BRENDA - Enzyme Database
show all sequences of 1.3.1.3

Crystal structures of human Delta4-3-ketosteroid 5beta-reductase (AKR1D1) reveal the presence of an alternative binding site responsible for substrate inhibition

Faucher, F.; Cantin, L.; Luu-The, V.; Labrie, F.; Breton, R.; Biochemistry 47, 13537-13546 (2008)

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
expression of GST-tagged enzyme in Escherichia coli
Homo sapiens
Crystallization (Commentary)
Crystallization (Commentary)
Organism
purifed recombinant h5beta-red in ternary complex with NADPH and androstenedione, hanging-drop vapor diffusion technique, 2:1 v/v ratio of protein and well solution, about 5 days, X-ray diffraction structure determination and analysis at 2.0-2.3 A resolution
Homo sapiens
Engineering
Protein Variants
Commentary
Organism
V309F
replacement of one of the residues delineating this site by a phenylalanine completely abolishes the enzyme's substrate inhibition, but the catalytic efficiency of the mutated enzyme is similar to that of the wild-type h5beta-red enzyme
Homo sapiens
Y132F
replacement of one of the residues delineating this site by a phenylalanine completely abolishes the enzyme's substrate inhibition, but the catalytic efficiency of the mutated enzyme is similar to that of the wild-type h5beta-red enzyme
Homo sapiens
Inhibitors
Inhibitors
Commentary
Organism
Structure
androstenedione
the enzyme is rapidly inhibited by the substrate once its concentration reaches 2times the Km value. Androstenedione completely impedes the passage of another substrate molecule toward the catalytic site
Homo sapiens
additional information
structural features of substrate inhibition of h5beta-red by C19- and C21-steroids, overview
Homo sapiens
progesterone
the enzyme is rapidly inhibited by the substrate once its concentration reaches 2times the Km value
Homo sapiens
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
Michaelis-Menten kinetics for the reduction of androstenedione, overview
Homo sapiens
0.00037
-
androstenedione
pH 7.4, 37°C, wild-type enzyme
Homo sapiens
0.00094
-
androstenedione
pH 7.4, 37°C, mutant Y132F
Homo sapiens
0.01629
-
androstenedione
pH 7.4, 37°C, mutant V309F
Homo sapiens
Organism
Organism
UniProt
Commentary
Textmining
Homo sapiens
P51857
-
-
Purification (Commentary)
Purification (Commentary)
Organism
recombinant GST-tagged enzyme from Escherichia coli by glutathione affinity and anion exchange chromatography, and gel filtration
Homo sapiens
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
7alpha,12alpha-dihydroxy-4-cholesten-3-one + NADPH + H+
-
702225
Homo sapiens
?
-
-
-
?
7alpha-hydroxy-4-cholesten-3-one + NADPH + H+
-
702225
Homo sapiens
?
-
-
-
?
androstenedione + NADPH + H+
-
702225
Homo sapiens
?
-
-
-
?
additional information
the large steroid-binding site of this enzyme also contains a subsite in which the androstenedione molecule is bound, steroid-binding cavity structure of h5 beta-red, structure comparison
702225
Homo sapiens
?
-
-
-
?
progesterone + NADPH + H+
-
702225
Homo sapiens
?
-
-
-
?
Subunits
Subunits
Commentary
Organism
More
steroid-binding cavity structure of h5 beta-red, structure comparison
Homo sapiens
Synonyms
Synonyms
Commentary
Organism
AKR1D1
-
Homo sapiens
DELTA4-3-ketosteroid 5beta-reductase
-
Homo sapiens
h5beta-red
-
Homo sapiens
h5beta-reductase
-
Homo sapiens
More
human 5beta-red belongs to the aldo-keto reductase, AKR, superfamily and is the first member of the 1D subfamily, AKR1D1
Homo sapiens
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Homo sapiens
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.013
-
androstenedione
pH 7.4, 37°C, wild-type enzyme
Homo sapiens
0.0405
-
androstenedione
pH 7.4, 37°C, mutant Y132F
Homo sapiens
0.0425
-
androstenedione
pH 7.4, 37°C, mutant V309F
Homo sapiens
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.3
-
assay at
Homo sapiens
Cofactor
Cofactor
Commentary
Organism
Structure
NADPH
-
Homo sapiens
Cloned(Commentary) (protein specific)
Commentary
Organism
expression of GST-tagged enzyme in Escherichia coli
Homo sapiens
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADPH
-
Homo sapiens
Crystallization (Commentary) (protein specific)
Crystallization
Organism
purifed recombinant h5beta-red in ternary complex with NADPH and androstenedione, hanging-drop vapor diffusion technique, 2:1 v/v ratio of protein and well solution, about 5 days, X-ray diffraction structure determination and analysis at 2.0-2.3 A resolution
Homo sapiens
Engineering (protein specific)
Protein Variants
Commentary
Organism
V309F
replacement of one of the residues delineating this site by a phenylalanine completely abolishes the enzyme's substrate inhibition, but the catalytic efficiency of the mutated enzyme is similar to that of the wild-type h5beta-red enzyme
Homo sapiens
Y132F
replacement of one of the residues delineating this site by a phenylalanine completely abolishes the enzyme's substrate inhibition, but the catalytic efficiency of the mutated enzyme is similar to that of the wild-type h5beta-red enzyme
Homo sapiens
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
androstenedione
the enzyme is rapidly inhibited by the substrate once its concentration reaches 2times the Km value. Androstenedione completely impedes the passage of another substrate molecule toward the catalytic site
Homo sapiens
additional information
structural features of substrate inhibition of h5beta-red by C19- and C21-steroids, overview
Homo sapiens
progesterone
the enzyme is rapidly inhibited by the substrate once its concentration reaches 2times the Km value
Homo sapiens
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
Michaelis-Menten kinetics for the reduction of androstenedione, overview
Homo sapiens
0.00037
-
androstenedione
pH 7.4, 37°C, wild-type enzyme
Homo sapiens
0.00094
-
androstenedione
pH 7.4, 37°C, mutant Y132F
Homo sapiens
0.01629
-
androstenedione
pH 7.4, 37°C, mutant V309F
Homo sapiens
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant GST-tagged enzyme from Escherichia coli by glutathione affinity and anion exchange chromatography, and gel filtration
Homo sapiens
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
7alpha,12alpha-dihydroxy-4-cholesten-3-one + NADPH + H+
-
702225
Homo sapiens
?
-
-
-
?
7alpha-hydroxy-4-cholesten-3-one + NADPH + H+
-
702225
Homo sapiens
?
-
-
-
?
androstenedione + NADPH + H+
-
702225
Homo sapiens
?
-
-
-
?
additional information
the large steroid-binding site of this enzyme also contains a subsite in which the androstenedione molecule is bound, steroid-binding cavity structure of h5 beta-red, structure comparison
702225
Homo sapiens
?
-
-
-
?
progesterone + NADPH + H+
-
702225
Homo sapiens
?
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
More
steroid-binding cavity structure of h5 beta-red, structure comparison
Homo sapiens
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Homo sapiens
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.013
-
androstenedione
pH 7.4, 37°C, wild-type enzyme
Homo sapiens
0.0405
-
androstenedione
pH 7.4, 37°C, mutant Y132F
Homo sapiens
0.0425
-
androstenedione
pH 7.4, 37°C, mutant V309F
Homo sapiens
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.3
-
assay at
Homo sapiens
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
2.609
-
androstenedione
pH 7.4, 37°C, mutant V309F
Homo sapiens
35.13
-
androstenedione
pH 7.4, 37°C, wild-type enzyme
Homo sapiens
43.08
-
androstenedione
pH 7.4, 37°C, mutant Y132F
Homo sapiens
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
2.609
-
androstenedione
pH 7.4, 37°C, mutant V309F
Homo sapiens
35.13
-
androstenedione
pH 7.4, 37°C, wild-type enzyme
Homo sapiens
43.08
-
androstenedione
pH 7.4, 37°C, mutant Y132F
Homo sapiens
Other publictions for EC 1.3.1.3
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
Synonyms
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)
726120
Bauer
Vein patterning 1-encoded prog ...
Digitalis lanata, Arabidopsis thaliana
Phytochemistry
77
53-59
2012
-
-
2
1
15
-
-
12
-
-
-
4
-
2
-
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1
-
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4
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4
2
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12
2
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2
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2
2
1
15
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12
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4
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1
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4
-
2
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12
2
-
-
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-
4
4
-
12
12
724713
Mindnich
The effect of disease associat ...
Homo sapiens
Chem. Biol. Interact.
191
250-254
2011
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-
1
-
5
-
-
-
-
-
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3
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5
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5
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3
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3
3
-
-
-
726492
Chen
Substrate specificity and inhi ...
Homo sapiens
Steroids
76
484-490
2011
-
-
-
-
-
-
6
11
-
-
-
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3
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12
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3
1
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6
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11
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12
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1
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11
1
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2
2
-
11
11
725399
Drury
Characterization of disease-re ...
Homo sapiens
J. Biol. Chem.
285
24529-24537
2010
-
-
2
-
10
-
1
9
-
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4
-
5
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1
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5
1
3
1
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8
1
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1
2
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2
1
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10
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2
2
9
-
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4
-
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1
-
-
-
-
5
1
1
-
-
8
1
-
-
-
-
1
1
-
8
8
725633
McNeilly
Bile acids modulate glucocorti ...
Rattus norvegicus
J. Hepatol.
52
705-711
2010
-
1
-
-
-
-
1
-
1
-
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1
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1
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1
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-
1
-
-
1
-
-
697264
Di Costanzo
Aldo-keto reductases in which ...
Digitalis lanata
Chem. Biol. Interact.
178
127-133
2009
-
-
-
1
-
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-
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4
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3
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4
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4
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1
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1
1
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4
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4
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704908
Ueki
SRD5B1 gene analysis needed fo ...
Homo sapiens
J. Gastroenterol. Hepatol.
24
776-785
2009
-
-
1
-
2
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-
-
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1
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1
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1
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705710
Di Costanzo
Structure and catalytic mechan ...
Homo sapiens
Mol. Cell. Endocrinol.
301
191-198
2009
-
-
-
1
1
-
-
-
-
-
-
4
-
4
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2
-
1
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5
-
3
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1
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1
1
1
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4
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1
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5
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685271
Faucher
The crystal structure of human ...
Homo sapiens
Biochemistry
47
8261-8270
2008
-
-
1
1
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1
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3
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1
1
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1
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3
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687723
Di Costanzo
Crystal structure of human liv ...
Homo sapiens
J. Biol. Chem.
283
16830-16839
2008
-
-
1
1
2
-
1
1
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3
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1
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2
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3
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3
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1
1
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1
1
1
2
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1
1
1
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1
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2
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3
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698762
Thorn
The crystal structure of proge ...
Digitalis lanata
J. Biol. Chem.
283
17260-17269
2008
-
-
1
1
2
-
-
1
-
-
-
-
-
8
-
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1
-
-
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1
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1
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2
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1
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1
1
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1
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1
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702225
Faucher
Crystal structures of human De ...
Homo sapiens
Biochemistry
47
13537-13546
2008
-
-
1
1
2
-
3
4
-
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-
6
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1
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5
1
5
1
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3
1
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1
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1
1
1
2
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3
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4
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1
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5
1
1
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3
1
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-
-
-
-
-
-
3
3
706774
Palermo
Human Delta4-3-oxosteroid 5bet ...
Homo sapiens
Steroids
73
417-423
2008
-
-
-
-
1
-
-
-
-
-
-
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-
4
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1
1
-
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-
671346
Gavidia
Plant progesterone 5beta-reduc ...
Digitalis purpurea
Phytochemistry
68
853-864
2007
-
1
1
-
-
-
-
2
-
-
2
-
-
12
-
-
1
-
-
5
-
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2
1
2
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1
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1
1
1
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2
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1
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5
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2
1
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671101
Egerer-Sieber
Crystallization and preliminar ...
Digitalis lanata
Acta Crystallogr. Sect. F
62
186-188
2006
-
1
1
1
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7
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1
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676376
Herl
Molecular cloning and heterolo ...
Digitalis lanata
Phytochemistry
67
225-231
2006
-
1
1
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-
5
-
-
1
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-
11
-
-
1
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1
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6
1
2
1
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1
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