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Information on EC 1.14.14.114 - amorpha-4,11-diene 12-monooxygenase
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EC Tree
1.14.14.114 amorpha-4,11-diene 12-monooxygenaseIUBMB Comments
A cytochrome P-450 (heme-thiolate) protein. Cloned from the plant Artemisia annua (sweet wormwood). Part of the biosynthetic pathway of artemisinin.
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Word Map
- 1.14.14.114
- annua
- artemisia
-
malaria
-
artemisinic
- trichomes
-
sesquiterpene
-
dihydroartemisinic
- lactone
-
glandular
-
anti-malarial
-
trichome-specific
-
farnesyl
-
endoperoxide
- sesquiterpenoids
-
artemisinin-based
-
one-hybrid
-
arteannuin
-
amorphadiene
- asteraceae
- synthesis
-
t-shaped
-
jasmonate-responsive
-
12-hydroxylase
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
cyp71av1, amorpha-4,11-diene c-12 oxidase, amorpha-4,11-diene 12-monooxygenase, amorpha-4,11-diene monooxygenase, cytochrome p450 monooxygenase 71 av1, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CYP71AV1
EC 1.14.13.158
-
-
formerly
-
CYP71AV1
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
amorpha-4,11-diene + 3 O2 + 3 [reduced NADPH-hemoprotein reductase] = artemisinate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O
overall reaction
-
-
-
amorpha-4,11-diene + O2 + [reduced NADPH-hemoprotein reductase] = artemisinic alcohol + [oxidized NADPH-hemoprotein reductase] + H2O
(1a)
-
-
-
artemisinic alcohol + O2 + [reduced NADPH-hemoprotein reductase] = artemisinic aldehyde + [oxidized NADPH-hemoprotein reductase] + 2 H2O
(1b)
-
-
-
artemisinic aldehyde + O2 + [reduced NADPH-hemoprotein reductase] = artemisinate + [oxidized NADPH-hemoprotein reductase] + H2O
(1c)
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
amorpha-4,11-diene,[reduced NADPH-hemoprotein reductase]:oxygen oxidoreductase (12-hydroxylating)
A cytochrome P-450 (heme-thiolate) protein. Cloned from the plant Artemisia annua (sweet wormwood). Part of the biosynthetic pathway of artemisinin.
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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
2-nonenal + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
amorpha-4,11-diene + 3 O2 + [reduced NADPH-hemoprotein reductase]
artemisinate + [oxidized NADPH-hemoprotein reductase] + 4 H2O
amorpha-4,11-diene + O2 + [reduced NADPH-hemoprotein reductase]
artemisinic alcohol + [oxidized NADPH-hemoprotein reductase] + H2O
amorpha-4,11-diene + [reduced NADPH-hemoprotein reductase] + O2
artemisinic alcohol + [oxidized NADPH-hemoprotein reductase] + H2O
artemisinic alcohol + O2 + [reduced NADPH-hemoprotein reductase]
artemisinic aldehyde + [oxidized NADPH-hemoprotein reductase] + 2 H2O
artemisinic alcohol + [reduced NADPH-hemoprotein reductase] + O2
artemisinic aldehyde + [oxidized NADPH-hemoprotein reductase] + H2O
artemisinic aldehyde + O2 + [reduced NADPH-hemoprotein reductase]
artemisinate + [oxidized NADPH-hemoprotein reductase] + H2O
artemisinic aldehyde + [reduced NADPH-hemoprotein reductase] + O2
artemisinate + [oxidized NADPH-hemoprotein reductase] + H2O
dihydroartemisinic alcohol + [reduced NADPH-hemoprotein reductase] + O2
dihydroartemisinic aldehyde + [oxidized NADPH-hemoprotein reductase] + H2O
dihydroartemisinic aldehyde + [reduced NADPH-hemoprotein reductase] + O2
dihydroartemisinate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
octanal + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
amorpha-4,11-diene + 3 O2 + [reduced NADPH-hemoprotein reductase]
artemisinate + [oxidized NADPH-hemoprotein reductase] + 4 H2O
-
-
-
?
amorpha-4,11-diene + 3 O2 + [reduced NADPH-hemoprotein reductase]
artemisinate + [oxidized NADPH-hemoprotein reductase] + 4 H2O
-
-
-
?
amorpha-4,11-diene + 3 O2 + [reduced NADPH-hemoprotein reductase]
artemisinate + [oxidized NADPH-hemoprotein reductase] + 4 H2O
-
-
-
?
amorpha-4,11-diene + 3 O2 + [reduced NADPH-hemoprotein reductase]
artemisinate + [oxidized NADPH-hemoprotein reductase] + 4 H2O
overall reaction via artemsinic alcohol and artemsinic aldehyde, multistep process
-
-
?
amorpha-4,11-diene + 3 O2 + [reduced NADPH-hemoprotein reductase]
artemisinate + [oxidized NADPH-hemoprotein reductase] + 4 H2O
-
overall reaction via artemsinic alcohol and artemsinic aldehyde, multistep process
-
-
?
amorpha-4,11-diene + 3 O2 + [reduced NADPH-hemoprotein reductase]
artemisinate + [oxidized NADPH-hemoprotein reductase] + 4 H2O
overall reaction via artemsinic alcohol and artemsinic aldehyde, multistep process
-
-
?
amorpha-4,11-diene + 3 O2 + [reduced NADPH-hemoprotein reductase]
artemisinate + [oxidized NADPH-hemoprotein reductase] + 4 H2O
overall reaction, multistep process
-
-
?
amorpha-4,11-diene + 3 O2 + [reduced NADPH-hemoprotein reductase]
artemisinate + [oxidized NADPH-hemoprotein reductase] + 4 H2O
overall reactionvia artemsinic alcohol and artemsinic aldehyde, multistep process
-
-
?
amorpha-4,11-diene + 3 O2 + [reduced NADPH-hemoprotein reductase]
artemisinate + [oxidized NADPH-hemoprotein reductase] + 4 H2O
-
-
-
-
?
amorpha-4,11-diene + O2 + [reduced NADPH-hemoprotein reductase]
artemisinic alcohol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
amorpha-4,11-diene + O2 + [reduced NADPH-hemoprotein reductase]
artemisinic alcohol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
amorpha-4,11-diene + O2 + [reduced NADPH-hemoprotein reductase]
artemisinic alcohol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
amorpha-4,11-diene + O2 + [reduced NADPH-hemoprotein reductase]
artemisinic alcohol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
amorpha-4,11-diene + [reduced NADPH-hemoprotein reductase] + O2
artemisinic alcohol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
amorpha-4,11-diene + [reduced NADPH-hemoprotein reductase] + O2
artemisinic alcohol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
artemisinic alcohol + O2 + [reduced NADPH-hemoprotein reductase]
artemisinic aldehyde + [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
artemisinic alcohol + O2 + [reduced NADPH-hemoprotein reductase]
artemisinic aldehyde + [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
-
?
artemisinic alcohol + O2 + [reduced NADPH-hemoprotein reductase]
artemisinic aldehyde + [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
artemisinic alcohol + O2 + [reduced NADPH-hemoprotein reductase]
artemisinic aldehyde + [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
-
?
artemisinic alcohol + [reduced NADPH-hemoprotein reductase] + O2
artemisinic aldehyde + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
artemisinic alcohol + [reduced NADPH-hemoprotein reductase] + O2
artemisinic aldehyde + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
artemisinic aldehyde + O2 + [reduced NADPH-hemoprotein reductase]
artemisinate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
artemisinic aldehyde + O2 + [reduced NADPH-hemoprotein reductase]
artemisinate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
artemisinic aldehyde + O2 + [reduced NADPH-hemoprotein reductase]
artemisinate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
artemisinic aldehyde + O2 + [reduced NADPH-hemoprotein reductase]
artemisinate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
artemisinic aldehyde + [reduced NADPH-hemoprotein reductase] + O2
artemisinate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
artemisinic aldehyde + [reduced NADPH-hemoprotein reductase] + O2
artemisinate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
dihydroartemisinic alcohol + [reduced NADPH-hemoprotein reductase] + O2
dihydroartemisinic aldehyde + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
dihydroartemisinic alcohol + [reduced NADPH-hemoprotein reductase] + O2
dihydroartemisinic aldehyde + [oxidized NADPH-hemoprotein reductase] + H2O
about 50% of the rate with artemisinic alcohol
-
-
?
additional information
?
-
no substrate: dihydroartemisinic aldehyde
-
-
?
additional information
?
-
no substrates: limonene, alpha-pinene, beta-pinene and pinocarveol, and the sesquiterpenes ()-alloisolongifolene, caryophyllene, ()-alpha-gurjunene, (+)-gamma-gurjunene, (+)-ledene,(+)-beta-selinene and (+)-valencene
-
-
?
additional information
?
-
-
no substrates: limonene, alpha-pinene, beta-pinene and pinocarveol, and the sesquiterpenes ()-alloisolongifolene, caryophyllene, ()-alpha-gurjunene, (+)-gamma-gurjunene, (+)-ledene,(+)-beta-selinene and (+)-valencene
-
-
?
additional information
?
-
-
no substrates: Sinapaldehyde, 2-phenylpropanal
-
-
?
additional information
?
-
no substrates: Sinapaldehyde, 2-phenylpropanal
-
-
?
additional information
?
-
conversion of dihydroartemsinic aldehyde to artemisinate is nonenzymatic in trichomes by nonenzymatic autoxidation of dihydroartemsinic aldehyde to dihydroartemsinic acid tertiary hydroperoxide and subsequent nonenzymatic rearrangement to artemisinin
-
-
?
additional information
?
-
-
conversion of dihydroartemsinic aldehyde to artemisinate is nonenzymatic in trichomes by nonenzymatic autoxidation of dihydroartemsinic aldehyde to dihydroartemsinic acid tertiary hydroperoxide and subsequent nonenzymatic rearrangement to artemisinin
-
-
?
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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
amorpha-4,11-diene + 3 O2 + [reduced NADPH-hemoprotein reductase]
artemisinate + [oxidized NADPH-hemoprotein reductase] + 4 H2O
amorpha-4,11-diene + O2 + [reduced NADPH-hemoprotein reductase]
artemisinic alcohol + [oxidized NADPH-hemoprotein reductase] + H2O
artemisinic alcohol + O2 + [reduced NADPH-hemoprotein reductase]
artemisinic aldehyde + [oxidized NADPH-hemoprotein reductase] + 2 H2O
artemisinic aldehyde + O2 + [reduced NADPH-hemoprotein reductase]
artemisinate + [oxidized NADPH-hemoprotein reductase] + H2O
amorpha-4,11-diene + 3 O2 + [reduced NADPH-hemoprotein reductase]
artemisinate + [oxidized NADPH-hemoprotein reductase] + 4 H2O
-
-
-
?
amorpha-4,11-diene + 3 O2 + [reduced NADPH-hemoprotein reductase]
artemisinate + [oxidized NADPH-hemoprotein reductase] + 4 H2O
-
-
-
?
amorpha-4,11-diene + 3 O2 + [reduced NADPH-hemoprotein reductase]
artemisinate + [oxidized NADPH-hemoprotein reductase] + 4 H2O
-
-
-
?
amorpha-4,11-diene + 3 O2 + [reduced NADPH-hemoprotein reductase]
artemisinate + [oxidized NADPH-hemoprotein reductase] + 4 H2O
overall reaction via artemsinic alcohol and artemsinic aldehyde, multistep process
-
-
?
amorpha-4,11-diene + 3 O2 + [reduced NADPH-hemoprotein reductase]
artemisinate + [oxidized NADPH-hemoprotein reductase] + 4 H2O
-
overall reaction via artemsinic alcohol and artemsinic aldehyde, multistep process
-
-
?
amorpha-4,11-diene + 3 O2 + [reduced NADPH-hemoprotein reductase]
artemisinate + [oxidized NADPH-hemoprotein reductase] + 4 H2O
overall reaction via artemsinic alcohol and artemsinic aldehyde, multistep process
-
-
?
amorpha-4,11-diene + 3 O2 + [reduced NADPH-hemoprotein reductase]
artemisinate + [oxidized NADPH-hemoprotein reductase] + 4 H2O
overall reaction, multistep process
-
-
?
amorpha-4,11-diene + 3 O2 + [reduced NADPH-hemoprotein reductase]
artemisinate + [oxidized NADPH-hemoprotein reductase] + 4 H2O
overall reactionvia artemsinic alcohol and artemsinic aldehyde, multistep process
-
-
?
amorpha-4,11-diene + 3 O2 + [reduced NADPH-hemoprotein reductase]
artemisinate + [oxidized NADPH-hemoprotein reductase] + 4 H2O
-
-
-
-
?
amorpha-4,11-diene + O2 + [reduced NADPH-hemoprotein reductase]
artemisinic alcohol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
amorpha-4,11-diene + O2 + [reduced NADPH-hemoprotein reductase]
artemisinic alcohol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
amorpha-4,11-diene + O2 + [reduced NADPH-hemoprotein reductase]
artemisinic alcohol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
amorpha-4,11-diene + O2 + [reduced NADPH-hemoprotein reductase]
artemisinic alcohol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
artemisinic alcohol + O2 + [reduced NADPH-hemoprotein reductase]
artemisinic aldehyde + [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
artemisinic alcohol + O2 + [reduced NADPH-hemoprotein reductase]
artemisinic aldehyde + [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
-
?
artemisinic alcohol + O2 + [reduced NADPH-hemoprotein reductase]
artemisinic aldehyde + [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
artemisinic alcohol + O2 + [reduced NADPH-hemoprotein reductase]
artemisinic aldehyde + [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
-
?
artemisinic aldehyde + O2 + [reduced NADPH-hemoprotein reductase]
artemisinate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
artemisinic aldehyde + O2 + [reduced NADPH-hemoprotein reductase]
artemisinate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
artemisinic aldehyde + O2 + [reduced NADPH-hemoprotein reductase]
artemisinate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
artemisinic aldehyde + O2 + [reduced NADPH-hemoprotein reductase]
artemisinate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADPH-hemoprotein reductase
A flavoprotein containing both FMN and FAD. This enzyme catalyses the transfer of electrons from NADPH, an obligatory two-electron donor, to microsomal P-450 monooxygenases, EC 1.14.14._
-
NADPH-hemoprotein reductase
-
A flavoprotein containing both FMN and FAD. This enzyme catalyses the transfer of electrons from NADPH, an obligatory two-electron donor, to microsomal P-450 monooxygenases, EC 1.14.14._
-
NADPH-hemoprotein reductase
A flavoprotein containing both FMN and FAD. This enzyme catalyses the transfer of electrons from NADPH, an obligatory two-electron donor, to microsomal P-450 monooxygenases, EC 1.14.14._
-
NADPH-hemoprotein reductase
-
A flavoprotein containing both FMN and FAD. This enzyme catalyses the transfer of electrons from NADPH, an obligatory two-electron donor, to microsomal P-450 monooxygenases, EC 1.14.14._
-
NADPH-hemoprotein reductase
A flavoprotein containing both FMN and FAD. This enzyme catalyses the transfer of electrons from NADPH, an obligatory two-electron donor, to microsomal P-450 monooxygenases, EC 1.14.14._
-
NADPH-hemoprotein reductase
-
A flavoprotein containing both FMN and FAD. This enzyme catalyses the transfer of electrons from NADPH, an obligatory two-electron donor, to microsomal P-450 monooxygenases, EC 1.14.14._
-
NADPH-hemoprotein reductase
A flavoprotein containing both FMN and FAD. This enzyme catalyses the transfer of electrons from NADPH, an obligatory two-electron donor, to microsomal P-450 monooxygenases, EC 1.14.14._
-
NADPH-hemoprotein reductase
A flavoprotein containing both FMN and FAD. This enzyme catalyses the transfer of electrons from NADPH, an obligatory two-electron donor, to microsomal P-450 monooxygenases, EC 1.14.14._
-
NADPH-hemoprotein reductase
-
A flavoprotein containing both FMN and FAD. This enzyme catalyses the transfer of electrons from NADPH, an obligatory two-electron donor, to microsomal P-450 monooxygenases, EC 1.14.14._
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
expression of farnesyl diphosphate synthase takes place in apical and sub-apical cells as well as in mesophyl cells while the three enzymes involved in artemisinin biosynthesis, i.e. amorpha-4,11-diene synthase, amorpha-4,11-diene hydroxylase, a cytochrome P450 monooxygenase, and artemisinic aldehyde DELTA11(13) reductase are expressed only in the apical cells
brenda
the production of artemisinin occurs in specialized 10-cell biseriate glandular trichomes present on the leaves, stems, and inflorescences of Artemisia annua
brenda
artemisinin production in Artemisia annua is localized in glandular trichomes on the surface of leaves, shoots and flowers
brenda
of stems, old and young leaves, and flower buds gathered 5-20 d after budding
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
abolished activation of AabHLH1 by mutated E-boxes of the CYP71AV1 promoter
malfunction
the enzyme knockout mutant cyp71av1-1 reveals that the consequence of blocking the artemisinin biosynthetic pathway is the redirection of sesquiterpene metabolism to a sesquiterpene epoxide, termed arteannuin X. Disruption of CYP71AV1 results in the accumulation of a sesquiterpene epoxide at the expense of artemisinin
metabolism
amorpha-4,11-diene synthase (ADS) and Cyt P450 monooxygenase CYP71AV1 in Artemisia annua are two key enzymes involved in the biosynthesis of artemisinin. The promoters of ADS and CYP71AV1 contain E-box elements, which are putative binding sites for basic helix-loop-helix (bHLH) transcription factors. The E-box is important for the CYP71AV1 promoter activity. AabHLH1 can positively regulate the biosynthesis of artemisinin. AabHLH1 protein is capable of binding to the E-box cis-elements, present in both ADS and CYP71AV1 promoters, and possesses transactivation activity in yeast
metabolism
the amorpha-4,11-diene C-12 oxidase (CYP71AV1) enzyme, responsible for a series of oxidation reactions in the artemisinin biosynthetic pathway, overview
metabolism
the enzyme is involved in the artemisinin biosynthesis
metabolism
the first oxidation step by cytochrome P450 (CYP71AV1) is the main rate-limiting step in the dihydroartemisinic acid (DHAA) pathway
physiological function
-
the first committed steps in the conversion of farnesyl diphosphate to artemisinin are conducted by amorpha-4,11-diene synthase, amorpha-4,11-diene hydroxylase, a cytochrome P450 monooxygenase, ie. CYP71AV1, and artemisinic aldehyde DELTA11(13) reductase
physiological function
amorpha-4,11-diene 12-monooxygenase (CYP71AV1) catalyzes the multistep oxidation of amorpha-4,11-diene to artemisinic alcohol and artemisinic aldehyde
physiological function
amorpha-4,11-diene 12-monooxygenase (CYP71AV1) catalyzes the multistep oxidation of amorpha-4,11-diene to artemisinic alcohol and artemisinic aldehyde
physiological function
amorpha-4,11-diene 12-monooxygenase (CYP71AV1) catalyzes the multistep oxidation of amorpha-4,11-diene to artemisinic alcohol and artemisinic aldehyde
physiological function
-
amorpha-4,11-diene 12-monooxygenase (CYP71AV1) catalyzes the multistep oxidation of amorpha-4,11-diene to artemisinic alcohol and artemisinic aldehyde
physiological function
enzyme CYP71AV1 is the critical enzyme that is capable of catalyzing three consecutive oxidation reactions at C-12 position of amorpha-4,11-diene to artemisinate. The heme catalytic site is situated at the C-terminal domain
physiological function
the antimalarial artemisinin is a sesquiterpene lactone produced by glandular secretory trichomes on the leaves, stems, and inflorescences of Artemisia annua. Glandular secretory trichomes are able to redirect flux into a sesquiterpene epoxide. The amorpha-4,11-diene C-12 oxidase (CYP71AV1) enzyme, responsible for a series of oxidation reactions in the artemisinin biosynthetic pathway
physiological function
the positive regulator and transcription factor, glandular trichome-specific WRKY 1, is involved in the regulatory network of the artemisinin biosynthetic pathway, overview. Both AaMYC2 and AabZIP1 form a feed-forward loop with AaGSW1 to regulate CYP71AV1
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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). AMO_ARTAN
495
1
55711
Swiss-Prot
Secretory Pathway (Reliability: 3)
AMO_ARTAN
495
1
55711
Swiss-Prot
Secretory Pathway (Reliability: 3)
A0A2P6S6H4_ROSCH
309
1
34943
TrEMBL
Secretory Pathway (Reliability: 2)
K7ZR99_9ASTR
495
0
55786
TrEMBL
other Location (Reliability: 2)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
construction of enzyme knockout mutant cyp71av1-1, phenotype, overview
additional information
-
construction of enzyme knockout mutant cyp71av1-1, phenotype, overview
additional information
Saccharomyces cerevisiae expressing the native Artemisia annua cytochrome P450 monooxygenase (CYP71AV1) and artemisinic aldehyde D11(13) reductase (DBR2) is used as a whole-cell biocatalyst to produce the immediate artemisinin precursor, dihydroartemisinic acid (DHAA). Introducing artemisinic aldehyde dehydrogenase (ALDH1) from Artemisia annua, which recycles NADPH, results in a significant enhancement in artemisinate titer. Method optimization and evaluation, host screening and cofactor engineering, overview. The co-expression of DBR2 and modulation of abiotic conditions result in a higher yield. Optimal condition are 80 OD yeast cells in 0.05 ml reaction at pH 8.0. Growing the yeast cells at 20°C in galactose medium increases the dihydroartemisinate titer by 50%
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis
gene cyp71av1, recombinant expression of cytochrome P450 CYP71AV1 in Saccharomyces cerevisiae, coexpression with artemisinic aldehyde D11(13) reductase (DBR2), and artemisinic aldehyde dehydrogenase (ALDH1), which recycles NADPH
gene CYP71AV1, semi-quantitative RT-PCR enzyme expression analysis, the expression level of CYP71AV1 significantly increases with the overexpression of AabHLH1
DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis
DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis
DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
endophyte Penicillium oxalicum strain B4 induces the enzyme and leads to enhanced growth and artemisinin content of host plant in an in vitro dual culture of endophyte with regenerated plantlets via generation of reactive oxygen species (ROS) including superoxide ions and H2O2
the expression level of CYP71AV1 significantly increases with the overexpression of transcription factor AabHLH1. The promoters of ADS and CYP71AV1 contain E-box elements, which are putative binding sites for basic helix-loop-helix (bHLH) transcription factors. The E-box is important for the CYP71AV1 promoter activity. AabHLH1 can positively regulate the biosynthesis of artemisinin. AabHLH1 protein is capable of binding to the E-box cis-elements, present in both ADS and CYP71AV1 promoters, and possesses transactivation activity in yeast. Transient expression of AabHLH1 in Artemisia annua leaves increases transcript levels of the genes involved in artemisinin biosynthesis, such as ADS, CYP71AV1 and HMGR
transcription factor protein glandular trichome-specific WRKY 1, i.e. AaGSW1, promotes artemisinin biosynthesis in Artemisia annua by inducing CYP71AV1 expression. AaGSW1 positively regulates CYP71AV1 and AaORA expression by directly binding to the W-box motifs in their promoters. Overexpression of AaGSW1 in Artemisia annua (via Agrobacterium tumefaciens transformation method) significantly improves artemisinin and dihydroartemisinic acid contents. AaGSW1 can be directly regulated by AaMYC2 and AabZIP1, which are positive regulators of jasmonate- and abscisic acid-mediated artemisinin biosynthetic pathways, respectively. AaGSW1 binds to the W-box in the CYP71AV1 promoter in vitro and activates the transcription of CYP71AV1 in vivo. Global expression profile and phylogenetic analysis of WRKY transcription factors in Artemisia annua, overview
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
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heterologous expression of Artemisia annua amorphadiene synthase and CYP71AV1 in tobacco lead to the accumulation of amorphadiene and artemisinic alcohol, but not artemisinic acid. Additional expression of artemisinic aldehyde DELTA11(13) double-bond reductase DBR2 with or without aldehyde dehydrogenase 1 leads to the additional accumulation dihydroartemisinic alcohol. Results and suggest that amorphane sesquiterpenoid aldehydes are formed, but conditions in the transgenic tobacco cells favour reduction to alcohols rather than oxidation to acids
synthesis
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selection of self-pollinated plants for artemisin biosynthesis. Selfpollinated F2 plants selected are grown under optimized growth conditions. 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 increases from the bottom to the top leaves. Leaves, flowers, and young seedlings of F2 plants produce artemisinin. In leaves, the levels of artemisinin increase from the bottom to the top of the plants, showing a positive correlation to the density increase of glandular trichomes. Progeny of selfpollinated plants expresses the amorpha-4, 11-diene synthase and cytochrome P450 monooxygenase 71 AV1genes, which are involved in artemisinin biosynthesis in leaves and flowers
synthesis
Saccharomyces cerevisiae expressing the native Artemisia annua cytochrome P450 monooxygenase (CYP71AV1) and artemisinic aldehyde D11(13) reductase (DBR2) is used as a whole-cell biocatalyst to produce the immediate artemisinin precursor, dihydroartemisinic acid (DHAA)
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Olsson, M.E.; Olofsson, L.M.; Lindahl, A.L.; Lundgren, A.; Brodelius, M.; Brodelius, P.E.
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Artemisia annua
brenda
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Artemisia annua
brenda
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Botany
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Artemisia annua, Artemisia annua (C5I9X1)
-
brenda
Teoh, K.H.; Polichuk, D.R.; Reed, D.W.; Nowak, G.; Covello, P.S.
Artemisia annua L. (Asteraceae) trichome-specific cDNAs reveal CYP71AV1, a cytochrome P450 with a key role in the biosynthesis of the antimalarial sesquiterpene lactone artemisinin
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Artemisia annua (Q1PS23), Artemisia annua
brenda
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Artemisia annua
brenda
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Artemisia annua (Q1PS23)
brenda
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Artemisia annua (Q1PS23), Artemisia annua
brenda
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55
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Artemisia annua (Q1PS23), Artemisia annua
brenda
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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 kurramensis, Artemisia absinthium (K7ZPJ9), Artemisia absinthium, Artemisia afra (K7ZR99), Artemisia annua (Q1PS23), Artemisia annua
brenda
Zheng, L.; Tian, H.; Yuan, Y.; Wang, J.
The influence of endophytic Penicillium oxalicum B4 on growth and artemisinin biosynthesis of in vitro propagated plantlets of Artemisia annua L.
Plant Growth Regul.
80
93-102
2016
Artemisia annua (Q1PS23)
-
brenda
Czechowski, T.; Larson, T.R.; Catania, T.M.; Harvey, D.; Brown, G.D.; Graham, I.A.
Artemisia annua mutant impaired in artemisinin synthesis demonstrates importance of nonenzymatic conversion in terpenoid metabolism
Proc. Natl. Acad. Sci. USA
113
15150-15155
2016
Artemisia annua (Q1PS23), Artemisia annua
brenda
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