BRENDA - Enzyme Database show
show all sequences of 1.1.1.270

Characterization of rabbit aldose reductase-like protein with 3beta-hydroxysteroid dehydrogenase activity

Endo, S.; Matsunaga, T.; Kumada, S.; Fujimoto, A.; Ohno, S.; El-Kabbani, O.; Hu, D.; Toyooka, N.; Mano, J.; Tajima, K.; Hara, A.; Arch. Biochem. Biophys. 527, 23-30 (2012)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
DNA and amino acid sequence determination and analysis, expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3) pLysS
Oryctolagus cuniculus
Engineering
Amino acid exchange
Commentary
Organism
F303Q
site-directed mutagenesis, the enzyme shows reduced 3-ketoreductase activity compared to the wild-type enzyme
Oryctolagus cuniculus
F303Q/M304S
site-directed mutagenesis, the enzyme shows reduced 3-ketoreductase activity compared to the wild-type enzyme. The double mutation impairs the affinity and catalytic efficiency, although it did not affect the stereospecific reduction of the two 3-ketosteroids into the corresponding 3beta-hydroxysteroids
Oryctolagus cuniculus
L116F
site-directed mutagenesis
Oryctolagus cuniculus
M304S
site-directed mutagenesis, the enzyme shows reduced 3-ketoreductase activity compared to the wild-type enzyme. The M304S mutation causes a 4fold increase in the Km value for pyridine-3-aldehyde
Oryctolagus cuniculus
Inhibitors
Inhibitors
Commentary
Organism
Structure
(Z)-2-(4-methoxyphenylimino)-7-hydroxy-N-(pyridin-2-yl)-2H-chromene-3-carboxamide
noncompetitive in the reduction reaction, competitive in the oxidation reaction
Oryctolagus cuniculus
3-(4-hydroxy-2-methoxyphenyl)acrylic acid 3-(3-hydroxyphenyl)propyl ester
uncompetitive in the reduction reaction, competitive in the oxidation reaction
Oryctolagus cuniculus
AL1567
-
Oryctolagus cuniculus
bisdemethoxycurcumin
-
Oryctolagus cuniculus
diethylstilbestrol
-
Oryctolagus cuniculus
Diphenic acid
competitive in the oxidation reaction
Oryctolagus cuniculus
epalrestat
-
Oryctolagus cuniculus
minalrestat
competitive in the oxidation reaction
Oryctolagus cuniculus
oleanolic acid
competitive in the oxidation reaction
Oryctolagus cuniculus
quercetin
-
Oryctolagus cuniculus
sorbinil
-
Oryctolagus cuniculus
sulindac
-
Oryctolagus cuniculus
Tolrestat
competitive in the oxidation reaction
Oryctolagus cuniculus
zopolrestat
-
Oryctolagus cuniculus
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.001
-
NADPH
pH 7.4, 25°C, wild-type enzyme
Oryctolagus cuniculus
0.0023
-
5beta-pregnane-21-ol-3,20-dione
pH 7.4, 25°C, mutant L116F
Oryctolagus cuniculus
0.0024
-
5beta-pregnane-21-ol-3,20-dione
pH 7.4, 25°C, wild-type enzyme
Oryctolagus cuniculus
0.0035
-
5beta-dihydrotestosterone
pH 7.4, 25°C, wild-type enzyme
Oryctolagus cuniculus
0.0072
-
5beta-dihydrotestosterone
pH 7.4, 25°C, mutant L116F
Oryctolagus cuniculus
0.011
-
Pyridine-3-aldehyde
pH 7.4, 25°C, wild-type enzyme and mutant F303Q
Oryctolagus cuniculus
0.013
-
5beta-pregnane-21-ol-3,20-dione
pH 7.4, 25°C, mutant F303Q
Oryctolagus cuniculus
0.017
-
5beta-dihydrotestosterone
pH 7.4, 25°C, mutant F303Q
Oryctolagus cuniculus
0.02
-
5beta-dihydrotestosterone
pH 7.4, 25°C, mutant M304S
Oryctolagus cuniculus
0.022
-
Pyridine-3-aldehyde
pH 7.4, 25°C, mutant L116F
Oryctolagus cuniculus
0.023
-
5beta-pregnane-21-ol-3,20-dione
pH 7.4, 25°C, mutant M304S
Oryctolagus cuniculus
0.039
-
5beta-dihydrotestosterone
pH 7.4, 25°C, mutant F303Q/M304S
Oryctolagus cuniculus
0.039
-
Pyridine-3-aldehyde
pH 7.4, 25°C, mutant M304S
Oryctolagus cuniculus
0.048
-
Pyridine-3-aldehyde
pH 7.4, 25°C, mutant F303Q/M304S
Oryctolagus cuniculus
0.05
-
5beta-pregnane-21-ol-3,20-dione
pH 7.4, 25°C, mutant F303Q/M304S
Oryctolagus cuniculus
0.18
-
methylglyoxal
pH 7.4, 25°C, mutant L116F
Oryctolagus cuniculus
0.209
-
methylglyoxal
pH 7.4, 25°C, mutant M304S
Oryctolagus cuniculus
0.222
-
methylglyoxal
pH 7.4, 25°C, wild-type enzyme
Oryctolagus cuniculus
0.25
-
methylglyoxal
pH 7.4, 25°C, mutant F303Q/M304S
Oryctolagus cuniculus
0.253
-
methylglyoxal
pH 7.4, 25°C, mutant F303Q
Oryctolagus cuniculus
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
cytosol
-
Oryctolagus cuniculus
5829
-
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
35000
-
native enzyme, gel filtration
Oryctolagus cuniculus
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Oryctolagus cuniculus
the enzyme, termed AKR1B19, acts not only as a reductase for reactive carbonyl compounds derived from lipid peroxidation like AR-like proteins of other species, but also as a superior reductive 3beta-HSD for 3-keto-5alpha/beta-dihydro-C19/C21/C24-steroids
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Oryctolagus cuniculus
-
-
-
Purification (Commentary)
Commentary
Organism
native enzyme from lungs by ammonium sufate fractionation, gel filtration, and anion exchange chromatography, recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 (DE3) pLysS by nickel affinity chromatography and ultrafiltration
Oryctolagus cuniculus
Source Tissue
Source Tissue
Commentary
Organism
Textmining
adrenal gland
-
Oryctolagus cuniculus
-
colon
-
Oryctolagus cuniculus
-
lung
-
Oryctolagus cuniculus
-
additional information
the enzyme expression occurs in all rabbit tissues, although its expression levels in the renal cortex, adrenal gland, small intestine and colon are high
Oryctolagus cuniculus
-
renal cortex
-
Oryctolagus cuniculus
-
small intestine
-
Oryctolagus cuniculus
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
5alpha-androstan-3,17-dione + NADPH + H+
-
724124
Oryctolagus cuniculus
5alpha-androstan-3beta-ol-17-one + NADP+
-
-
-
r
5alpha-dihydrotestosterone + NADPH + H+
-
724124
Oryctolagus cuniculus
3beta,17beta-dihydroxy-5alpha-androstane + NADP+
-
-
-
r
5alpha-pregnan-3,20-dione + NADPH + H+
-
724124
Oryctolagus cuniculus
5alpha-pregnane-3beta-ol-20-one + NADP+
-
-
-
r
5alpha-pregnane-21-ol-3,20-dione + NADPH + H+
-
724124
Oryctolagus cuniculus
5alpha-pregnane-3beta,21-diol-20-one + NADP+
-
-
-
r
5beta-androstan-3,17-dione + NADPH + H+
-
724124
Oryctolagus cuniculus
5beta-androstan-3beta-ol-17-one + NADP+
-
-
-
r
5beta-androstan-3beta-ol-17-one + NADP+
-
724124
Oryctolagus cuniculus
5beta-androstan-3,17-dione + NADPH + H+
-
-
-
r
5beta-androstane-3beta,17beta-diol + NADP+
-
724124
Oryctolagus cuniculus
5beta-androstane-17beta-ol-3-one + NADPH + H+
-
-
-
r
5beta-cholanic acid-3,7-dione + NADPH + H+
-
724124
Oryctolagus cuniculus
5beta-cholanic acid-3beta-ol-7-one + NADP+
-
-
-
r
5beta-dihydrocorticosterone + NADPH + H+
-
724124
Oryctolagus cuniculus
(3beta,5beta,11beta)-3,11,21-trihydroxypregnan-20-one + NADP+
-
-
-
r
5beta-dihydrocortisone + NADPH + H+
-
724124
Oryctolagus cuniculus
?
-
-
-
r
5beta-dihydrotestosterone + NADPH + H+
-
724124
Oryctolagus cuniculus
3beta,17beta-dihydroxy-5beta-androstane + NADP+
-
-
-
r
5beta-hydroxy-5beta cholanic acid + NADP+
-
724124
Oryctolagus cuniculus
3-oxo-5-beta-cholanic acid + NADPH + H+
-
-
-
r
5beta-pregnan-3,20-dione + NADPH + H+
-
724124
Oryctolagus cuniculus
5beta-pregnane-3beta-ol-20-one + NADP+
-
-
-
r
5beta-pregnane-20-ol-3-one + NADPH + H+
-
724124
Oryctolagus cuniculus
5beta-pregnane-3beta,20-diol + NADP+
-
-
-
r
5beta-pregnane-21-ol-3,20-dione + NADPH + H+
-
724124
Oryctolagus cuniculus
5beta-pregnane-3beta,21-diol-20-one + NADP+
-
-
-
r
5beta-pregnane-3beta,20alpha-diol + NADP+
-
724124
Oryctolagus cuniculus
5beta-pregnane-20alpha-ol-3-one + NADPH + H+
-
-
-
r
5beta-pregnane-3beta,20beta-diol + NADP+
-
724124
Oryctolagus cuniculus
5beta-pregnane-20beta-ol-3-one + NADPH + H+
-
-
-
r
5beta-pregnane-3beta,21-diol-20-one + NADP+
-
724124
Oryctolagus cuniculus
5beta-pregnane-21-ol-3,20-dione + NADPH + H+
-
-
-
r
5beta-pregnane-3beta-ol-20-one + NADP+
-
724124
Oryctolagus cuniculus
5beta-pregnan-3,20-dione + NADPH + H+
-
-
-
r
dehydrolithocholic acid + NADPH + H+
-
724124
Oryctolagus cuniculus
?
-
-
-
r
farnesol + NADP+
-
724124
Oryctolagus cuniculus
farnesal + NADPH + H+
-
-
-
?
geranylgeraniol + NADP+
-
724124
Oryctolagus cuniculus
geranylgeranial + NADPH + H+
-
-
-
?
isolithocholic acid + NADP+
-
724124
Oryctolagus cuniculus
? + NADPH + H+
-
-
-
r
methylglyoxal + NADP+
-
724124
Oryctolagus cuniculus
? + NADPH + H+
-
-
-
?
additional information
the enzyme, termed AKR1B19, acts not only as a reductase for reactive carbonyl compounds derived from lipid peroxidation like AR-like proteins of other species, but also as a superior reductive 3beta-HSD for 3-keto-5alpha/beta-dihydro-C19/C21/C24-steroids
724124
Oryctolagus cuniculus
?
-
-
-
-
additional information
substrate specificity of the bifunctional enzyme, for carbonyl compounds and steroids, overview. No reductase activity is observed for 17- and 20-ketosteroids, DELTA4-3-ketosteroids (testosterone, 4-androstene-3,17-dione and progesterone), and prostaglandins (D2, E2, and A1). In the reverse reaction, the enzyme oxidizes 3beta-hydroxy-5alpha/beta-dihydrosteroids, but shows no significant dehydrogenase activity for DELTA5-3beta-hydroxysteroids (dehydroepiandrosterone, pregnenolone, and 5-pregnene-3beta,20alpha-diol) and 3alpha-hydroxysteroids (5alpha/beta-androstan-3alpha-ol-17-ones, 5alpha/beta-androstane-3alpha,17beta-diols, 5alpha/beta-pregnan-3alpha-ol-20-ones and lithocholic acid). The reactivity towards all-trans-retinal of AKR1B19 is low
724124
Oryctolagus cuniculus
?
-
-
-
-
pyridine-3-aldehyde + NADP+
-
724124
Oryctolagus cuniculus
pyridin-3-ylmethanol + NADPH + H+
-
-
-
?
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
-
assay at
Oryctolagus cuniculus
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.02
-
5beta-dihydrotestosterone
pH 7.4, 25°C, mutant F303Q/M304S
Oryctolagus cuniculus
0.023
-
5beta-pregnane-21-ol-3,20-dione
pH 7.4, 25°C, mutant F303Q/M304S
Oryctolagus cuniculus
0.042
-
5beta-pregnane-21-ol-3,20-dione
pH 7.4, 25°C, mutant M304S
Oryctolagus cuniculus
0.047
-
5beta-dihydrotestosterone
pH 7.4, 25°C, mutant M304S
Oryctolagus cuniculus
0.062
-
5beta-pregnane-21-ol-3,20-dione
pH 7.4, 25°C, mutant F303Q
Oryctolagus cuniculus
0.063
-
5beta-pregnane-21-ol-3,20-dione
pH 7.4, 25°C, mutant L116F
Oryctolagus cuniculus
0.08
-
5beta-dihydrotestosterone
pH 7.4, 25°C, mutant F303Q
Oryctolagus cuniculus
0.092
-
5beta-pregnane-21-ol-3,20-dione
pH 7.4, 25°C, wild-type enzyme
Oryctolagus cuniculus
0.107
-
5beta-dihydrotestosterone
pH 7.4, 25°C, mutant L116F
Oryctolagus cuniculus
0.113
-
5beta-dihydrotestosterone
pH 7.4, 25°C, wild-type enzyme
Oryctolagus cuniculus
0.3
-
methylglyoxal
pH 7.4, 25°C, wild-type enzyme
Oryctolagus cuniculus
0.32
-
methylglyoxal
pH 7.4, 25°C, mutant L116F
Oryctolagus cuniculus
0.37
-
methylglyoxal
pH 7.4, 25°C, mutant M304S
Oryctolagus cuniculus
0.4
-
methylglyoxal
pH 7.4, 25°C, mutant F303Q/M304S
Oryctolagus cuniculus
0.58
-
methylglyoxal
pH 7.4, 25°C, mutant F303Q
Oryctolagus cuniculus
0.6
-
Pyridine-3-aldehyde
pH 7.4, 25°C, mutant L116F
Oryctolagus cuniculus
0.72
-
Pyridine-3-aldehyde
pH 7.4, 25°C, wild-type enzyme
Oryctolagus cuniculus
0.73
-
NADPH
pH 7.4, 25°C, wild-type enzyme
Oryctolagus cuniculus
0.78
-
Pyridine-3-aldehyde
pH 7.4, 25°C, mutant M304S
Oryctolagus cuniculus
0.87
-
Pyridine-3-aldehyde
pH 7.4, 25°C, mutant F303Q
Oryctolagus cuniculus
1.2
-
Pyridine-3-aldehyde
pH 7.4, 25°C, mutant F303Q/M304S
Oryctolagus cuniculus
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.2
6.4
-
Oryctolagus cuniculus
Cofactor
Cofactor
Commentary
Organism
Structure
NADH
the NADH-linked reductase activity is only 18% of the NADPH-linked activity
Oryctolagus cuniculus
NADPH
AKR1B19 shows high coenzyme preference to NADPH
Oryctolagus cuniculus
IC50 Value
IC50 Value
IC50 Value Maximum
Commentary
Organism
Inhibitor
Structure
0.000008
-
pH 7.4, 25°C, wild-type enzyme
Oryctolagus cuniculus
(Z)-2-(4-methoxyphenylimino)-7-hydroxy-N-(pyridin-2-yl)-2H-chromene-3-carboxamide
0.000043
-
pH 7.4, 25°C, wild-type enzyme
Oryctolagus cuniculus
minalrestat
0.00006
-
pH 7.4, 25°C, wild-type enzyme
Oryctolagus cuniculus
3-(4-hydroxy-2-methoxyphenyl)acrylic acid 3-(3-hydroxyphenyl)propyl ester
0.00016
-
pH 7.4, 25°C, wild-type enzyme
Oryctolagus cuniculus
Tolrestat
0.0004
-
pH 7.4, 25°C, wild-type enzyme
Oryctolagus cuniculus
oleanolic acid
0.0006
-
pH 7.4, 25°C, wild-type enzyme
Oryctolagus cuniculus
bisdemethoxycurcumin
0.00086
-
pH 7.4, 25°C, wild-type enzyme
Oryctolagus cuniculus
sulindac
0.0012
-
pH 7.4, 25°C, wild-type enzyme
Oryctolagus cuniculus
zopolrestat
0.0015
-
pH 7.4, 25°C, wild-type enzyme
Oryctolagus cuniculus
epalrestat
0.0015
-
pH 7.4, 25°C, wild-type enzyme
Oryctolagus cuniculus
quercetin
0.0017
-
pH 7.4, 25°C, wild-type enzyme
Oryctolagus cuniculus
AL1567
0.0028
-
pH 7.4, 25°C, wild-type enzyme
Oryctolagus cuniculus
diethylstilbestrol
0.0053
-
pH 7.4, 25°C, wild-type enzyme
Oryctolagus cuniculus
sorbinil
0.26
-
pH 7.4, 25°C, wild-type enzyme
Oryctolagus cuniculus
Diphenic acid
Cloned(Commentary) (protein specific)
Commentary
Organism
DNA and amino acid sequence determination and analysis, expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3) pLysS
Oryctolagus cuniculus
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADH
the NADH-linked reductase activity is only 18% of the NADPH-linked activity
Oryctolagus cuniculus
NADPH
AKR1B19 shows high coenzyme preference to NADPH
Oryctolagus cuniculus
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
F303Q
site-directed mutagenesis, the enzyme shows reduced 3-ketoreductase activity compared to the wild-type enzyme
Oryctolagus cuniculus
F303Q/M304S
site-directed mutagenesis, the enzyme shows reduced 3-ketoreductase activity compared to the wild-type enzyme. The double mutation impairs the affinity and catalytic efficiency, although it did not affect the stereospecific reduction of the two 3-ketosteroids into the corresponding 3beta-hydroxysteroids
Oryctolagus cuniculus
L116F
site-directed mutagenesis
Oryctolagus cuniculus
M304S
site-directed mutagenesis, the enzyme shows reduced 3-ketoreductase activity compared to the wild-type enzyme. The M304S mutation causes a 4fold increase in the Km value for pyridine-3-aldehyde
Oryctolagus cuniculus
IC50 Value (protein specific)
IC50 Value
IC50 Value Maximum
Commentary
Organism
Inhibitor
Structure
0.000008
-
pH 7.4, 25°C, wild-type enzyme
Oryctolagus cuniculus
(Z)-2-(4-methoxyphenylimino)-7-hydroxy-N-(pyridin-2-yl)-2H-chromene-3-carboxamide
0.000043
-
pH 7.4, 25°C, wild-type enzyme
Oryctolagus cuniculus
minalrestat
0.00006
-
pH 7.4, 25°C, wild-type enzyme
Oryctolagus cuniculus
3-(4-hydroxy-2-methoxyphenyl)acrylic acid 3-(3-hydroxyphenyl)propyl ester
0.00016
-
pH 7.4, 25°C, wild-type enzyme
Oryctolagus cuniculus
Tolrestat
0.0004
-
pH 7.4, 25°C, wild-type enzyme
Oryctolagus cuniculus
oleanolic acid
0.0006
-
pH 7.4, 25°C, wild-type enzyme
Oryctolagus cuniculus
bisdemethoxycurcumin
0.00086
-
pH 7.4, 25°C, wild-type enzyme
Oryctolagus cuniculus
sulindac
0.0012
-
pH 7.4, 25°C, wild-type enzyme
Oryctolagus cuniculus
zopolrestat
0.0015
-
pH 7.4, 25°C, wild-type enzyme
Oryctolagus cuniculus
epalrestat
0.0015
-
pH 7.4, 25°C, wild-type enzyme
Oryctolagus cuniculus
quercetin
0.0017
-
pH 7.4, 25°C, wild-type enzyme
Oryctolagus cuniculus
AL1567
0.0028
-
pH 7.4, 25°C, wild-type enzyme
Oryctolagus cuniculus
diethylstilbestrol
0.0053
-
pH 7.4, 25°C, wild-type enzyme
Oryctolagus cuniculus
sorbinil
0.26
-
pH 7.4, 25°C, wild-type enzyme
Oryctolagus cuniculus
Diphenic acid
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
(Z)-2-(4-methoxyphenylimino)-7-hydroxy-N-(pyridin-2-yl)-2H-chromene-3-carboxamide
noncompetitive in the reduction reaction, competitive in the oxidation reaction
Oryctolagus cuniculus
3-(4-hydroxy-2-methoxyphenyl)acrylic acid 3-(3-hydroxyphenyl)propyl ester
uncompetitive in the reduction reaction, competitive in the oxidation reaction
Oryctolagus cuniculus
AL1567
-
Oryctolagus cuniculus
bisdemethoxycurcumin
-
Oryctolagus cuniculus
diethylstilbestrol
-
Oryctolagus cuniculus
Diphenic acid
competitive in the oxidation reaction
Oryctolagus cuniculus
epalrestat
-
Oryctolagus cuniculus
minalrestat
competitive in the oxidation reaction
Oryctolagus cuniculus
oleanolic acid
competitive in the oxidation reaction
Oryctolagus cuniculus
quercetin
-
Oryctolagus cuniculus
sorbinil
-
Oryctolagus cuniculus
sulindac
-
Oryctolagus cuniculus
Tolrestat
competitive in the oxidation reaction
Oryctolagus cuniculus
zopolrestat
-
Oryctolagus cuniculus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.001
-
NADPH
pH 7.4, 25°C, wild-type enzyme
Oryctolagus cuniculus
0.0023
-
5beta-pregnane-21-ol-3,20-dione
pH 7.4, 25°C, mutant L116F
Oryctolagus cuniculus
0.0024
-
5beta-pregnane-21-ol-3,20-dione
pH 7.4, 25°C, wild-type enzyme
Oryctolagus cuniculus
0.0035
-
5beta-dihydrotestosterone
pH 7.4, 25°C, wild-type enzyme
Oryctolagus cuniculus
0.0072
-
5beta-dihydrotestosterone
pH 7.4, 25°C, mutant L116F
Oryctolagus cuniculus
0.011
-
Pyridine-3-aldehyde
pH 7.4, 25°C, wild-type enzyme and mutant F303Q
Oryctolagus cuniculus
0.013
-
5beta-pregnane-21-ol-3,20-dione
pH 7.4, 25°C, mutant F303Q
Oryctolagus cuniculus
0.017
-
5beta-dihydrotestosterone
pH 7.4, 25°C, mutant F303Q
Oryctolagus cuniculus
0.02
-
5beta-dihydrotestosterone
pH 7.4, 25°C, mutant M304S
Oryctolagus cuniculus
0.022
-
Pyridine-3-aldehyde
pH 7.4, 25°C, mutant L116F
Oryctolagus cuniculus
0.023
-
5beta-pregnane-21-ol-3,20-dione
pH 7.4, 25°C, mutant M304S
Oryctolagus cuniculus
0.039
-
5beta-dihydrotestosterone
pH 7.4, 25°C, mutant F303Q/M304S
Oryctolagus cuniculus
0.039
-
Pyridine-3-aldehyde
pH 7.4, 25°C, mutant M304S
Oryctolagus cuniculus
0.048
-
Pyridine-3-aldehyde
pH 7.4, 25°C, mutant F303Q/M304S
Oryctolagus cuniculus
0.05
-
5beta-pregnane-21-ol-3,20-dione
pH 7.4, 25°C, mutant F303Q/M304S
Oryctolagus cuniculus
0.18
-
methylglyoxal
pH 7.4, 25°C, mutant L116F
Oryctolagus cuniculus
0.209
-
methylglyoxal
pH 7.4, 25°C, mutant M304S
Oryctolagus cuniculus
0.222
-
methylglyoxal
pH 7.4, 25°C, wild-type enzyme
Oryctolagus cuniculus
0.25
-
methylglyoxal
pH 7.4, 25°C, mutant F303Q/M304S
Oryctolagus cuniculus
0.253
-
methylglyoxal
pH 7.4, 25°C, mutant F303Q
Oryctolagus cuniculus
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
cytosol
-
Oryctolagus cuniculus
5829
-
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
35000
-
native enzyme, gel filtration
Oryctolagus cuniculus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Oryctolagus cuniculus
the enzyme, termed AKR1B19, acts not only as a reductase for reactive carbonyl compounds derived from lipid peroxidation like AR-like proteins of other species, but also as a superior reductive 3beta-HSD for 3-keto-5alpha/beta-dihydro-C19/C21/C24-steroids
?
-
-
-
Purification (Commentary) (protein specific)
Commentary
Organism
native enzyme from lungs by ammonium sufate fractionation, gel filtration, and anion exchange chromatography, recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 (DE3) pLysS by nickel affinity chromatography and ultrafiltration
Oryctolagus cuniculus
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
adrenal gland
-
Oryctolagus cuniculus
-
colon
-
Oryctolagus cuniculus
-
lung
-
Oryctolagus cuniculus
-
additional information
the enzyme expression occurs in all rabbit tissues, although its expression levels in the renal cortex, adrenal gland, small intestine and colon are high
Oryctolagus cuniculus
-
renal cortex
-
Oryctolagus cuniculus
-
small intestine
-
Oryctolagus cuniculus
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
5alpha-androstan-3,17-dione + NADPH + H+
-
724124
Oryctolagus cuniculus
5alpha-androstan-3beta-ol-17-one + NADP+
-
-
-
r
5alpha-dihydrotestosterone + NADPH + H+
-
724124
Oryctolagus cuniculus
3beta,17beta-dihydroxy-5alpha-androstane + NADP+
-
-
-
r
5alpha-pregnan-3,20-dione + NADPH + H+
-
724124
Oryctolagus cuniculus
5alpha-pregnane-3beta-ol-20-one + NADP+
-
-
-
r
5alpha-pregnane-21-ol-3,20-dione + NADPH + H+
-
724124
Oryctolagus cuniculus
5alpha-pregnane-3beta,21-diol-20-one + NADP+
-
-
-
r
5beta-androstan-3,17-dione + NADPH + H+
-
724124
Oryctolagus cuniculus
5beta-androstan-3beta-ol-17-one + NADP+
-
-
-
r
5beta-androstan-3beta-ol-17-one + NADP+
-
724124
Oryctolagus cuniculus
5beta-androstan-3,17-dione + NADPH + H+
-
-
-
r
5beta-androstane-3beta,17beta-diol + NADP+
-
724124
Oryctolagus cuniculus
5beta-androstane-17beta-ol-3-one + NADPH + H+
-
-
-
r
5beta-cholanic acid-3,7-dione + NADPH + H+
-
724124
Oryctolagus cuniculus
5beta-cholanic acid-3beta-ol-7-one + NADP+
-
-
-
r
5beta-dihydrocorticosterone + NADPH + H+
-
724124
Oryctolagus cuniculus
(3beta,5beta,11beta)-3,11,21-trihydroxypregnan-20-one + NADP+
-
-
-
r
5beta-dihydrocortisone + NADPH + H+
-
724124
Oryctolagus cuniculus
?
-
-
-
r
5beta-dihydrotestosterone + NADPH + H+
-
724124
Oryctolagus cuniculus
3beta,17beta-dihydroxy-5beta-androstane + NADP+
-
-
-
r
5beta-hydroxy-5beta cholanic acid + NADP+
-
724124
Oryctolagus cuniculus
3-oxo-5-beta-cholanic acid + NADPH + H+
-
-
-
r
5beta-pregnan-3,20-dione + NADPH + H+
-
724124
Oryctolagus cuniculus
5beta-pregnane-3beta-ol-20-one + NADP+
-
-
-
r
5beta-pregnane-20-ol-3-one + NADPH + H+
-
724124
Oryctolagus cuniculus
5beta-pregnane-3beta,20-diol + NADP+
-
-
-
r
5beta-pregnane-21-ol-3,20-dione + NADPH + H+
-
724124
Oryctolagus cuniculus
5beta-pregnane-3beta,21-diol-20-one + NADP+
-
-
-
r
5beta-pregnane-3beta,20alpha-diol + NADP+
-
724124
Oryctolagus cuniculus
5beta-pregnane-20alpha-ol-3-one + NADPH + H+
-
-
-
r
5beta-pregnane-3beta,20beta-diol + NADP+
-
724124
Oryctolagus cuniculus
5beta-pregnane-20beta-ol-3-one + NADPH + H+
-
-
-
r
5beta-pregnane-3beta,21-diol-20-one + NADP+
-
724124
Oryctolagus cuniculus
5beta-pregnane-21-ol-3,20-dione + NADPH + H+
-
-
-
r
5beta-pregnane-3beta-ol-20-one + NADP+
-
724124
Oryctolagus cuniculus
5beta-pregnan-3,20-dione + NADPH + H+
-
-
-
r
dehydrolithocholic acid + NADPH + H+
-
724124
Oryctolagus cuniculus
?
-
-
-
r
farnesol + NADP+
-
724124
Oryctolagus cuniculus
farnesal + NADPH + H+
-
-
-
?
geranylgeraniol + NADP+
-
724124
Oryctolagus cuniculus
geranylgeranial + NADPH + H+
-
-
-
?
isolithocholic acid + NADP+
-
724124
Oryctolagus cuniculus
? + NADPH + H+
-
-
-
r
methylglyoxal + NADP+
-
724124
Oryctolagus cuniculus
? + NADPH + H+
-
-
-
?
additional information
the enzyme, termed AKR1B19, acts not only as a reductase for reactive carbonyl compounds derived from lipid peroxidation like AR-like proteins of other species, but also as a superior reductive 3beta-HSD for 3-keto-5alpha/beta-dihydro-C19/C21/C24-steroids
724124
Oryctolagus cuniculus
?
-
-
-
-
additional information
substrate specificity of the bifunctional enzyme, for carbonyl compounds and steroids, overview. No reductase activity is observed for 17- and 20-ketosteroids, DELTA4-3-ketosteroids (testosterone, 4-androstene-3,17-dione and progesterone), and prostaglandins (D2, E2, and A1). In the reverse reaction, the enzyme oxidizes 3beta-hydroxy-5alpha/beta-dihydrosteroids, but shows no significant dehydrogenase activity for DELTA5-3beta-hydroxysteroids (dehydroepiandrosterone, pregnenolone, and 5-pregnene-3beta,20alpha-diol) and 3alpha-hydroxysteroids (5alpha/beta-androstan-3alpha-ol-17-ones, 5alpha/beta-androstane-3alpha,17beta-diols, 5alpha/beta-pregnan-3alpha-ol-20-ones and lithocholic acid). The reactivity towards all-trans-retinal of AKR1B19 is low
724124
Oryctolagus cuniculus
?
-
-
-
-
pyridine-3-aldehyde + NADP+
-
724124
Oryctolagus cuniculus
pyridin-3-ylmethanol + NADPH + H+
-
-
-
?
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
-
assay at
Oryctolagus cuniculus
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.02
-
5beta-dihydrotestosterone
pH 7.4, 25°C, mutant F303Q/M304S
Oryctolagus cuniculus
0.023
-
5beta-pregnane-21-ol-3,20-dione
pH 7.4, 25°C, mutant F303Q/M304S
Oryctolagus cuniculus
0.042
-
5beta-pregnane-21-ol-3,20-dione
pH 7.4, 25°C, mutant M304S
Oryctolagus cuniculus
0.047
-
5beta-dihydrotestosterone
pH 7.4, 25°C, mutant M304S
Oryctolagus cuniculus
0.062
-
5beta-pregnane-21-ol-3,20-dione
pH 7.4, 25°C, mutant F303Q
Oryctolagus cuniculus
0.063
-
5beta-pregnane-21-ol-3,20-dione
pH 7.4, 25°C, mutant L116F
Oryctolagus cuniculus
0.08
-
5beta-dihydrotestosterone
pH 7.4, 25°C, mutant F303Q
Oryctolagus cuniculus
0.092
-
5beta-pregnane-21-ol-3,20-dione
pH 7.4, 25°C, wild-type enzyme
Oryctolagus cuniculus
0.107
-
5beta-dihydrotestosterone
pH 7.4, 25°C, mutant L116F
Oryctolagus cuniculus
0.113
-
5beta-dihydrotestosterone
pH 7.4, 25°C, wild-type enzyme
Oryctolagus cuniculus
0.3
-
methylglyoxal
pH 7.4, 25°C, wild-type enzyme
Oryctolagus cuniculus
0.32
-
methylglyoxal
pH 7.4, 25°C, mutant L116F
Oryctolagus cuniculus
0.37
-
methylglyoxal
pH 7.4, 25°C, mutant M304S
Oryctolagus cuniculus
0.4
-
methylglyoxal
pH 7.4, 25°C, mutant F303Q/M304S
Oryctolagus cuniculus
0.58
-
methylglyoxal
pH 7.4, 25°C, mutant F303Q
Oryctolagus cuniculus
0.6
-
Pyridine-3-aldehyde
pH 7.4, 25°C, mutant L116F
Oryctolagus cuniculus
0.72
-
Pyridine-3-aldehyde
pH 7.4, 25°C, wild-type enzyme
Oryctolagus cuniculus
0.73
-
NADPH
pH 7.4, 25°C, wild-type enzyme
Oryctolagus cuniculus
0.78
-
Pyridine-3-aldehyde
pH 7.4, 25°C, mutant M304S
Oryctolagus cuniculus
0.87
-
Pyridine-3-aldehyde
pH 7.4, 25°C, mutant F303Q
Oryctolagus cuniculus
1.2
-
Pyridine-3-aldehyde
pH 7.4, 25°C, mutant F303Q/M304S
Oryctolagus cuniculus
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.2
6.4
-
Oryctolagus cuniculus
General Information
General Information
Commentary
Organism
evolution
the rabbit aldose reductase-like protein that shars an 86% sequence identity to human aldo-keto reductase (AKR) 1B10 and is assigned as AKR1B19 in the AKR superfamily. It is bifunctional and also acts as a 3-ketoreductase reducing 3-keto-5alpha/beta-dihydro-C19/C21/C24-steroids into the corresponding 3betahydroxysteroids
Oryctolagus cuniculus
malfunction
single and double mutations, F303Q, M304S and F303Q/M304S, significantly impair the 3-ketoreductase activity, suggesting that the two residues play critical roles in recognition of the steroidal substrate
Oryctolagus cuniculus
physiological function
the rabbit aldose reductase-like protein, assigned as AKR1B19, is bifunctional, it shows aldose reductase activity for various aldehydes and alpha-dicarbonyl compounds acting as a defense system against cytotoxic carbonyl compounds in rabbit tissues, and it also acts as a 3-ketoreductase reducing 3-keto-5alpha/beta-dihydro-C19/C21/C24-steroids into the corresponding 3beta-hydroxysteroids
Oryctolagus cuniculus
General Information (protein specific)
General Information
Commentary
Organism
evolution
the rabbit aldose reductase-like protein that shars an 86% sequence identity to human aldo-keto reductase (AKR) 1B10 and is assigned as AKR1B19 in the AKR superfamily. It is bifunctional and also acts as a 3-ketoreductase reducing 3-keto-5alpha/beta-dihydro-C19/C21/C24-steroids into the corresponding 3betahydroxysteroids
Oryctolagus cuniculus
malfunction
single and double mutations, F303Q, M304S and F303Q/M304S, significantly impair the 3-ketoreductase activity, suggesting that the two residues play critical roles in recognition of the steroidal substrate
Oryctolagus cuniculus
physiological function
the rabbit aldose reductase-like protein, assigned as AKR1B19, is bifunctional, it shows aldose reductase activity for various aldehydes and alpha-dicarbonyl compounds acting as a defense system against cytotoxic carbonyl compounds in rabbit tissues, and it also acts as a 3-ketoreductase reducing 3-keto-5alpha/beta-dihydro-C19/C21/C24-steroids into the corresponding 3beta-hydroxysteroids
Oryctolagus cuniculus
Other publictions for EC 1.1.1.270
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)
740936
Ferrante
4-Methylzymosterone and other ...
Saccharomyces cerevisiae
Lipids
51
1103-1113
2016
-
1
-
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3
-
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2
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-
741250
Chen
Metabolism of androstenone, 17 ...
Sus scrofa
PLoS ONE
10
e113194
2015
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-
-
-
-
-
1
-
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-
-
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1
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1
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1
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1
-
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1
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
726098
Debieu
Role of sterol 3-ketoreductase ...
Botrytis cinerea
Pest Manag. Sci.
69
642-651
2013
-
-
-
-
1
-
5
-
1
1
-
-
-
5
-
-
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-
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1
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3
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1
-
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1
-
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1
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1
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1
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5
-
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1
1
-
-
-
-
-
-
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1
-
-
3
-
1
-
-
-
1
-
-
-
-
2
2
-
-
-
740097
Layer
Characterization of a mutation ...
Mus musculus
Biochim. Biophys. Acta
1831
361-369
2013
-
-
-
-
-
-
-
-
-
-
-
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4
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-
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-
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1
1
-
-
-
724124
Endo
Characterization of rabbit ald ...
Oryctolagus cuniculus
Arch. Biochem. Biophys.
527
23-30
2012
-
-
1
-
4
-
14
20
1
-
1
1
-
3
-
-
1
-
-
6
-
-
27
-
1
-
-
21
1
-
-
2
-
-
14
-
-
1
2
-
4
-
14
14
-
20
1
-
1
1
-
-
-
1
-
6
-
-
27
-
1
-
-
21
1
-
-
-
-
3
3
-
-
-
702462
Taramino
Interactions of oxidosqualene ...
Saccharomyces cerevisiae
Biochim. Biophys. Acta
1801
156-162
2010
-
-
-
-
-
-
-
-
-
-
-
-
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3
-
-
-
-
-
-
-
-
-
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-
-
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-
-
-
-
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-
-
-
-
-
-
-
1
1
-
-
-
711300
Taramino
Divergent interactions involvi ...
Homo sapiens, Mus musculus
Biochim. Biophys. Acta
1801
1232-1237
2010
-
-
-
-
2
-
-
-
-
-
-
-
-
7
-
-
-
-
-
1
-
-
-
-
-
-
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-
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-
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2
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-
-
-
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1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
725813
Thomas
The functions of key residues ...
Homo sapiens
J. Steroid Biochem. Mol. Biol.
120
192-199
2010
-
1
1
-
6
-
1
-
-
-
-
-
-
2
-
-
1
-
-
6
-
-
7
-
1
-
-
-
1
-
-
2
4
-
-
-
1
1
2
-
6
-
-
1
4
-
-
-
-
-
-
-
-
1
-
6
-
-
7
-
1
-
-
-
1
-
-
-
-
3
3
-
-
-
673822
Tam
Activities of 3beta-HSD and ar ...
Taeniopygia guttata
Gen. Comp. Endocrinol.
150
26-33
2006
-
-
-
-
-
-
-
-
-
-
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3
-
1
-
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-
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5
-
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3
-
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2
-
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2
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3
-
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5
-
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3
-
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-
-
-
-
-
-
-
675595
Steckelbroeck
Tibolone metabolism in human l ...
Homo sapiens
J. Pharmacol. Exp. Ther.
316
1300-1309
2006
-
-
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