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Information on EC 1.14.11.11 - hyoscyamine (6S)-dioxygenase
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1.14.11.11 hyoscyamine (6S)-dioxygenaseIUBMB Comments
Requires Fe2+ and ascorbate.
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Word Map
- 1.14.11.11
- scopolamine
-
tropane
- hyoscyamus
- niger
- belladonna
-
atropa
-
anisodus
- acutangulus
-
hairy
-
anticholinergic
-
6beta-hydroxylase
-
aerial
-
epoxidation
-
2-oxoglutarate-dependent
-
anisodamine
- n-methyltransferase
-
agrobacterium-mediated
- tanguticus
- datura
-
solanaceous
- putrescine
- metel
- tropinone
-
genetically-engineered
- pericycle
-
catharanthus
-
high-value
- roseus
-
2.1.1.53
-
biofunctional
-
gst-tag
-
bolt
-
underground
- tabacum
-
chemotype
- vindoline
- drug development
- pharmacology
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
6H6, AaH6H, AtH6H, H6H, HnH6H, hyoscyamine 6-hydroxylase, hyoscyamine 6beta-hydroxylase, hyoscyamine-6beta-hydroxylase, oxygenase, hyoscyamine 6beta-di-, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
H6H
hyoscyamine 6-hydroxylase
-
-
-
-
hyoscyamine 6beta-hydroxylase
oxygenase, hyoscyamine 6beta-di-
-
-
-
-
hyoscyamine 6beta-hydroxylase
-
-
-
-
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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 SOURCE
PATHWAYS
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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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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 + succinate + CO2
L-hyoscyamine + 2-oxoglutarate + O2
-
-
-
r
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
-
-
-
-
?
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
?
-
-
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 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
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
-
-
-
-
?
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
-
-
-
?
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
-
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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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
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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
collected from Sari-Garmestan of Mazandaran province in the North of Iran, gene h6h
UniProt
brenda
-
-
-
brenda
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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
brenda
additional information
enzyme is constitutively expressed in all tissues examined
brenda
additional information
-
enzyme is constitutively expressed in all tissues examined
brenda
additional information
-
no activity in stem, leaf, pistil, petal and sepal tissue
brenda
additional information
-
mRNA of the hydroxylase is absent in leaves, stems and cultured cells
brenda
additional information
H6H tissue expression analysis, overview
brenda
additional information
-
H6H tissue expression analysis, overview
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
additional information
evolution
the enzyme belongs to the 2-oxoglutarate-depedent dioxygenase family
evolution
the enzyme is a member of the 2-oxoglutarate-dependent 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 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
-
hyoscyamine 6beta-hydroxylase converts hyoscyamine to scopolamine in the last step of scopolamine 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 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
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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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). HY6H_HYONI
344
0
39001
Swiss-Prot
other Location (Reliability: 3)
A0A0M4K1P1_DATST
347
0
39557
TrEMBL
other Location (Reliability: 3)
Q9XJ43_ATRBE
343
0
38547
TrEMBL
other Location (Reliability: 3)
B9RZI6_RICCO
346
0
39996
TrEMBL
other Location (Reliability: 2)
A0A1S6LXV6_9SOLA
311
0
35275
TrEMBL
other Location (Reliability: 5)
A0A2G9GFH2_9LAMI
254
0
29286
TrEMBL
other Location (Reliability: 3)
R4QZR8_9SOLA
344
0
38909
TrEMBL
other Location (Reliability: 4)
A0A6M6R352_MANOF
344
0
38936
TrEMBL
other Location (Reliability: 3)
A0A2P6P4I8_ROSCH
189
0
21424
TrEMBL
Mitochondrion (Reliability: 2)
A0A396GTW0_MEDTR
354
0
39090
TrEMBL
other Location (Reliability: 5)
B9T297_RICCO
333
0
38006
TrEMBL
other Location (Reliability: 3)
A2IBI0_9SOLA
344
0
38772
TrEMBL
other Location (Reliability: 2)
A0A2G9I024_9LAMI
336
0
37595
TrEMBL
other Location (Reliability: 5)
A0A2G9H9J9_9LAMI
349
0
40041
TrEMBL
other Location (Reliability: 2)
A0A2P6PVD5_ROSCH
72
0
8100
TrEMBL
Mitochondrion (Reliability: 5)
A0A2P6PVD3_ROSCH
173
0
19800
TrEMBL
other Location (Reliability: 4)
A0A6M6R148_9SOLA
344
0
38652
TrEMBL
other Location (Reliability: 3)
A0A396JP41_MEDTR
128
0
15244
TrEMBL
other Location (Reliability: 2)
A0A2G9GG96_9LAMI
334
0
37416
TrEMBL
other Location (Reliability: 4)
A0A396JUZ7_MEDTR
344
0
39818
TrEMBL
other Location (Reliability: 2)
B2CNC8_9SOLA
344
0
39001
TrEMBL
other Location (Reliability: 3)
A0A0M3SG09_BRUAR
347
0
39235
TrEMBL
other Location (Reliability: 2)
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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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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
K97A
the shows a 3.3fold improved hydroxylation activity compared with the wild-type enzyme
K97E
the shows a 2.7fold improved hydroxylation activity compared with the wild-type enzyme
K97G
the shows a 1.7fold improved hydroxylation activity compared with the wild-type enzyme
S14H
the shows a 2.4fold improved hydroxylation activity compared with the wild-type enzyme
S14P
the shows a 3.7fold improved hydroxylation activity compared with the wild-type enzyme
S14P/K97A
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
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
-
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
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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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
-
expression in Saccharomyces cerevisiae in tagged and untagged form
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
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
-
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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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
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
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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Eur. J. Biochem.
164
277-285
1987
Hyoscyamus niger
brenda
Matsuda, J.; Okabe, S.; Hashimoto, T.; Yamada, Y.
Molecular cloning of hyoscyamine 6 beta-hydroxylase, a 2-oxoglutarate-dependent dioxygenase, from cultured roots of Hyoscyamus niger
J. Biol. Chem.
266
9460-9464
1991
Hyoscyamus niger
brenda
Hashimoto, T.; Yamada, Y.
Hyoscyamine 6beta-hydroxylase, a 2-oxoglutarate-dependent dioxygenase, an alkaloid-producing root cultures
Plant Physiol.
81
619-625
1986
Atropa belladonna, Datura metel, Duboisia leichhardtii, Hyoscyamus albus, Hyoscyamus gyorffi, Hyoscyamus muticus, Hyoscyamus niger, Hyoscyamus pusillus
brenda
Rocha, P.; Stenzel, O.; Parr, A.; Walton, N.; Christou, P.; Drager, B.; Leech, M.J.
Functional expression of tropinone reductase I (trI) and hyoscyamine-6beta-hydroxylase (h6h) from Hyoscyamus niger in Nicotiana tabacum
Plant Sci.
162
905-913
2002
Hyoscyamus niger
-
brenda
Yun, D.J.; Hashimoto, T.; Yamada, Y.
Transgenic tobacco plants with two consecutive oxidation reactions catalyzed by hyoscyamine 6b-hydroxylase
Biosci. Biotechnol. Biochem.
57
502-503
1993
Hyoscyamus niger
-
brenda
Suzuki, K.I.; 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.
40
141-152
1999
Atropa belladonna
brenda
Matsuda, J.; Hashimoto, T.; Yamada, Y.
Analysis of active-site residues in hyoscyamine 6beta-hydroxylase
Plant Biotechnol.
14
51-57
1997
Hyoscyamus niger
-
brenda
Palazon, J.; Moyano, E.; Cusido, R.M.; Bonfill, M.; Oksman-Caldentey, K.M.; Pinol, M.T.
Alkaloid production in Duboisia hybrid hairy roots and plants overexpressing the h6h gene
Plant Sci.
165
1289-1295
2003
Hyoscyamus niger
-
brenda
Kang, S.M.; Jung, H.Y.; Kang, Y.M.; Yun, D.J.; Bahk, J.D.; Yang, J.k.; Choi, M.S.
Effects of methyl jasmonate and salicylic acid on the production of tropane alkaloids and the expression of PMT and H6H in adventitious root cultures of Scopolia parviflora
Plant Sci.
166
745-751
2004
Scopolia parviflora
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.
71
249-253
2005
Anisodus tanguticus (Q6V0J1), Anisodus tanguticus
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
Biotechnol. Lett.
28
1271-1277
2006
Hyoscyamus niger
brenda
Rahman, L.u.; Kitamura, Y.; Yamaguchi, J.; Mukai, M.; Akiyama, K.; Yamamoto, H.; Muranaka, T.; Ikenaga, T.
Exogenous plant H6H but not bacterial HCHL gene is expressed in Duboisia leichhardtii hairy roots and affects tropane alkaloid production
Enzyme Microb. Technol.
39
1183-1189
2006
Hyoscyamus niger
-
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
J. Exp. Bot.
56
2611-2618
2005
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
J. Biochem. Mol. Biol.
40
715-722
2007
Anisodus acutangulus (A2IBI0), Anisodus acutangulus
brenda
Cardillo, A.B.; Talou, J.R.; Giulietti, A.M.
Expression of Brugmansia candida hyoscyamine 6beta-hydroxylase gene in Saccharomyces cerevisiae and its potential use as biocatalyst
Microb. Cell Fact.
7
17
2008
Brugmansia x candida (B2CNC8)
brenda
Higa, A.; Miyamoto, E.; Rahman, L.u.; Kitamura, Y.
Root tip-dependent, active riboflavin secretion by Hyoscyamus albus hairy roots under iron deficiency
Plant Physiol. Biochem.
46
452-460
2008
Hyoscyamus albus
brenda
Jaber-Vazdekis, N.; Gonzalez, C.; Ravelo, A.G.; Zarate, R.
Cloning, characterization and analysis of expression profiles of a cDNA encoding a hyoscyamine 6beta-hydroxylase (H6H) from Atropa baetica Willk
Plant Physiol. Biochem.
47
20-25
2009
Atropa baetica (A9Q1G4), Atropa baetica
brenda
Pramod, K.K.; Singh, S.; Jayabaskaran, C.
Biochemical and structural characterization of recombinant hyoscyamine 6beta-hydroxylase from Datura metel L
Plant Physiol. Biochem.
48
966-970
2010
Datura metel
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.
Functional identification of hyoscyamine 6beta-hydroxylase from Anisodus acutangulus and overproduction of scopolamine in genetically-engineered Escherichia coli
Biotechnol. Lett.
33
1361-1365
2011
Anisodus acutangulus
brenda
Kai, G.; Zhang, A.; Guo, Y.; Li, L.; Cui, L.; Luo, X.; Liu, C.; Xiao, J.
Enhancing the production of tropane alkaloids in transgenic Anisodus acutangulus hairy root cultures by over-expressing tropinone reductase I and hyoscyamine-6beta-hydroxylase
Mol. Biosyst.
8
2883-2890
2012
Anisodus acutangulus (A2IBI0), Anisodus acutangulus
brenda
Vakili, B.; Karimi, F.; Sharifi, M.; Behmanesh, M.
Chromium-induced tropane alkaloid production and H6H gene expression in Atropa belladonna L. (Solanaceae) in vitro-propagated plantlets
Plant Physiol. Biochem.
52
98-103
2012
Atropa belladonna (Q9XJ43)
brenda
Dehghan, E.; Shahriari Ahmadi, F.; Ghotbi Ravandi, E.; Reed, D.W.; Covello, P.S.; Bahrami, A.R.
An atypical pattern of accumulation of scopolamine and other tropane alkaloids and expression of alkaloid pathway genes in Hyoscyamus senecionis
Plant Physiol. Biochem.
70
188-194
2013
Hyoscyamus senecionis (J7HDC2), Hyoscyamus senecionis
brenda
Cardillo, A.; Perassolo, M.; Sartuqui, M.; Rodriguez Talou, J.; Giulietti, A.
Production of tropane alkaloids by biotransformation using recombinant Escherichia coli whole cells
Biochem. Eng. J.
125
180-189
2017
Brugmansia x candida (B2CNC8)
-
brenda
Cao, Y.D.; He, Y.C.; Li, H.; Kai, G.Y.; Xu, J.H.; Yu, H.L.
Efficient biosynthesis of rare natural product scopolamine using E. coli cells expressing a S14P/K97A mutant of hyoscyamine 6beta-hydroxylase AaH6H
J. Biotechnol.
211
123-129
2015
Anisodus acutangulus (A2IBI0), Anisodus acutangulus
brenda
Xia, K.; Liu, X.; Zhang, Q.; Qiang, W.; Guo, J.; Lan, X.; Chen, M.; Liao, Z.
Promoting scopolamine biosynthesis in transgenic Atropa belladonna plants with pmt and h6h overexpression under field conditions
Plant Physiol. Biochem.
106
46-53
2016
Hyoscyamus niger (P24397), Hyoscyamus niger
brenda
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