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Enzyme Nomenclature
Information on EC 1.14.11.11 - hyoscyamine (6S)-dioxygenase
for references in articles please use BRENDA:EC1.14.11.11
Word Map on EC 1.14.11.11
- 1.14.11.11
- scopolamine
-
alkaloid
- hyoscyamus
-
tropane
- niger
-
atropa
- belladonna
-
anisodus
- acutangulus
-
hairy
-
aerial
-
anticholinergic
-
6beta-hydroxylase
-
epoxidation
-
2-oxoglutarate-dependent
- metel
-
solanaceous
-
his-tagged
- datura
- n-methyltransferase
-
agrobacterium-mediated
- putrescine
-
gst-tag
- tabacum
-
underground
-
biofunctional
- roseus
- vindoline
- pericycle
-
2.1.1.53
-
genetically-engineered
-
bolt
-
catharanthus
- tropinone
- pharmacology
- drug development
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
1.14.11.11
-
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RECOMMENDED NAME
GeneOntology No.
hyoscyamine (6S)-dioxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-hyoscyamine + 2-oxoglutarate + O2 = (6S)-hydroxyhyoscyamine + succinate + CO2
-
-
-
-
L-hyoscyamine + 2-oxoglutarate + O2 = (6S)-hydroxyhyoscyamine + succinate + CO2
proposed mechanism of epoxidation catalyzed by the enzyme, overview
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decarboxylation
-
-
-
-
epoxidation
-
-
-
-
hydroxylation
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
hydroxylation
-
-
-
-
hydroxylation
-
converts L-hyoscyamine to 6beta-hydroxyhyoscyamine and then to scopolamine
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
L-hyoscyamine,2-oxoglutarate:oxygen oxidoreductase ((6S)-hydroxylating)
Requires Fe2+ and ascorbate.
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CAS REGISTRY NUMBER
COMMENTARY
103865-33-4
-
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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
UniProt
-
-
-
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
additional information
evolution
the enzyme is a member of the 2-oxoglutarate-dependent dioxygenase family
evolution
the enzyme belongs to the 2-oxoglutarate-depedent dioxygenase family
metabolism
-
hyoscyamine 6b-hydroxylase, H6H, is an important enzyme in the biosynthesis of tropane alkaloids. It catalyzes the hydroxylation of hyoscyamine to give 6beta-hydroxyhyoscyamine and its epoxidation in the biosynthetic pathway leading to scopolamine. The DmrH6H epoxidase activity Is low compared to the hydroxylase activity
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 1.14.11.14
metabolism
hyoscyamine 6b-hydroxylase catalyzes two consecutive oxidation reactions. The first reaction is the hydroxylation of hyoscyamine to 6beta-hydroxyhyoscyamine and the second is epoxidation of 6beta-hydroxyhyoscyamine yielding scopolamine, EC 1.14.11.14, the final metabolite in the tropane alkaloid biosynthetic pathway
metabolism
the enzyme catalyzes the last two steps in the scopolamine biosynthetic pathway performing two consecutive oxidation reactions including the hydroxylation of hyoscyamine to 6beta-hydroxyhyoscyamine and the epoxidation of 6beta-hydroxyhyoscyamine to yield scopolamine. Biosynthesis pathway of tropane alkaloids, overview
metabolism
-
the enzyme catalyzes the hydroxylation of (-)-hyoscyamine and the subsequent epoxidation of 6beta-hydroxyhyoscyamine to form scopolamine, a natural alkaloid
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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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-hydroxy-3-phenylpropionyltropine + 2-oxoglutarate + O2
2-hydroxy-3-phenylpropionyl-6-hydroxytropine + succinate + CO2
-
15% of the activity with L-hyoscyamine
-
?
2-oxoglutarate + p-hydroxyatropine + O2
?
-
26% of the activity with L-hyoscyamine
-
-
?
2-oxoglutarate + trans-cinnamoyltropine + O2
succinate + trans-cinnamoyl-6-hydroxytropine + CO2
-
39% of the activity with L-hyoscyamine
-
?
3-hydroxy-3-phenylpropionyltropine + 2-oxoglutarate + O2
3-hydroxy-3-phenylpropionyl-6-hydroxytropine + succinate + CO2
-
56% of the activity with L-hyoscyamine
-
?
6,7-dehydrohyoscyamine + 2-oxoglutarate + O2
scopolamine + succinate + CO2
-
119% of the activity with L-hyoscyamine
-
?
6beta-hydroxyhyoscyamine
scopolamine
-
weak epoxidase activity, 2-5% of the hydroxylase activity
-
-
?
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
-
45% of the activity with L-hyoscyamine
-
?
hyoscyamine + O2 + 2-oxoglutarate + O2
scopolamine + succinate + CO2
-
-
-
-
?
isobutyltropine + 2-oxoglutarate + O2
?
-
15% of the activity with L-hyoscyamine
-
-
?
L-homatropine + 2-oxoglutarate + O2
6-hydroxyhomatropine + succinate + CO2
-
81% of the activity with L-hyoscyamine
-
?
L-norhyoscyamine + 2-oxoglutarate + O2
6-hydroxynorhyoscyamine + succinate + CO2
-
81% of the activity with L-hyoscyamine
-
?
noratropine-N-acetic acid + 2-oxoglutarate + O2
?
-
17% of the activity with L-hyoscyamine
-
-
?
phenylacetyltropine + 2-oxoglutarate + O2
6-hydroxyphenylacetyltropine + succinate + CO2
-
81% of the activity with L-hyoscyamine
-
?
phenylalanyltropine + 2-oxoglutarate + O2
?
-
8% of the activity with L-hyoscyamine
-
-
?
(6S)-6-hydroxyhyoscyamine + 2-oxoglutarate + O2
scopolamine + succinate + CO2
-
-
-
?
(6S)-6-hydroxyhyoscyamine + 2-oxoglutarate + O2
scopolamine + succinate + CO2
key enzyme in the biosynthesis pathway of scopolamine
-
-
?
(6S)-6-hydroxyhyoscyamine + 2-oxoglutarate + O2
scopolamine + succinate + CO2
-
-
-
?
(6S)-6-hydroxyhyoscyamine + 2-oxoglutarate + O2
scopolamine + succinate + CO2
-
-
-
-
?
(6S)-6-hydroxyhyoscyamine + 2-oxoglutarate + O2
scopolamine + succinate + CO2
-
-
-
-
ir
L-hyoscyamine + 2-oxoglutarate + O2
(6S)-hydroxyhyoscyamine + succinate + CO2
-
-
-
-
?
L-hyoscyamine + 2-oxoglutarate + O2
(6S)-hydroxyhyoscyamine + succinate + CO2
-
the enzyme catalyzes the hydroxylation of (-)-hyoscyamine and the subsequent epoxidation of 6beta-hydroxyhyoscyamine to form scopolamine, a natural alkaloid
-
-
?
L-hyoscyamine + 2-oxoglutarate + O2
(6S)-hydroxyhyoscyamine + succinate + CO2
-
-
-
-
?
L-hyoscyamine + 2-oxoglutarate + O2
(6S)-hydroxyhyoscyamine + succinate + CO2
-
-
-
?
L-hyoscyamine + 2-oxoglutarate + O2
(6S)-hydroxyhyoscyamine + succinate + CO2
-
-
H6H produces 6beta-hydroxyhyoscyamine and its derivative, scopolamine, the DmrH6H epoxidase activity is low compared to the hydroxylase activity
-
?
L-hyoscyamine + 2-oxoglutarate + O2
(6S)-hydroxyhyoscyamine + succinate + CO2
-
the binding of the substrates, hyoscyamine and 2-oxoglutarate, to the enzyme induces significant conformational changes
H6H produces 6beta-hydroxyhyoscyamine and its derivative, scopolamine, the DmrH6H epoxidase activity is low compared to the hydroxylase activity
-
?
L-hyoscyamine + 2-oxoglutarate + O2
(6S)-hydroxyhyoscyamine + succinate + CO2
-
-
-
?
L-hyoscyamine + 2-oxoglutarate + O2
6beta-hydroxyhyoscyamine + succinate + CO2
-
-
-
?
L-hyoscyamine + 2-oxoglutarate + O2
6beta-hydroxyhyoscyamine + succinate + CO2
key enzyme in the biosynthesis pathway of scopolamine
-
-
?
L-hyoscyamine + 2-oxoglutarate + O2
6beta-hydroxyhyoscyamine + succinate + CO2
-
-
-
?
L-hyoscyamine + 2-oxoglutarate + O2
6beta-hydroxyhyoscyamine + succinate + CO2
-
-
-
?
L-hyoscyamine + 2-oxoglutarate + O2
6beta-hydroxyhyoscyamine + succinate + CO2
-
-
-
?
L-hyoscyamine + 2-oxoglutarate + O2
6beta-hydroxyhyoscyamine + succinate + CO2
-
-
-
?
L-hyoscyamine + 2-oxoglutarate + O2
6beta-hydroxyhyoscyamine + succinate + CO2
-
-
-
?
L-hyoscyamine + 2-oxoglutarate + O2
6beta-hydroxyhyoscyamine + succinate + CO2
-
-
-
?
L-hyoscyamine + 2-oxoglutarate + O2
6beta-hydroxyhyoscyamine + succinate + CO2
Hyoscyamus gyorffi
-
-
-
?
L-hyoscyamine + 2-oxoglutarate + O2
6beta-hydroxyhyoscyamine + succinate + CO2
-
-
-
?
L-hyoscyamine + 2-oxoglutarate + O2
6beta-hydroxyhyoscyamine + succinate + CO2
-
-
-
?
L-hyoscyamine + 2-oxoglutarate + O2
6beta-hydroxyhyoscyamine + succinate + CO2
-
-
-
?
L-hyoscyamine + 2-oxoglutarate + O2
6beta-hydroxyhyoscyamine + succinate + CO2
-
-
-
?
L-hyoscyamine + 2-oxoglutarate + O2
6beta-hydroxyhyoscyamine + succinate + CO2
-
-
-
?
L-hyoscyamine + 2-oxoglutarate + O2
6beta-hydroxyhyoscyamine + succinate + CO2
-
-
-
?
L-hyoscyamine + 2-oxoglutarate + O2
6beta-hydroxyhyoscyamine + succinate + CO2
-
-
-
-
?
L-hyoscyamine + 2-oxoglutarate + O2
6beta-hydroxyhyoscyamine + succinate + CO2
-
-
-
-
ir
L-hyoscyamine + 2-oxoglutarate + O2
6beta-hydroxyhyoscyamine + succinate + CO2
-
only the L-isomer of hyoscyamine serves as substrate, D-hyoscyamine is nearly inactive
-
?
L-hyoscyamine + 2-oxoglutarate + O2
6beta-hydroxyhyoscyamine + succinate + CO2
-
the enzyme catalyzes two consecutive oxidation reactions leading from hyoscyamine to scopolamine
-
-
-
L-hyoscyamine + 2-oxoglutarate + O2
6beta-hydroxyhyoscyamine + succinate + CO2
-
enzyme is involved in biosynthetic pathway leading to scopolamine
-
?
L-hyoscyamine + 2-oxoglutarate + O2
6beta-hydroxyhyoscyamine + succinate + CO2
-
-
-
?
additional information
?
-
-
the enzyme also catalyzes the reaction of EC 1.14.11.14
-
-
-
additional information
?
-
-
the enzyme also catalyzes the reaction of EC 1.14.11.14
-
-
-
additional information
?
-
-
hyoscyamine 6beta-hydroxylase, a 2-oxoglutarate-dependent dioxygenase, converts L-hyoscyamine to its 6,7-epoxy derivative, scopolamine, in two sequential steps. 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, which is the reaction of EC 1.14.11.14, 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 reaction of EC 1.14.11.14
-
-
-
additional information
?
-
-
high specificity for 2-oxoglutarate in hydroxylation
-
-
-
additional information
?
-
-
the enzyme also catalyzes the reaction of EC 1.14.11.14
-
-
-
additional information
?
-
the enzyme also catalyzes the reaction of EC 1.14.11.14
-
-
-
additional information
?
-
-
methyl jasmonate and salicylic acid increase the expression of the enzyme
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
Q6V0J1
key enzyme in the biosynthesis pathway of scopolamine
-
-
?
(6S)-6-hydroxyhyoscyamine + 2-oxoglutarate + O2
scopolamine + succinate + CO2
-
-
-
-
?
L-hyoscyamine + 2-oxoglutarate + O2
(6S)-hydroxyhyoscyamine + succinate + CO2
-
-
-
-
?
L-hyoscyamine + 2-oxoglutarate + O2
(6S)-hydroxyhyoscyamine + succinate + CO2
-
the enzyme catalyzes the hydroxylation of (-)-hyoscyamine and the subsequent epoxidation of 6beta-hydroxyhyoscyamine to form scopolamine, a natural alkaloid
-
-
?
L-hyoscyamine + 2-oxoglutarate + O2
(6S)-hydroxyhyoscyamine + succinate + CO2
-
-
-
-
?
L-hyoscyamine + 2-oxoglutarate + O2
(6S)-hydroxyhyoscyamine + succinate + CO2
Q9XJ43
-
-
-
?
L-hyoscyamine + 2-oxoglutarate + O2
(6S)-hydroxyhyoscyamine + succinate + CO2
-
-
H6H produces 6beta-hydroxyhyoscyamine and its derivative, scopolamine, the DmrH6H epoxidase activity is low compared to the hydroxylase activity
-
?
L-hyoscyamine + 2-oxoglutarate + O2
(6S)-hydroxyhyoscyamine + succinate + CO2
J7HDC2
-
-
-
?
L-hyoscyamine + 2-oxoglutarate + O2
6beta-hydroxyhyoscyamine + succinate + CO2
Q6V0J1
key enzyme in the biosynthesis pathway of scopolamine
-
-
?
L-hyoscyamine + 2-oxoglutarate + O2
6beta-hydroxyhyoscyamine + succinate + CO2
-
-
-
-
?
L-hyoscyamine + 2-oxoglutarate + O2
6beta-hydroxyhyoscyamine + succinate + CO2
-
the enzyme catalyzes two consecutive oxidation reactions leading from hyoscyamine to scopolamine
-
-
-
L-hyoscyamine + 2-oxoglutarate + O2
6beta-hydroxyhyoscyamine + succinate + CO2
-
enzyme is involved in biosynthetic pathway leading to 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. 6,7-Dehydrohyoscyamine, a potential precursor for the last step of epoxidation, is an obligatory intermediate in the biosynthesis of scopolamine
-
-
-
additional information
?
-
-
methyl jasmonate and salicylic acid increase the expression of the enzyme
-
-
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Fe2+
without addition of Fe2+, only 1.3% of the activity is detected
Fe2+
-
dependent, about 25-30% decreased production of scopolamine and hyoscyamine in absence of iron in medium
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INHIBITORS
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
8-methyl-8-azabicyclo[3.2.1]octan-3-yl 2-(4-(dimethylamino)phenyl)acetate
-
-
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
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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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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
7.8
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
cell culture, methyl jasmonate and salicylic acid increase the expression of the enzyme
additional information
-
enzyme is constitutively expressed in all tissues examined
additional information
-
no activity in stem, leaf, pistil, petal and sepal tissue
additional information
-
mRNA of the hydroxylase is absent in leaves, stems and cultured cells
additional information
H6H tissue expression analysis, overview
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
39000
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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SUBUNITS
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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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acetone
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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 His-tagged enzyme from Escherichia coli by nickel affinity chromatography
-
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
cDNA from Hyoscyamus niger is simultaneously introduced into Nicotiana tabacum using particle bombardment and expressed under the control of the CaMV 35S promoter
-
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 as a fusion protein to maltose-binding protein
-
gene h6h, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, gene expression profiling and real-time RT-PCR analysis
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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T1 progeny of transgenic Atropa belladonna, in which putrescine N-methyltransferase (EC 2.1.1.53) from Nicotiana tabacum (NtPMT) and hyoscyamine 6beta-hydroxylase (EC 1.14.11.14) from Hyoscyamus niger (HnH6H) are overexpressed, are established to investigate tropane alkaloids biosynthesis and distribution in ripe fruits, leaves, stems, primary roots and secondary roots under field conditions. Both NtPMT and HnH6H are detected at the transcriptional level in transgenic plants, whereas they are not detected in wild-type plants. Metabolically engineered Atropa belladonna based on overexpressing NtPMT and HnH6H shows a chemotype of rich scopolamine that greatly improves the commercial and pharmaceutical properties of Atropa belladonna
the gene encoding hyosyamine 6-hydroxylase is placed under the regulation of the CaMV 35S promoter and introduced into the genome of a scopolamine-rich Duboisia hybrid by a binary vector system using Agrobacterium rhizogenes strain LBA9402. The scopolamine levels in the resulting engineered hairy root lines increases up to three times compared to wild-type hairy roots, but there is no clear increase in the engineered regenerated plants
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the h6hcDNA is amplified from Brugmansia candida total RNA preparations, it is inserted in frame to the trx tag into the pET32a(+) vector. Escherichia coli Origami strains are used as host for the expression. Produce of high quantities of a soluble and functional enzyme
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
trivalent chromium, as KCr(SO4)2, induces the enzyme expression at 1 mM
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K97A
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the shows a 3.3fold improved hydroxylation activity compared with the wild-type enzyme
K97E
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the shows a 2.7fold improved hydroxylation activity compared with the wild-type enzyme
K97G
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the shows a 1.7fold improved hydroxylation activity compared with the wild-type enzyme
S14H
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the shows a 2.4fold improved hydroxylation activity compared with the wild-type enzyme
S14P
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the shows a 3.7fold improved hydroxylation activity compared with the wild-type enzyme
S14P/K97A
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double mutant shows a 4.4fold improved hydroxylation activity compared with the wild-type enzyme, and the in vivo epoxidation activity is also improved by 2.3times. With this mutant, in a 5 l bioreactor with a working volume of 3 l, scopolamine is produced via a single-enzyme-mediated two-step transformation from hyoscyamine of 500 mg/l in 97% yield (1.068 g)
additional information
additional information
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enhanced 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 tropan alkaloid contents in transgenic lines, overview
additional information
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functional expression in Saccharomyces cerevisiae as tagged and untagged proteins. The untagged form is about 3-fold as active as the tagged protein
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
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tropane alkaloids, such as hyoscyamine, 6-hydroxyhyoscyamine and scopolamine, are secondary metabolites that are traditionally applied in medicine due to their anticholinergic activity. An alternative strategy for the production of the most valuable alkaloids, 6beta-hydroxyhyoscyamine and scopolamine, using Escherichia coli harboring the hyoscyamine-6beta-hydroxylase enzyme as biocatalysts is developed
pharmacology
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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
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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.11.11)
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