BRENDA - Enzyme Database show
show all sequences of 1.1.1.206

Molecular cloning and catalytic characterization of a recombinant tropine biosynthetic tropinone reductase from Withania coagulans leaf

Kushwaha, A.K.; Sangwan, N.S.; Tripathi, S.; Sangwan, R.S.; Gene 516, 238-247 (2013)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene TRI, isolated from aerial tissue, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, overexpression of the His-tagged enzyme in Escherichia coli strain BL21 (DE3)
Withania coagulans
Inhibitors
Inhibitors
Commentary
Organism
Structure
K+
slight inhibitory effect at 5 mM
Withania coagulans
Li+
slight inhibitory effect at 5 mM
Withania coagulans
Na+
slight inhibitory effect at 5 mM
Withania coagulans
NH4+
slight inhibitory effect at 5 mM
Withania coagulans
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.126
-
NADPH
pH 6.6, 30°C, recombinant enzyme
Withania coagulans
0.208
-
NADP+
pH 6.6, 30°C, recombinant enzyme
Withania coagulans
1.451
-
tropinone
pH 6.6, 30°C, recombinant enzyme
Withania coagulans
26.31
-
Tropine
pH 6.6, 30°C, recombinant enzyme
Withania coagulans
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
29340
-
x * 29340, sequence calculation
Withania coagulans
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Withania coagulans
the enzyme TR-I has a wide substrate specificity but does not cover the substrates of other well-known plant SDR related to menthol metabolism
?
-
-
-
tropinone + NADPH + H+
Withania coagulans
preferred substrate
tropine + NADP+
-
-
r
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Withania coagulans
L7QI79
-
-
Purification (Commentary)
Commentary
Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography
Withania coagulans
Source Tissue
Source Tissue
Commentary
Organism
Textmining
leaf
-
Withania coagulans
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1-methylpyrrolidine + NADPH + H+
-
725098
Withania coagulans
? + NADP+
-
-
-
?
1-propyl-4-piperidone + NADPH + H+
-
725098
Withania coagulans
? + NADP+
-
-
-
?
2-pyrrolidone + NADPH + H+
-
725098
Withania coagulans
? + NADP+
-
-
-
?
3-methylcyclohexanone + NADPH + H+
-
725098
Withania coagulans
? + NADP+
-
-
-
?
4-chlor-1-methylpiperidine + NADPH + H+
-
725098
Withania coagulans
? + NADP+
-
-
-
?
4-ethylcyclohexanone + NADPH + H+
-
725098
Withania coagulans
4-ethylcyclohexanol + NADP+
-
-
-
?
4-methylcyclohexanone + NADPH + H+
-
725098
Withania coagulans
4-methylcyclohexanol + NADP+
-
-
-
?
4-piperidone + NADPH + H+
-
725098
Withania coagulans
? + NADP+
-
-
-
?
exo-6-hydroxytropinone + NADPH + H+
-
725098
Withania coagulans
? + NADP+
-
-
-
?
additional information
the enzyme TR-I has a wide substrate specificity but does not cover the substrates of other well-known plant SDR related to menthol metabolism
725098
Withania coagulans
?
-
-
-
-
additional information
no activity by TR-I with 1-methyl-2-pyrrolidone
725098
Withania coagulans
?
-
-
-
-
N-methyl-4-piperidone + NADPH + H+
-
725098
Withania coagulans
? + NADP+
-
-
-
?
N-methylpiperidine + NADPH + H+
-
725098
Withania coagulans
? + NADP+
-
-
-
?
tetrahydro-4H-thiopyran-4-one + NADPH + H+
-
725098
Withania coagulans
? + NADP+
-
-
-
?
tropine + NADP+
in vitro reaction kinetics show that the enzyme predominantly favours the reverse reaction
725098
Withania coagulans
tropinone + NADPH + H+
-
-
-
r
tropinone + NADPH + H+
best substrate
725098
Withania coagulans
tropine + NADP+
-
-
-
r
tropinone + NADPH + H+
preferred substrate
725098
Withania coagulans
tropine + NADP+
-
-
-
r
Subunits
Subunits
Commentary
Organism
?
x * 29340, sequence calculation
Withania coagulans
More
superimposition of three-dimensional models of tropinone reductases,overview
Withania coagulans
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
assay at
Withania coagulans
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
50
-
purified recombinant enzyme, 30 min, over 92% of maximal activity remaining
Withania coagulans
60
-
purified recombinant enzyme, 30 min, 30% of maximal activity remaining
Withania coagulans
70
-
purified recombinant enzyme, 30 min, 7% of maximal activity remaining
Withania coagulans
80
-
purified recombinant enzyme, 30 min, inactivation
Withania coagulans
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
1.87
-
Tropine
pH 6.6, 30°C, recombinant enzyme
Withania coagulans
2.94
-
NADP+
pH 6.6, 30°C, recombinant enzyme
Withania coagulans
6.76
-
NADPH
pH 6.6, 30°C, recombinant enzyme
Withania coagulans
16.74
-
tropinone
pH 6.6, 30°C, recombinant enzyme
Withania coagulans
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.6
-
-
Withania coagulans
pH Range
pH Minimum
pH Maximum
Commentary
Organism
6.1
7
narrow pH range
Withania coagulans
Cofactor
Cofactor
Commentary
Organism
Structure
NADP+
-
Withania coagulans
NADPH
-
Withania coagulans
Cloned(Commentary) (protein specific)
Commentary
Organism
gene TRI, isolated from aerial tissue, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, overexpression of the His-tagged enzyme in Escherichia coli strain BL21 (DE3)
Withania coagulans
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADP+
-
Withania coagulans
NADPH
-
Withania coagulans
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
K+
slight inhibitory effect at 5 mM
Withania coagulans
Li+
slight inhibitory effect at 5 mM
Withania coagulans
Na+
slight inhibitory effect at 5 mM
Withania coagulans
NH4+
slight inhibitory effect at 5 mM
Withania coagulans
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.126
-
NADPH
pH 6.6, 30°C, recombinant enzyme
Withania coagulans
0.208
-
NADP+
pH 6.6, 30°C, recombinant enzyme
Withania coagulans
1.451
-
tropinone
pH 6.6, 30°C, recombinant enzyme
Withania coagulans
26.31
-
Tropine
pH 6.6, 30°C, recombinant enzyme
Withania coagulans
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
29340
-
x * 29340, sequence calculation
Withania coagulans
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Withania coagulans
the enzyme TR-I has a wide substrate specificity but does not cover the substrates of other well-known plant SDR related to menthol metabolism
?
-
-
-
tropinone + NADPH + H+
Withania coagulans
preferred substrate
tropine + NADP+
-
-
r
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography
Withania coagulans
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
leaf
-
Withania coagulans
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1-methylpyrrolidine + NADPH + H+
-
725098
Withania coagulans
? + NADP+
-
-
-
?
1-propyl-4-piperidone + NADPH + H+
-
725098
Withania coagulans
? + NADP+
-
-
-
?
2-pyrrolidone + NADPH + H+
-
725098
Withania coagulans
? + NADP+
-
-
-
?
3-methylcyclohexanone + NADPH + H+
-
725098
Withania coagulans
? + NADP+
-
-
-
?
4-chlor-1-methylpiperidine + NADPH + H+
-
725098
Withania coagulans
? + NADP+
-
-
-
?
4-ethylcyclohexanone + NADPH + H+
-
725098
Withania coagulans
4-ethylcyclohexanol + NADP+
-
-
-
?
4-methylcyclohexanone + NADPH + H+
-
725098
Withania coagulans
4-methylcyclohexanol + NADP+
-
-
-
?
4-piperidone + NADPH + H+
-
725098
Withania coagulans
? + NADP+
-
-
-
?
exo-6-hydroxytropinone + NADPH + H+
-
725098
Withania coagulans
? + NADP+
-
-
-
?
additional information
the enzyme TR-I has a wide substrate specificity but does not cover the substrates of other well-known plant SDR related to menthol metabolism
725098
Withania coagulans
?
-
-
-
-
additional information
no activity by TR-I with 1-methyl-2-pyrrolidone
725098
Withania coagulans
?
-
-
-
-
N-methyl-4-piperidone + NADPH + H+
-
725098
Withania coagulans
? + NADP+
-
-
-
?
N-methylpiperidine + NADPH + H+
-
725098
Withania coagulans
? + NADP+
-
-
-
?
tetrahydro-4H-thiopyran-4-one + NADPH + H+
-
725098
Withania coagulans
? + NADP+
-
-
-
?
tropine + NADP+
in vitro reaction kinetics show that the enzyme predominantly favours the reverse reaction
725098
Withania coagulans
tropinone + NADPH + H+
-
-
-
r
tropinone + NADPH + H+
best substrate
725098
Withania coagulans
tropine + NADP+
-
-
-
r
tropinone + NADPH + H+
preferred substrate
725098
Withania coagulans
tropine + NADP+
-
-
-
r
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 29340, sequence calculation
Withania coagulans
More
superimposition of three-dimensional models of tropinone reductases,overview
Withania coagulans
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
assay at
Withania coagulans
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
50
-
purified recombinant enzyme, 30 min, over 92% of maximal activity remaining
Withania coagulans
60
-
purified recombinant enzyme, 30 min, 30% of maximal activity remaining
Withania coagulans
70
-
purified recombinant enzyme, 30 min, 7% of maximal activity remaining
Withania coagulans
80
-
purified recombinant enzyme, 30 min, inactivation
Withania coagulans
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
1.87
-
Tropine
pH 6.6, 30°C, recombinant enzyme
Withania coagulans
2.94
-
NADP+
pH 6.6, 30°C, recombinant enzyme
Withania coagulans
6.76
-
NADPH
pH 6.6, 30°C, recombinant enzyme
Withania coagulans
16.74
-
tropinone
pH 6.6, 30°C, recombinant enzyme
Withania coagulans
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.6
-
-
Withania coagulans
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
6.1
7
narrow pH range
Withania coagulans
General Information
General Information
Commentary
Organism
evolution
tropinone reductase TR-I belongs to the short chain dehydrogenase/reductase family, SDR, of enzymes and has a YSASK as the signature YXXXK motif of SDRs, catalytic tetrade comprises N, S, Y, and K residues, overview
Withania coagulans
metabolism
the enzyme catalyzes a step intermediary enroute to biosynthesis of tropane esters of medicinal importance, i.e. hyoscyamine/scopolamine
Withania coagulans
additional information
superimposition of three-dimensional models of tropinone reductases,overview
Withania coagulans
General Information (protein specific)
General Information
Commentary
Organism
evolution
tropinone reductase TR-I belongs to the short chain dehydrogenase/reductase family, SDR, of enzymes and has a YSASK as the signature YXXXK motif of SDRs, catalytic tetrade comprises N, S, Y, and K residues, overview
Withania coagulans
metabolism
the enzyme catalyzes a step intermediary enroute to biosynthesis of tropane esters of medicinal importance, i.e. hyoscyamine/scopolamine
Withania coagulans
additional information
superimposition of three-dimensional models of tropinone reductases,overview
Withania coagulans
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.071
-
Tropine
pH 6.6, 30°C, recombinant enzyme
Withania coagulans
11.53
-
tropinone
pH 6.6, 30°C, recombinant enzyme
Withania coagulans
14
-
NADP+
pH 6.6, 30°C, recombinant enzyme
Withania coagulans
53
-
NADPH
pH 6.6, 30°C, recombinant enzyme
Withania coagulans
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.071
-
Tropine
pH 6.6, 30°C, recombinant enzyme
Withania coagulans
11.53
-
tropinone
pH 6.6, 30°C, recombinant enzyme
Withania coagulans
14
-
NADP+
pH 6.6, 30°C, recombinant enzyme
Withania coagulans
53
-
NADPH
pH 6.6, 30°C, recombinant enzyme
Withania coagulans
Other publictions for EC 1.1.1.206
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
725098
Kushwaha
Molecular cloning and catalyti ...
Withania coagulans
Gene
516
238-247
2013
-
-
1
-
-
-
4
4
-
-
1
2
-
4
-
-
1
-
-
2
-
-
17
2
1
-
4
4
1
1
-
2
-
-
-
-
-
1
2
-
-
-
-
4
-
4
-
-
1
2
-
-
-
1
-
2
-
-
17
2
1
-
4
4
1
1
-
-
-
3
3
-
4
4
726209
Dehghan
An atypical pattern of accumul ...
Hyoscyamus muticus, Hyoscyamus senecionis
Plant Physiol. Biochem.
70C
188-194
2013
-
-
-
-
-
-
-
-
-
-
-
2
-
4
-
-
-
-
-
3
-
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
3
-
-
2
-
-
-
-
-
-
-
-
-
-
2
2
-
-
-
725946
Kai
Enhancing the production of tr ...
Anisodus acutangulus
Mol. Biosyst.
8
2883-2890
2012
-
1
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
719169
Kai
Co-expression of AaPMT and AaT ...
Anisodus acutangulus
BMC Biotechnol.
11
43
2011
-
1
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
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-
-
1
-
-
-
-
-
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-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
696874
Kai
Molecular cloning, characteriz ...
Anisodus acutangulus
Biotechnol. Appl. Biochem.
54
:177-186
2009
1
-
1
-
-
-
1
-
-
-
1
-
-
1
-
-
-
-
-
3
-
-
1
-
-
-
-
-
-
-
-
-
-
1
-
1
-
1
-
-
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
3
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
689548
Brock
The functional divergence of s ...
Cochlearia officinalis
Plant J.
54
388-401
2008
-
-
1
-
-
-
-
-
-
-
-
2
-
1
-
-
-
-
-
-
-
-
4
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
4
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
689953
Freydank
Protein structure modeling ind ...
Solanum dulcamara
Proteins
72
173-183
2008
-
-
1
-
-
-
-
-
-
-
-
1
-
3
-
-
1
-
-
-
-
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
1
2
-
-
-
-
-
-
-
-
-
-
1
-
-
-
1
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
670518
Draeger
Tropinone reductases, enzymes ...
Atropa belladonna, Datura stramonium, Duboisia leichhardtii, Duboisia myoporoides, Hyoscyamus muticus, Hyoscyamus niger, Scopolia atropoides
Phytochemistry
67
327-337
2006
-
-
-
-
-
-
-
7
-
-
-
7
-
9
-
-
-
-
-
-
-
-
27
-
-
-
-
1
4
-
-
7
-
-
-
-
-
-
7
-
-
-
-
-
-
7
-
-
-
7
-
-
-
-
-
-
-
-
27
-
-
-
-
1
4
-
-
-
-
-
-
-
-
-
656413
Richter
Overexpression of tropinone re ...
Atropa belladonna, Datura stramonium
J. Exp. Bot.
56
645-652
2005
-
-
2
-
2
-
-
-
-
-
-
2
-
2
-
-
1
-
-
1
1
-
4
-
2
-
-
-
2
-
-
2
-
-
-
-
-
2
2
-
2
-
-
-
-
-
-
-
-
2
-
-
-
1
-
1
1
-
4
-
2
-
-
-
2
-
-
-
-
-
-
-
-
-
439278
Rocha
-
Functional expression of tropi ...
Hyoscyamus niger
Plant Sci.
162
905-913
2002
-
-
1
-
-
-
-
-
-
-
-
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-
1
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
347972
Nakajima
Site-directed mutagenesis of p ...
Datura stramonium
J. Biol. Chem.
274
16563-16568
1999
-
-
1
-
5
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
5
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
347973
Boswell
Specificities of the enzymes o ...
Brugmansia sp., Datura stramonium
Phytochemistry
52
871-878
1999
-
-
-
-
-
-
-
-
-
-
-
-
-
6
-
-
2
-
-
2
-
-
25
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
2
-
-
25
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
348028
Nakajima
Crystal structures of two trop ...
Datura stramonium
Proc. Natl. Acad. Sci. USA
95
4876-4881
1998
-
-
1
1
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
347970
Bartholomew
-
Tropine dehydrogenase: purific ...
Pseudomonas sp., Pseudomonas sp. AT3
Biochem. J.
307
603-608
1995
-
-
-
-
-
-
-
3
-
-
2
2
-
4
-
-
1
-
-
-
2
-
6
1
-
-
1
-
-
-
-
2
-
-
-
-
-
-
2
-
-
-
-
-
-
3
-
-
2
2
-
-
-
1
-
-
2
-
6
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
347969
Nakajima
Opposite stereospecificity of ...
Datura stramonium
J. Biol. Chem.
269
11695-11698
1994
-
-
1
-
1
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
1
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
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-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
348024
Hashimoto
Two tropinone reductases with ...
Atropa acuminata, Atropa belladonna, Datura stramonium, Duboisia hopwoodii, Duboisia leichhardtii, Hyoscyamus albus, Hyoscyamus bohemicus, Hyoscyamus canariensis, Hyoscyamus muticus, Hyoscyamus niger, Hyoscyamus niger Hn, Hyoscyamus pusillus, no activity in Brassica campestris, no activity in Browallia americana, no activity in Calystegia sepium, no activity in Nicotiana tabacum, no activity in Physalis alkekengi, Physalis edulis, Physalis philadelphica, Physochlaina orientalis
Plant Physiol.
100
836-845
1992
-
-
-
-
-
-
16
11
-
-
2
-
-
20
-
-
1
-
-
4
15
1
18
1
-
-
-
-
2
-
-
3
-
-
-
-
-
-
3
-
-
-
-
16
-
11
-
-
2
-
-
-
-
1
-
4
15
1
18
1
-
-
-
-
2
-
-
-
-
-
-
-
-
-
347967
Koelen
Partial purification and prope ...
Datura stramonium
J. Med. Plant Res.
44
227-230
1982
-
-
-
-
-
-
1
7
-
-
1
1
-
2
-
-
1
-
-
1
-
4
4
-
1
-
4
-
2
-
1
2
-
-
-
-
-
-
2
-
-
-
-
1
-
7
-
-
1
1
-
-
-
1
-
1
-
4
4
-
1
-
4
-
2
-
1
-
-
-
-
-
-
-