685-697
2011
Artemisia annua
brenda
Pu, G.; Ma, D.; Wang, H.; Ye, H.; Liu, B.
Expression and localization of amorpha-4,11-diene synthase in Artemisia annua L.
Plant Mol. Biol. Rep.
31
32-37
2013
Artemisia annua
-
brenda
Muangphrom, P.; Seki, H.; Suzuki, M.; Komori, A.; Nishiwaki, M.; Mikawa, R.; Fukushima, E.O.; Muranaka, T.
Functional analysis of amorpha-4,11-diene synthase (ADS) homologs from non-artemisinin-producing artemisia species the discovery of novel koidzumiol and (+)-alpha-bisabolol synthases
Plant Cell Physiol.
57
1678-1688
2016
Artemisia annua (Q9AR04), Artemisia annua
brenda
Chen, X.; Zhang, C.; Zou, R.; Stephanopoulos, G.; Too, H.P.
In vitro metabolic engineering of amorpha-4,11-diene biosynthesis at enhanced rate and specific yield of production
ACS Synth. Biol.
6
1691-1700
2017
Artemisia annua
brenda
Fang, X.; Li, J.X.; Huang, J.Q.; Xiao, Y.L.; Zhang, P.; Chen, X.Y.
Systematic identification of functional residues of Artemisia annua amorpha-4,11-diene synthase
Biochem. J.
474
2191-2202
2017
Artemisia annua
brenda
Li, Z.; Gao, R.; Hao, Q.; Zhao, H.; Cheng, L.; He, F.; Liu, L.; Liu, X.; Chou, W.K.; Zhu, H.; Cane, D.E.
The T296V mutant of amorpha-4,11-diene synthase is defective in allylic diphosphate isomerization but retains the ability to cyclize the intermediate (3R)-nerolidyl diphosphate to amorpha-4,11-diene
Biochemistry
55
6599-6604
2016
Artemisia annua (Q9AR04)
brenda
Catania, T.M.; Branigan, C.A.; Stawniak, N.; Hodson, J.; Harvey, D.; Larson, T.R.; Czechowski, T.; Graham, I.A.
Silencing amorpha-4,11-diene synthase genes in Artemisia annua leads to FPP accumulation
Front. Plant Sci.
9
547
2018
Artemisia annua
brenda
Eslami, H.; Mohtashami, S.K.; Basmanj, M.T.; Rahati, M.; Rahimi, H.
An in-silico insight into the substrate binding characteristics of the active site of amorpha-4,11-diene synthase, a key enzyme in artemisinin biosynthesis
J. Mol. Model.
23
202
2017
Artemisia annua (A2TEY7), Artemisia annua
brenda
Abdallah, I.I.; Czepnik, M.; van Merkerk, R.; Quax, W.J.
Insights into the three-dimensional structure of amorpha-4,11-diene synthase and probing of plasticity residues
J. Nat. Prod.
79
2455-2463
2016
Artemisia annua
brenda
Abdallah, I.I.; van Merkerk, R.; Klumpenaar, E.; Quax, W.J.
Catalysis of amorpha-4,11-diene synthase unraveled and improved by mutability landscape guided engineering
Sci. Rep.
8
9961
2018
Artemisia annua (Q9AR04)
brenda