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Information on EC 1.14.20.13 - 6beta-hydroxyhyoscyamine epoxidase
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EC Tree
1.14.20.13 6beta-hydroxyhyoscyamine epoxidaseIUBMB Comments
Requires Fe2+ and ascorbate.
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Word Map
- 1.14.20.13
- scopolamine
- hyoscyamus
- atropa
-
tropane
- niger
-
hairy
- belladonna
- datura
- tanguticus
-
agrobacterium
-
2-oxoglutarate-dependent
- nicotiana
- baetica
- shoot
-
anisodus
- rhizogenes
-
1.14.11.11
- tabacum
-
anisodamine
- pharmacology
- muticus
-
solanaceous
-
anticholinergic
- putrescine
-
bioconversion
- n-methyltransferase
-
2.1.1.53
- synthesis
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
H&H, H6H, hydroxyhyoscyamine dioxygenase, hyoscyamine 6beta-hydroxylase, hyoscyamine-6beta-hydroxylase, hyosOH epoxidase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
H6H
hydroxyhyoscyamine dioxygenase
-
-
-
-
hyoscyamine 6beta-hydroxylase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(6S)-6beta-hydroxyhyoscyamine + 2-oxoglutarate + O2 = scopolamine + succinate + CO2 + H2O
-
-
-
-
(6S)-6beta-hydroxyhyoscyamine + 2-oxoglutarate + O2 = scopolamine + succinate + CO2 + H2O
proposed mechanism of epoxidation catalyzed by the enzyme, overview
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
(6S)-6beta-hydroxyhyoscyamine,2-oxoglutarate oxidoreductase (epoxide-forming)
Requires Fe2+ and ascorbate.
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CAS REGISTRY NUMBER
COMMENTARY
121479-53-6
-
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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
(6S)-hydroxyhyoscyamine + 2-oxoglutarate + O2
scopolamine + succinate + CO2
-
-
-
?
3-hydroxy-3-phenylpropionyltropine + 2-oxoglutarate + O2
3-hydroxy-3-phenylpropionyl-6-hydroxytropine + succinate + CO2 + H2O
-
-
-
?
6,7-dehydrohyoscyamine + 2-oxoglutarate + O2
scopolamine + succinate + CO2
-
-
-
?
8-methyl-8-azabicyclo[3.2.1]octan-3-yl 2-(4-(dimethylamino)phenyl)acetate + 2-oxoglutarate + O2
?
-
-
-
-
?
8-methyl-8-azabicyclo[3.2.1]octan-3-yl benzoate + 2-oxoglutarate + O2
?
-
-
-
-
?
apoatropine + 2-oxoglutarate + O2
6-hydroxyapoatropine + succinate + CO2 + H2O
-
-
-
?
l-homatropine + 2-oxoglutarate + O2
6-hydroxyhomatropine + succinate + CO2 + H2O
-
-
-
?
norhyoscyamine + 2-oxoglutarate + O2
6-hydroxynorhyoscyamine + succinate + CO2 + H2O
-
-
-
?
phenylacetyltropine + 2-oxoglutarate + O2
6-hydroxyphenylacetyltropine + succinate + CO2 + H2O
-
-
-
?
t-cinnamoyltropine + 2-oxoglutarate + O2
t-cinnamoyl-6-hydroxytropine + succinate + CO2 + H2O
-
-
-
?
(6S)-6-hydroxyhyoscyamine + 2-oxoglutarate + O2
scopolamine + succinate + CO2
-
-
-
?
(6S)-6-hydroxyhyoscyamine + 2-oxoglutarate + O2
scopolamine + succinate + CO2
-
alkaloid metabolism, scopolamine is formed by oxidative transformation of hyoscyamine in several solanaceous species
-
?
(6S)-6beta-hydroxyhyoscyamine + 2-oxoglutarate + O2
scopolamine + succinate + CO2
-
-
-
?
(6S)-6beta-hydroxyhyoscyamine + 2-oxoglutarate + O2
scopolamine + succinate + CO2
-
-
-
-
?
(6S)-6beta-hydroxyhyoscyamine + 2-oxoglutarate + O2
scopolamine + succinate + CO2
-
-
-
-
?
(6S)-6beta-hydroxyhyoscyamine + 2-oxoglutarate + O2
scopolamine + succinate + CO2
-
via 6,7-dehydrohyoscyamine or not, two possible pathways for the epoxidation in the biosynthesis of scopolamine, overview
-
-
?
(6S)-6beta-hydroxyhyoscyamine + 2-oxoglutarate + O2
scopolamine + succinate + CO2 + H2O
-
-
-
?
(6S)-6beta-hydroxyhyoscyamine + 2-oxoglutarate + O2
scopolamine + succinate + CO2 + H2O
-
-
-
-
?
(6S)-6beta-hydroxyhyoscyamine + 2-oxoglutarate + O2
scopolamine + succinate + CO2 + H2O
-
-
-
-
?
(6S)-6beta-hydroxyhyoscyamine + 2-oxoglutarate + O2
scopolamine + succinate + CO2 + H2O
-
-
-
?
additional information
?
-
enzyme catalyzes both the hydroxylation of hyoscyamine, reaction of EC 1.14.11.11, and the epoxidation of 6beta-hydroxyhyoscyamine to generate scopolamine
-
-
?
additional information
?
-
-
enzyme catalyzes both the hydroxylation of hyoscyamine, reaction of EC 1.14.11.11, and the epoxidation of 6beta-hydroxyhyoscyamine to generate scopolamine
-
-
?
additional information
?
-
-
hyoscyamine 6beta-hydroxylase, a 2-oxoglutarate-dependent dioxygenase, converts L-hyoscyamine to its 6,7-epoxy derivative, scopolamine, in two sequential steps, the enzyme also catalyzes the reaaction of EC 1.14.11.11. 6,7-Dehydrohyoscyamine, a potential precursor for the last step of epoxidation, is an obligatory intermediate in the biosynthesis of scopolamine
-
-
?
additional information
?
-
-
hyoscyamine 6beta-hydroxylase, a 2-oxoglutarate-dependent dioxygenase, converts L-hyoscyamine to its 6,7-epoxy derivative, scopolamine, in two sequential steps. The catalytic efficiency of AbH6H, especially for the second oxidation, is low. The epoxidation step is much slower than the hydroxylation step. Substrate analogues 1-methylpiperidin-4-yl 2-phenylacetate, 8-methyl-8-azabicyclo[3.2.1]octan-3-yl 3-phenylpropanoate, 8-oxabicyclo[3.2.1]octan-3-yl 2-phenylacetate, and 4 are no substrates for the enzyme
-
-
?
additional information
?
-
-
the enzyme also catalyzes the reaaction of EC 1.14.11.11
-
-
?
additional information
?
-
-
enzyme catalyzes both the hydroxylation of hyoscyamine, reaction of EC 1.14.11.11, and the epoxidation of 6beta-hydroxyhyoscyamine to generate scopolamine. Epoxidase activity is low compared to the hydroxylase activity. The binding of the substrates, hyoscyamine and 2-oxoglutarate, to the enzyme induces significant conformational changes
-
-
?
additional information
?
-
enzyme catalyzes both the hydroxylation of hyoscyamine, reaction of EC 1.14.11.11, and the epoxidation of 6beta-hydroxyhyoscyamine to generate scopolamine
-
-
?
additional information
?
-
-
enzyme is able to catalyze hydroxylation, dehydrogenation and in vitro epoxidation reactions all giving scopolamine. Hydroxyl rebound is unlikely to take place during the cyclization reaction and the hydroxylase versus oxidative cyclase activity is correlated with the presence of an exo-hydroxy group having syn-periplanar geometry with respect to the adjacent H atom to be abstracted
-
-
?
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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
(6S)-6-hydroxyhyoscyamine + 2-oxoglutarate + O2
scopolamine + succinate + CO2
-
alkaloid metabolism, scopolamine is formed by oxidative transformation of hyoscyamine in several solanaceous species
-
?
(6S)-hydroxyhyoscyamine + 2-oxoglutarate + O2
scopolamine + succinate + CO2
-
-
-
?
6,7-dehydrohyoscyamine + 2-oxoglutarate + O2
scopolamine + succinate + CO2
-
-
-
?
additional information
?
-
-
hyoscyamine 6beta-hydroxylase, a 2-oxoglutarate-dependent dioxygenase, converts L-hyoscyamine to its 6,7-epoxy derivative, scopolamine, in two sequential steps, the enzyme also catalyzes the reaaction of EC 1.14.11.11. 6,7-Dehydrohyoscyamine, a potential precursor for the last step of epoxidation, is an obligatory intermediate in the biosynthesis of scopolamine
-
-
?
(6S)-6beta-hydroxyhyoscyamine + 2-oxoglutarate + O2
scopolamine + succinate + CO2
-
-
-
?
(6S)-6beta-hydroxyhyoscyamine + 2-oxoglutarate + O2
scopolamine + succinate + CO2
-
-
-
-
?
(6S)-6beta-hydroxyhyoscyamine + 2-oxoglutarate + O2
scopolamine + succinate + CO2
-
-
-
-
?
(6S)-6beta-hydroxyhyoscyamine + 2-oxoglutarate + O2
scopolamine + succinate + CO2
-
via 6,7-dehydrohyoscyamine or not, two possible pathways for the epoxidation in the biosynthesis of scopolamine, overview
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(1R,2R,4S,5S,7s)-7-{[(2S)-3-hydroxy-2-phenylpropanoyl]oxy}-9,9-dimethyl-3-oxa-9-azoniatricyclo[3.3.1.02,4]nonane
-
slight inhibition by the substrate analogue
3,4-dihydroxybenzoate
competitive inhibitor with respect to 2-oxoglutarate
8-methyl-8-azabicyclo[3.2.1]octan-3-yl 2-(4-(dimethylamino)phenyl)acetate
-
-
Pyridine 2,4-dicarboxylate
competitive inhibitor with respect to 2-oxoglutarate
additional information
-
synthesis and inhibitory potencies of substrate analogues, overview. No inhibition by substrate analogues 1-methylpiperidin-4-yl 2-phenylacetate, 8-methyl-8-azabicyclo[3.2.1]octan-3-yl 3-phenylpropanoate, and 8-oxabicyclo[3.2.1]octan-3-yl 2-phenylacetate
-
additional information
-
no marked effect on enzyme activity by addition of NAD+, NADH, NADP+, NADPH, ATP + MgSO4, FAD, FMN, pyrroloquinoline quinone, acetyl-CoA, 6,7-dimethyl-5,6,7,8-tetrahydrofolate, phenazine methosulfate, 2,6-dichlorophenolindophenol, cytochrome c and H2O2
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ascorbate
in absence of ascorbate, 14% of the activity in presence of 4 mM
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Dehydration
Epoxidation in Vivo of Hyoscyamine to Scopolamine Does Not Involve a Dehydration Step.
Infections
Tailoring Tropane Alkaloid Accumulation in Transgenic Hairy Roots of Atropa baetica by Over-expressing the Gene Encoding Hyoscyamine 6beta-hydroxylase.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
collected from Sari-Garmestan of Mazandaran province in the North of Iran, gene h6h
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
expressed specifically in tapetum and pollen mother cells
brenda
additional information
additional information
no expression in stem, leaf, pistil, petal, and sepal tissues
brenda
additional information
-
no expression in stem, leaf, pistil, petal, and sepal tissues
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
-
the enzyme is a member of the 2-oxoglutarate-dependent dioxygenase family
metabolism
physiological function
additional information
metabolism
-
hyoscyamine 6beta-hydroxylase catalyzes two consecutive oxidation reactions. The first reaction is the hydroxylation of hyoscyamine to 6beta-hydroxyhyoscyamine, Ec 1.14.11.11, and the second is epoxidation of 6beta-hydroxyhyoscyamine yielding scopolamine, the final metabolite in the tropane alkaloid biosynthetic pathway
metabolism
-
hyoscyamine 6beta-hydroxylase converts hyoscyamine to scopolamine in the last step of scopolamine biosynthetic pathway
metabolism
the enzyme is involved in biosynthesis pathway of tropane alkaloids catalyzing two oxidation steps to form scopolamine from hyoscyamine, overview, cf. EC 1.14.11.11
physiological function
Agrobacterium-mediated expression in non-hyoscyamine-producing Nicotiana tabacum and hyoscyamine-producing Hyoscyamus muticus. Transgenic Nicotiana tabacum hairy roots show a more efficient uptake of hyoscyamine from the culture medium and a higher rate of bioconversion of hyoscyamine to scopolamine than those of Hyoscamus muticus. The secretion of scopolamine in Nicotiana tabacum hairy roots is up to 85% of the total scopolamine being released to the culture medium. Exogenous hyoscyamine also causes changes in nicotine alkaloid accumulation in Nicotiana tabacum hairy roots
physiological function
-
overexpression in hairy roots of Atropa baetica leeds to an altered alkaloid profile in which hyoscyamine is entirely converted into scopolamine. Scopolamine accumulation increases up to 9fold amounting to 5.6 mg per g dry weight
physiological function
root cultures overexpressing the enzyme show remarkably elevated levels of scopolamine and anisodamine. Hyoscyamine 6beta-hydroxylases from both Scopolia lurida and Hyoscyamus niger promote anisodamine production at similar levels in Scopolia lurida root cultures. Hyoscyamus niger hyoscyamine 6beta-hydroxylase overexpressing root cultures have more scopolamine in them than Scopolia lurida hyoscyamine 6beta-hydroxylase-overexpressing root cultures
physiological function
-
root cultures overexpressing the enzyme show remarkably elevated levels of scopolamine and anisodamine. Hyoscyamine 6beta-hydroxylases from both Scopolia lurida and Hyoscyamus niger promote anisodamine production at similar levels in Scopolia lurida root cultures. Hyoscyamus niger hyoscyamine 6beta-hydroxylase overexpressing root cultures have more scopolamine in them than Scopolia lurida hyoscyamine 6beta-hydroxylase-overexpressing root cultures
additional information
-
the nitrogen atom in the tropane ring of L-hyoscyamine plays an important role in substrate recognition. Proposed mechanism of epoxidation catalyzed by H6H, overview
additional information
-
the transcript level of H6H increased under chromium treatment. This treatment also increases hyoscyamine and scopolamine contents, phenotype with decreased the growth parameters (weights and lengths of the plantlets) and chlorophyll contents and increased proline contents, 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). A0A072TWE2_MEDTR
337
0
37620
TrEMBL
other Location (Reliability: 3)
A0A072VLQ3_MEDTR
342
0
39057
TrEMBL
other Location (Reliability: 4)
A0A072VL42_MEDTR
342
0
39302
TrEMBL
other Location (Reliability: 3)
A0A396GTP8_MEDTR
333
0
37473
TrEMBL
other Location (Reliability: 5)
A0A2P6PVB0_ROSCH
343
0
39038
TrEMBL
other Location (Reliability: 3)
A0A7C9AMP4_OPUST
341
0
38680
TrEMBL
other Location (Reliability: 3)
I3SNT9_MEDTR
344
0
39733
TrEMBL
other Location (Reliability: 2)
A0A072VKK8_MEDTR
342
0
38993
TrEMBL
other Location (Reliability: 4)
A0A396HAK2_MEDTR
Medicago tribuloides
339
0
38391
TrEMBL
Chloroplast (Reliability: 4)
A0A396HAK2_MEDTR
339
0
38391
TrEMBL
Chloroplast (Reliability: 4)
A2IBI0_9SOLA
344
0
38772
TrEMBL
other Location (Reliability: 2)
HY6H_HYONI
344
0
39001
Swiss-Prot
other Location (Reliability: 3)
Q9XJ43_ATRBE
343
0
38547
TrEMBL
other Location (Reliability: 3)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
39238
-
1 * 39238, recombinant enzyme, mass spectrometry, 1 * 39369, sequence calculation
39369
-
1 * 39238, recombinant enzyme, mass spectrometry, 1 * 39369, sequence calculation
43000
-
x * 64000, recombinant GST-tagged enzyme, SDS-PAGE, x * 43000, recombinant His-tagged enzyme, SDS-PAGE
64000
-
x * 64000, recombinant GST-tagged enzyme, SDS-PAGE, x * 43000, recombinant His-tagged enzyme, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
-
1 * 39238, recombinant enzyme, mass spectrometry, 1 * 39369, sequence calculation
?
-
x * 64000, recombinant GST-tagged enzyme, SDS-PAGE, x * 43000, recombinant His-tagged enzyme, SDS-PAGE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
S14P/K97A
mutant displays 2.3fold improved epoxidation activity compared with the wild-type enzyme
additional information
additional information
-
enhancied production of tropane alkaloids in transgenic Anisodus acutangulus hairy root cultures by overexpressing tropinone reductase I and hyoscyamine-6beta-hydroxylase Agrobacterium-mediated gene transfer technology, quantification of tropanalkaloid contents in transgenic lines, overview
additional information
enhancied production of tropane alkaloids in transgenic Anisodus acutangulus hairy root cultures by overexpressing tropinone reductase I and hyoscyamine-6beta-hydroxylase Agrobacterium-mediated gene transfer technology, quantification of tropanalkaloid contents in transgenic lines, overview
additional information
-
enhancied production of tropane alkaloids in transgenic Anisodus acutangulus hairy root cultures by overexpressing tropinone reductase I and hyoscyamine-6beta-hydroxylase, quantification of tropan alkaloid contents in transgenic lines, overview
additional information
enhancied production of tropane alkaloids in transgenic Anisodus acutangulus hairy root cultures by overexpressing tropinone reductase I and hyoscyamine-6beta-hydroxylase, quantification of tropan alkaloid contents in transgenic lines, overview
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, purified recombinant enzyme, 20 mM phosphate, 2 months, loss of approximately 20% of activity
-
4°C, purified recombinant enzyme, 20 mM phosphate, 4 days, loss of over 50% activity
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant N- or C-terminally His-tagged from Escherichia coli by nickel affinity chromatography
-
recombinant N-terminally His- or GST-tagged enzyme from Escherichia coli strain BL21 (DE3) by nickel or glutathione affinity chromatography, respectively
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, overexpression of N- or C-terminally His-tagged enzyme in Escherichia coli strain BL21 (DE3), AbH6H loses of the first amino acid methionine during transcription
-
DNA and amino acid sequence determination and analysis, overexpression of N-terminally His- or GST-tagged enzyme in Escherichia coli strain BL21 (DE3)
-
expression in Escherichia coli
overexpression of the enzyme in hairy roots of transgenic Anisodus acutangulus using Agrobacterium tumefaciens strain C58C1 transfection method, coexpression with tropinone reductase I
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pharmacology
tropane alkaloids including hyoscyamine, anisodamine, scopolamine and anisodine, are used medicinally as anticholinergic agents with increasing market demand, improvement of production by metabolic engineering introduction of genes encoding the branch-controlling enzyme tropinone reductase I and the downstream rate-limiting enzyme hyoscyamine-6beta-hydroxylase
synthesis
synthesis
Escherichia coli cells harboring mutant S14P/K97A in a 5-l-bioreactor produce scopolamine via a single enzyme-mediated two-step transformation from 500 mg/l hyoscyamine in 97% conversion
synthesis
-
overexpression in hairy roots of Atropa baetica leeds to an altered alkaloid profile in which hyoscyamine is entirely converted into scopolamine. Scopolamine accumulation increases up to 9fold amounting to 5.6 mg per g dry weight
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hashimoto, T.; Kohno, J.; Yamada, Y.
6beta-hydroxyhyoscyamine epoxidase from cultured roots of Hyoscyamus niger
Phytochemistry
28
1077-1082
1989
Hyoscyamus niger
-
brenda
Li, J.; van Belkum, M.J.; Vederas, J.C.
Functional characterization of recombinant hyoscyamine 6beta-hydroxylase from Atropa belladonna
Bioorg. Med. Chem.
20
4356-4363
2012
Atropa belladonna
brenda
Kai, G.; Liu, Y.; Wang, X.; Yang, S.; Fu, X.; Luo, X.; Liao, P.
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Anisodus acutangulus, Anisodus acutangulus (A2IBI0)
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Vakili, B.; Karimi, F.; Sharifi, M.; Behmanesh, M.
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Atropa belladonna
brenda
Cao, Y.D.; He, Y.C.; Li, H.; Kai, G.Y.; Xu, J.H.; Yu, H.L.
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Anisodus acutangulus (A2IBI0)
brenda
Lan, X.; Zeng, J.; Liu, K.; Zhang, F.; Bai, G.; Chen, M.; Liao, Z.; Huang, L.
Comparison of two hyoscyamine 6beta-hydroxylases in engineering scopolamine biosynthesis in root cultures of Scopolia lurida
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Anisodus luridus, Hyoscyamus niger (P24397)
brenda
Zarate, R.; el Jaber-Vazdekis, N.; Medina, B.; Ravelo, A.G.
Tailoring tropane alkaloid accumulation in transgenic hairy roots of Atropa baetica by over-expressing the gene encoding hyoscyamine 6beta-hydroxylase
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Hyoscyamus niger
brenda
Hashimoto, T.; Yamada, Y.
Purification and characterization of hyoscyamine 6 beta-hydroxylase from root cultures of Hyoscyamus niger L. hydroxylase and epoxidase activities in the enzyme preparation
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Hyoscyamus niger (P24397)
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Ushimaru, R.; Ruszczycky, M.W.; Chang, W.C.; Yan, F.; Liu, Y.N.; Liu, H.W.
Substrate conformation correlates with the outcome of hyoscyamine 6beta-hydroxylase catalyzed oxidation reactions
J. Am. Chem. Soc.
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Hyoscyamus niger
brenda
Kai, G.; Chen, J.; Li, L.; Zhou, G.; Zhou, L.; Zhang, L.; Chen, Y.; Zhao, L.
Molecular cloning and characterization of a new cDNA encoding hyoscyamine 6beta-hydroxylase from roots of Anisodus acutangulus
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Anisodus acutangulus (A2IBI0), Anisodus acutangulus
brenda
Haekkinen, S.T.; Moyano, E.; Cusido, R.M.; Palazon, J.; Pinol, M.T.; Oksman-Caldentey, K.M.
Enhanced secretion of tropane alkaloids in Nicotiana tabacum hairy roots expressing heterologous hyoscyamine-6beta-hydroxylase
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Hyoscyamus niger (P24397), Hyoscyamus niger
brenda
Suzuki, K.; Yun, D.J.; Chen, X.Y.; Yamada, Y.; Hashimoto, T.
An Atropa belladonna hyoscyamine 6beta-hydroxylase gene is differentially expressed in the root pericycle and anthers
Plant Mol. Biol.
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1999
Atropa belladonna (Q9XJ43), Atropa belladonna
brenda
Pramod, K.K.; Singh, S.; Jayabaskaran, C.
Biochemical and structural characterization of recombinant hyoscyamine 6beta-hydroxylase from Datura metel L
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Datura metel
brenda
Liu, T.; Zhu, P.; Cheng, K.D.; Meng, C.; He, H.X.
Molecular cloning, expression and characterization of hyoscyamine 6beta-hydroxylase from hairy roots of Anisodus tanguticus
Planta Med.
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Anisodus tanguticus (Q6V0J1), Anisodus tanguticus
brenda
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