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(20S)-21-hydroxy-20-methylpregn-4-en-3-one + NADPH + H+
? + NADP+
-
-
-
?
1,4-androstadien-17beta-ol-3-one + NADPH + H+
?
-
-
-
-
?
11-deoxycortisol + NADPH
?
-
-
-
-
?
11beta,17alpha,21-trihydroxy-pregn-4-en-3,20-dione + NADPH
11beta,17alpha,21-trihydroxypregnan-3,20-dione + NADP+
17alpha,21-dihydroxy-pregn-4-en-3,20-dione + NADPH
17alpha,21-dihydroxy-pregnan-3,20-dione + NADP+
17alpha-hydroxyprogesterone + NADPH
?
-
-
-
-
?
17alpha-methylestr-4-en-3-one + NADPH
17alpha-methylestran-3-one + NADP+
17beta-hydroxyandrost-4-en-3-one + NADPH
17beta-hydroxy-5beta-androstan-3-one + NADP+
17beta-hydroxyestr-4-en-3-one + NADPH
17-hydroxyestran-3-one + NADP+
2-cyclohexen-1-one + NADPH + H+
? + NADP+
-
-
-
?
2-cyclohexen-1-one + NADPH + H+
cyclohexanone + NADP+
4-androstene-3,17-dione + NADPH
5beta-androstan-3,17-dione + NADP+
4-androstene-3,17-dione + NADPH + H+
5beta-androstan-3,15-dione + 3alpha-hydroxy-5beta-androstan-17-one + NADP+
-
-
-
?
4-androstene-3,17-dione + NADPH + H+
5beta-androstan-3,17-dione + NADP+
-
-
-
?
4-androstene-3,17-dione + NADPH + H+
?
-
-
-
-
?
4-cholesten-7alpha-ol-3-one + NADPH + H+
?
-
-
-
-
?
4-estren-17beta-ol-3-one + NADPH + H+
?
-
-
-
-
?
7alpha,12alpha-dihydroxy-4-cholesten-3-one + NADPH
7alpha,12alpha-dihydroxy-5-beta-cholestan-3-one + NADP+
-
-
-
-
?
7alpha,12alpha-dihydroxy-4-cholesten-3-one + NADPH + H+
?
-
-
-
?
7alpha,12beta-dihydroxy-4-cholesten-3-one + NADPH + H+
(5beta,7alpha,12beta)-7,12-dihydroxycholestan-3-one + NADP+
-
-
-
?
7alpha-hydroxy-4-cholesten + NADPH
7alpha-hydroxy-5beta-cholestan-3-one + NADP+
-
-
-
?
7alpha-hydroxy-4-cholesten-3-one + NADPH
(5beta,7alpha)-7-hydroxycholestan-3-one + NADP+
-
-
-
?
7alpha-hydroxy-4-cholesten-3-one + NADPH + H+
7alpha-hydroxy-5beta-cholestan-3-one + NADP+
-
-
-
-
r
7alpha-hydroxy-4-cholesten-3-one + NADPH + H+
?
-
-
-
?
aldosterone + NADPH + H+
?
-
-
-
-
?
androst-4-en-3,17-dione + NADPH
5beta-androstan-3,17-dione + NADP+
androstenedione + NADPH + H+
?
-
-
-
?
cholest-4-en-3-one + NADPH + H+
5beta-cholestan-3-one + NADP+
-
-
-
?
cholestenone + NADPH + H+
?
-
-
-
-
?
cortexone + NADPH
21-trihydroxy-5beta-pregnane-3,20-dione + NADP+
corticosterone + NADPH + H+
?
cortisol + NADPH
11beta,17,21-trihydroxy-5beta-pregnane-3,20-dione + NADP+
cortisol + NADPH + H+
11beta,17,21-trihydroxy-5beta-pregnane-3,20-dione + NADP+
-
-
-
?
cortisol + NADPH + H+
?
-
-
-
-
?
cortisone + NADPH + H+
17,21-dihydroxy-5beta-pregnane-3,11,20-trione + NADP+
cortisone + NADPH + H+
5beta-17,21dihydroxy-pregnan-3,11,20-trione + NADP+
cortisone + NADPH + H+
?
-
-
-
-
?
DELTA 4-cholestene-7alpha,12alpha-diol-3-one + NADPH + H+
5beta-cholestane-7alpha,12alpha-diol-3-one + NADP+
-
a bile acid intermediate
-
-
?
DELTA4-cholesten-7alpha-ol-3-one + NADPH + H+
5beta-cholestan-7alpha-ol-3-one + NADP+
-
a bile acid intermediate
-
-
?
deoxycorticosterone + NADPH
pregnan-21-ol-3,20-dione + NADP+
dexamethasone + NADPH + H+
? + NADP+
substrate of splice variant AKR1D1-002
-
-
?
epitestosterone + NADPH + H+
?
-
-
-
-
?
ethyl acrylate + NADPH + H+
? + NADP+
-
-
-
?
prednisolone + NADPH + H+
? + NADP+
substrate of splice variant AKR1D1-002
-
-
?
progesterone + NADPH + H+
5beta-pregnane-3,20-dione + NADP+
progesterone + NADPH + H+
?
progesterone + NADPH + H+
pregnan-3,20-dione + NADP+
testosterone + NADPH + H+
(5beta,17beta)-17-hydroxyandrostan-3-one + NADP+
testosterone + NADPH + H+
?
additional information
?
-
11beta,17alpha,21-trihydroxy-pregn-4-en-3,20-dione + NADPH
11beta,17alpha,21-trihydroxypregnan-3,20-dione + NADP+
-
-
-
?
11beta,17alpha,21-trihydroxy-pregn-4-en-3,20-dione + NADPH
11beta,17alpha,21-trihydroxypregnan-3,20-dione + NADP+
-
-
-
?
17alpha,21-dihydroxy-pregn-4-en-3,20-dione + NADPH
17alpha,21-dihydroxy-pregnan-3,20-dione + NADP+
-
-
-
?
17alpha,21-dihydroxy-pregn-4-en-3,20-dione + NADPH
17alpha,21-dihydroxy-pregnan-3,20-dione + NADP+
-
-
-
?
17alpha-methylestr-4-en-3-one + NADPH
17alpha-methylestran-3-one + NADP+
-
-
-
?
17alpha-methylestr-4-en-3-one + NADPH
17alpha-methylestran-3-one + NADP+
-
-
-
?
17beta-hydroxyandrost-4-en-3-one + NADPH
17beta-hydroxy-5beta-androstan-3-one + NADP+
-
trivial name testosterone
-
?
17beta-hydroxyandrost-4-en-3-one + NADPH
17beta-hydroxy-5beta-androstan-3-one + NADP+
-
trivial name testosterone
-
?
17beta-hydroxyandrost-4-en-3-one + NADPH
17beta-hydroxy-5beta-androstan-3-one + NADP+
-
trivial name testosterone
-
?
17beta-hydroxyestr-4-en-3-one + NADPH
17-hydroxyestran-3-one + NADP+
-
-
-
?
17beta-hydroxyestr-4-en-3-one + NADPH
17-hydroxyestran-3-one + NADP+
-
-
-
?
2-cyclohexen-1-one + NADPH + H+
cyclohexanone + NADP+
-
-
-
?
2-cyclohexen-1-one + NADPH + H+
cyclohexanone + NADP+
-
-
-
-
?
4-androstene-3,17-dione + NADPH
5beta-androstan-3,17-dione + NADP+
-
-
-
?
4-androstene-3,17-dione + NADPH
5beta-androstan-3,17-dione + NADP+
-
-
-
?
4-androstene-3,17-dione + NADPH
5beta-androstan-3,17-dione + NADP+
-
-
-
-
?
4-androstene-3,17-dione + NADPH
5beta-androstan-3,17-dione + NADP+
-
-
-
-
?
4-androstene-3,17-dione + NADPH
5beta-androstan-3,17-dione + NADP+
-
-
-
-
?
aldosterone + NADPH
?
-
low activity
-
-
?
aldosterone + NADPH
?
-
-
-
-
?
androst-4-en-3,17-dione + NADPH
5beta-androstan-3,17-dione + NADP+
-
-
-
?
androst-4-en-3,17-dione + NADPH
5beta-androstan-3,17-dione + NADP+
-
-
-
?
androst-4-en-3,17-dione + NADPH
5beta-androstan-3,17-dione + NADP+
-
-
-
?
cortexone + NADPH
21-trihydroxy-5beta-pregnane-3,20-dione + NADP+
-
-
-
?
cortexone + NADPH
21-trihydroxy-5beta-pregnane-3,20-dione + NADP+
-
-
-
?
corticosterone + NADPH + H+
?
-
-
-
-
?
corticosterone + NADPH + H+
?
-
low activity
-
-
?
cortisol + NADPH
11beta,17,21-trihydroxy-5beta-pregnane-3,20-dione + NADP+
-
-
-
?
cortisol + NADPH
11beta,17,21-trihydroxy-5beta-pregnane-3,20-dione + NADP+
-
-
-
?
cortisol + NADPH
?
-
very low activity
-
-
?
cortisol + NADPH
?
-
-
-
-
?
cortisone + NADPH
?
-
-
-
-
?
cortisone + NADPH
?
-
-
-
-
?
cortisone + NADPH + H+
17,21-dihydroxy-5beta-pregnane-3,11,20-trione + NADP+
-
-
-
?
cortisone + NADPH + H+
17,21-dihydroxy-5beta-pregnane-3,11,20-trione + NADP+
-
-
-
-
?
cortisone + NADPH + H+
5beta-17,21dihydroxy-pregnan-3,11,20-trione + NADP+
-
-
-
?
cortisone + NADPH + H+
5beta-17,21dihydroxy-pregnan-3,11,20-trione + NADP+
-
-
-
?
cortisone + NADPH + H+
5beta-17,21dihydroxy-pregnan-3,11,20-trione + NADP+
-
-
-
?
cortisone + NADPH + H+
5beta-17,21dihydroxy-pregnan-3,11,20-trione + NADP+
-
-
-
?
cortisone + NADPH + H+
5beta-17,21dihydroxy-pregnan-3,11,20-trione + NADP+
-
-
-
-
?
cortisone + NADPH + H+
5beta-17,21dihydroxy-pregnan-3,11,20-trione + NADP+
-
-
-
?
cortisone + NADPH + H+
5beta-17,21dihydroxy-pregnan-3,11,20-trione + NADP+
-
-
-
?
cortisone + NADPH + H+
5beta-17,21dihydroxy-pregnan-3,11,20-trione + NADP+
-
-
-
?
cortisone + NADPH + H+
5beta-17,21dihydroxy-pregnan-3,11,20-trione + NADP+
-
high substrate specificity
-
ir
cortisone + NADPH + H+
5beta-17,21dihydroxy-pregnan-3,11,20-trione + NADP+
-
-
-
?
deoxycorticosterone + NADPH
pregnan-21-ol-3,20-dione + NADP+
-
-
-
?
deoxycorticosterone + NADPH
pregnan-21-ol-3,20-dione + NADP+
-
-
-
?
progesterone + NADPH
?
-
-
-
-
?
progesterone + NADPH
?
-
-
-
-
?
progesterone + NADPH + H+
5beta-pregnane-3,20-dione + NADP+
-
-
-
?
progesterone + NADPH + H+
5beta-pregnane-3,20-dione + NADP+
-
no substrate inhibition observed
-
-
?
progesterone + NADPH + H+
5beta-pregnane-3,20-dione + NADP+
-
-
-
?
progesterone + NADPH + H+
5beta-pregnane-3,20-dione + NADP+
-
-
-
ir
progesterone + NADPH + H+
5beta-pregnane-3,20-dione + NADP+
-
-
-
-
?
progesterone + NADPH + H+
5beta-pregnane-3,20-dione + NADP+
-
-
-
?
progesterone + NADPH + H+
5beta-pregnane-3,20-dione + NADP+
5alpha-pregnane-3,20-dione, the 5alpha-isomer of the pregnane-3,20-dione is not formed
-
-
ir
progesterone + NADPH + H+
5beta-pregnane-3,20-dione + NADP+
-
stereospecific reduction of the 4-double-bond in cardenolide biosynthesis
-
-
?
progesterone + NADPH + H+
5beta-pregnane-3,20-dione + NADP+
-
highest substrate specificity
-
-
ir
progesterone + NADPH + H+
5beta-pregnane-3,20-dione + NADP+
-
-
-
-
?
progesterone + NADPH + H+
5beta-pregnane-3,20-dione + NADP+
-
-
-
?
progesterone + NADPH + H+
?
-
-
-
?
progesterone + NADPH + H+
?
-
-
-
-
?
progesterone + NADPH + H+
pregnan-3,20-dione + NADP+
-
-
-
?
progesterone + NADPH + H+
pregnan-3,20-dione + NADP+
-
-
-
?
progesterone + NADPH + H+
pregnan-3,20-dione + NADP+
-
-
-
?
testosterone + NADPH + H+
(5beta,17beta)-17-hydroxyandrostan-3-one + NADP+
-
-
-
?
testosterone + NADPH + H+
(5beta,17beta)-17-hydroxyandrostan-3-one + NADP+
-
-
-
?
testosterone + NADPH + H+
(5beta,17beta)-17-hydroxyandrostan-3-one + NADP+
-
-
-
-
?
testosterone + NADPH + H+
(5beta,17beta)-17-hydroxyandrostan-3-one + NADP+
-
-
-
?
testosterone + NADPH + H+
(5beta,17beta)-17-hydroxyandrostan-3-one + NADP+
substrate of splice variant AKR1D1-002
-
-
?
testosterone + NADPH + H+
(5beta,17beta)-17-hydroxyandrostan-3-one + NADP+
-
-
-
-
?
testosterone + NADPH + H+
(5beta,17beta)-17-hydroxyandrostan-3-one + NADP+
-
-
-
-
?
testosterone + NADPH + H+
?
-
-
-
-
?
testosterone + NADPH + H+
?
-
-
-
?
additional information
?
-
pregnenolone, 21-OH-pregenenolone and isoprogesterone are not accepted by recombinant 5beta-POR
-
-
?
additional information
?
-
-
pregnenolone, 21-OH-pregenenolone and isoprogesterone are not accepted by recombinant 5beta-POR
-
-
?
additional information
?
-
-
AKR1D1 catalyzes the stereospecific reduction of the delta4-double-bond of circulating steroid hormones that contain the delta4-3-ketosteroid functionality, e.g. the reduction of testosteron, progesterone and cortisol to yield the corresponding 5-dihydrosteroid
-
-
?
additional information
?
-
-
aldo-keto reductases are a major superfamily of monomeric NADPH-dependent carbonyl oxidoreductases, active site contains conserved residues D50, Y55, K84, and H117
-
-
?
additional information
?
-
-
the steroid 5beta-reductases catalyze a reaction that is unique in steroid enzymology since the resultant product contains a cis-A/B ring configuration and accordingly contains a 90° bend, the cis-A/B ring configuration is an essential characteristic of cardiac glycosides, e.g. digioxin and bile acids and their precursors
-
-
?
additional information
?
-
-
the recombinant enzyme catalyzes the stereospecific reduction of the delta4-double bond of several steroids with a 3-oxo,delta4,5 structure
-
-
?
additional information
?
-
AKR1D1 catalyzes reduction of DELTA4-ene double bonds in steroid hormones and bile acid precursors. Determination of reaction mechanism by mutational analysis revealing that the 4-pro-R hydride is transferred from the re-face of the nicotinamide ring to C5 of the steroid substrate. E120, a unique substitution in the AKR catalytic tetrad, permits a deeper penetration of the steroid substrate into the active site to promote optimal reactant positioning. It participates with Y58 to create a superacidic oxyanion hole for polarization of the C3 ketone, no role for K87 in the proton relay, overview
-
-
?
additional information
?
-
-
AKR1D1 catalyzes reduction of DELTA4-ene double bonds in steroid hormones and bile acid precursors. Determination of reaction mechanism by mutational analysis revealing that the 4-pro-R hydride is transferred from the re-face of the nicotinamide ring to C5 of the steroid substrate. E120, a unique substitution in the AKR catalytic tetrad, permits a deeper penetration of the steroid substrate into the active site to promote optimal reactant positioning. It participates with Y58 to create a superacidic oxyanion hole for polarization of the C3 ketone, no role for K87 in the proton relay, overview
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
-
AKR1D1 catalyzes the central 5beta-reduction step and reduces bile acid precursors such as DELTA4-cholesten-7alpha-ol-3-one and DELTA 4-cholestene-7alpha,12alpha-diol-3-one to 5beta-cholestan-7alpha-ol-3-one and 5beta-cholestane-7alpha,12alpha-diol-3-one, respectively
-
-
?
additional information
?
-
-
substrate specificity of homogeneous human recombinant AKR1D1 using C18, C19, C21, and C27 DELTA4-ketosteroids, AKR1D1 proficiently reduces all the steroids tested at physiological pH, overview
-
-
?
additional information
?
-
-
the enzyme catalyzes stereo-specifically reduces the DELTA4 double bond in 3-keto steroids and sterols to yield the 5beta-hydrogenated product
-
-
?
additional information
?
-
the enzyme catalyzes stereo-specifically reduces the DELTA4 double bond in 3-keto steroids and sterols to yield the 5beta-hydrogenated product
-
-
?
additional information
?
-
splice variant AKR1D1-002 efficiently metabolizes glucocorticoids and androgens and decreases receptor activation. Variants AKR1D1-001 and AKR1D1-006 poorly metabolize dexamethasone, but do not metabolize cortisol, prednisolone, testosterone or androstenedione
-
-
-
additional information
?
-
-
splice variant AKR1D1-002 efficiently metabolizes glucocorticoids and androgens and decreases receptor activation. Variants AKR1D1-001 and AKR1D1-006 poorly metabolize dexamethasone, but do not metabolize cortisol, prednisolone, testosterone or androstenedione
-
-
-
additional information
?
-
-
enzyme is involved in the biosynthesis of ecdysteroids, catalyzes the 5beta-reduction of a 3-oxo-DELTA4-diketol to a 3-oxo-5beta-diketol
-
-
?
additional information
?
-
-
NADH: no effect
-
-
?
additional information
?
-
-
enzyme reduces a variety of C19 and C21 steroids, highest activity with aldosterone
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
17alpha-hydroxyprogesterone + NADPH
?
-
-
-
-
?
2-cyclohexen-1-one + NADPH + H+
cyclohexanone + NADP+
4-androstene-3,17-dione + NADPH
5beta-androstan-3,17-dione + NADP+
aldosterone + NADPH
?
-
low activity
-
-
?
cholest-4-en-3-one + NADPH + H+
5beta-cholestan-3-one + NADP+
-
-
-
?
corticosterone + NADPH + H+
?
-
low activity
-
-
?
cortisol + NADPH
?
-
very low activity
-
-
?
cortisone + NADPH + H+
17,21-dihydroxy-5beta-pregnane-3,11,20-trione + NADP+
DELTA 4-cholestene-7alpha,12alpha-diol-3-one + NADPH + H+
5beta-cholestane-7alpha,12alpha-diol-3-one + NADP+
-
a bile acid intermediate
-
-
?
DELTA4-cholesten-7alpha-ol-3-one + NADPH + H+
5beta-cholestan-7alpha-ol-3-one + NADP+
-
a bile acid intermediate
-
-
?
progesterone + NADPH
?
-
-
-
-
?
progesterone + NADPH + H+
5beta-pregnane-3,20-dione + NADP+
progesterone + NADPH + H+
?
-
-
-
?
testosterone + NADPH + H+
(5beta,17beta)-17-hydroxyandrostan-3-one + NADP+
testosterone + NADPH + H+
?
-
-
-
?
additional information
?
-
2-cyclohexen-1-one + NADPH + H+
cyclohexanone + NADP+
-
-
-
?
2-cyclohexen-1-one + NADPH + H+
cyclohexanone + NADP+
-
-
-
-
?
4-androstene-3,17-dione + NADPH
5beta-androstan-3,17-dione + NADP+
-
-
-
-
?
4-androstene-3,17-dione + NADPH
5beta-androstan-3,17-dione + NADP+
-
-
-
-
?
cortisone + NADPH + H+
17,21-dihydroxy-5beta-pregnane-3,11,20-trione + NADP+
-
-
-
?
cortisone + NADPH + H+
17,21-dihydroxy-5beta-pregnane-3,11,20-trione + NADP+
-
-
-
-
?
progesterone + NADPH + H+
5beta-pregnane-3,20-dione + NADP+
-
-
-
?
progesterone + NADPH + H+
5beta-pregnane-3,20-dione + NADP+
-
-
-
-
?
progesterone + NADPH + H+
5beta-pregnane-3,20-dione + NADP+
-
stereospecific reduction of the 4-double-bond in cardenolide biosynthesis
-
-
?
testosterone + NADPH + H+
(5beta,17beta)-17-hydroxyandrostan-3-one + NADP+
-
-
-
-
?
testosterone + NADPH + H+
(5beta,17beta)-17-hydroxyandrostan-3-one + NADP+
-
-
-
?
additional information
?
-
-
AKR1D1 catalyzes the stereospecific reduction of the delta4-double-bond of circulating steroid hormones that contain the delta4-3-ketosteroid functionality, e.g. the reduction of testosteron, progesterone and cortisol to yield the corresponding 5-dihydrosteroid
-
-
?
additional information
?
-
-
aldo-keto reductases are a major superfamily of monomeric NADPH-dependent carbonyl oxidoreductases, active site contains conserved residues D50, Y55, K84, and H117
-
-
?
additional information
?
-
-
the steroid 5beta-reductases catalyze a reaction that is unique in steroid enzymology since the resultant product contains a cis-A/B ring configuration and accordingly contains a 90° bend, the cis-A/B ring configuration is an essential characteristic of cardiac glycosides, e.g. digioxin and bile acids and their precursors
-
-
?
additional information
?
-
-
AKR1D1 catalyzes the central 5beta-reduction step and reduces bile acid precursors such as DELTA4-cholesten-7alpha-ol-3-one and DELTA 4-cholestene-7alpha,12alpha-diol-3-one to 5beta-cholestan-7alpha-ol-3-one and 5beta-cholestane-7alpha,12alpha-diol-3-one, respectively
-
-
?
additional information
?
-
-
enzyme is involved in the biosynthesis of ecdysteroids, catalyzes the 5beta-reduction of a 3-oxo-DELTA4-diketol to a 3-oxo-5beta-diketol
-
-
?
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3-oxo-5beta-steroid 4-dehydrogenase deficiency
Characterization of disease-related 5beta-reductase (AKR1D1) mutations reveals their potential to cause bile acid deficiency.
Adrenoleukodystrophy
Case report of dysregulation of primary bile acid synthesis in a family with X-linked adrenoleukodystrophy.
Alagille Syndrome
[Clinical characteristics and gene variants of patients with infantile intrahepatic cholestasis].
Arthritis, Rheumatoid
Circulating Biomarkers for Predicting Infliximab Response in Rheumatoid Arthritis: A Systematic Bioinformatics Analysis.
Biliary Atresia
Urinary 7alpha-hydroxy-3-oxochol-4-en-24-oic and 3-oxochola-4,6-dien-24-oic acids in infants with cholestasis.
Carcinoma, Hepatocellular
AKR1D1 is a novel regulator of metabolic phenotype in human hepatocytes and is dysregulated in non-alcoholic fatty liver disease.
Carcinoma, Hepatocellular
AKR1D1 regulates glucocorticoid availability and glucocorticoid receptor activation in human hepatoma cells.
Carcinoma, Hepatocellular
Diagnostic and prognostic values of AKR1C3 and AKR1D1 in hepatocellular carcinoma.
Carcinoma, Hepatocellular
Differential activity and expression of human 5?-reductase (AKR1D1) splice variants.
Carcinoma, Hepatocellular
Differential Feedback Regulation of ?4-3-Oxosteroid 5?-Reductase Expression by Bile Acids.
Cholestasis
In-Depth Dissection of the P133R Mutation in Steroid 5?-Reductase (AKR1D1): A Molecular Basis of Bile Acid Deficiency.
Cholestasis
Infant cholestasis patient with a novel missense mutation in the AKR1D1 gene successfully treated by early adequate supplementation with chenodeoxycholic acid: A case report and review of the literature.
Cholestasis
Urinary 7alpha-hydroxy-3-oxochol-4-en-24-oic and 3-oxochola-4,6-dien-24-oic acids in infants with cholestasis.
Cholestasis, Intrahepatic
AKR1D1 and CYP7B1 mutations in patients with inborn errors of bile acid metabolism: Possibly underdiagnosed diseases.
Cholestasis, Intrahepatic
[Clinical characteristics and gene variants of patients with infantile intrahepatic cholestasis].
Cystic Fibrosis
[Clinical characteristics and gene variants of patients with infantile intrahepatic cholestasis].
delta4-3-oxosteroid 5beta-reductase deficiency
?4-3-oxosteroid-5?-reductase deficiency: Responses to oral bile acid therapy and long-term outcomes.
delta4-3-oxosteroid 5beta-reductase deficiency
Cholic Acid to Treat HSD3B7 and AKR1D1 Deficiencies.
delta4-3-oxosteroid 5beta-reductase deficiency
Determination of 3-oxo-delta4- and 3-oxo-delta4,6-bile acids and related compounds in biological fluids of infants with cholestasis by gas chromatography-mass spectrometry.
delta4-3-oxosteroid 5beta-reductase deficiency
Diagnosis of the first Japanese patient with 3-oxo-delta4-steroid 5beta-reductase deficiency by use of immunoblot analysis.
delta4-3-oxosteroid 5beta-reductase deficiency
Urinary 7alpha-hydroxy-3-oxochol-4-en-24-oic and 3-oxochola-4,6-dien-24-oic acids in infants with cholestasis.
Diabetes Complications
The aldo-keto reductases (AKRs): Overview.
Fatty Liver
AKR1D1 is a novel regulator of metabolic phenotype in human hepatocytes and is dysregulated in non-alcoholic fatty liver disease.
Hepatitis
In-Depth Dissection of the P133R Mutation in Steroid 5?-Reductase (AKR1D1): A Molecular Basis of Bile Acid Deficiency.
Hepatitis
Infant cholestasis patient with a novel missense mutation in the AKR1D1 gene successfully treated by early adequate supplementation with chenodeoxycholic acid: A case report and review of the literature.
Insulin Resistance
AKR1D1 is a novel regulator of metabolic phenotype in human hepatocytes and is dysregulated in non-alcoholic fatty liver disease.
Liver Cirrhosis
Plasma fetal bile acids 7?-hydroxy-3-oxochol-4-en-24-oic acid and 3-oxachola-4,6-dien-24-oic acid indicate severity of liver cirrhosis.
Liver Diseases
A combination of mutations in AKR1D1 and SKIV2L in a family with severe infantile liver disease.
Liver Diseases
AKR1D1 is a novel regulator of metabolic phenotype in human hepatocytes and is dysregulated in non-alcoholic fatty liver disease.
Liver Diseases
Determination of 3-oxo-delta4- and 3-oxo-delta4,6-bile acids and related compounds in biological fluids of infants with cholestasis by gas chromatography-mass spectrometry.
Liver Failure, Acute
Urinary 7alpha-hydroxy-3-oxochol-4-en-24-oic and 3-oxochola-4,6-dien-24-oic acids in infants with cholestasis.
Neoplasms
Diagnostic and prognostic values of AKR1C3 and AKR1D1 in hepatocellular carcinoma.
Neoplasms
Regulation Network and Prognostic Significance of Aldo-Keto Reductase (AKR) Superfamily Genes in Hepatocellular Carcinoma.
Neoplasms
The aldo-keto reductases (AKRs): Overview.
Niemann-Pick Diseases
[Clinical characteristics and gene variants of patients with infantile intrahepatic cholestasis].
Non-alcoholic Fatty Liver Disease
AKR1D1 is a novel regulator of metabolic phenotype in human hepatocytes and is dysregulated in non-alcoholic fatty liver disease.
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0.0032
1,4-androstadien-17beta-ol-3-one
-
pH 6.0, 37°C
0.116 - 1.15
2-cyclohexen-1-one
0.0009 - 2.193
4-androstene-3,17-dione
0.0008
4-cholesten-7alpha-ol-3-one
-
pH 6.0, 37°C
0.003
4-estren-17beta-ol-3-one
-
pH 6.0, 37°C
0.0122
7alpha,12alpha-dihydroxy-4-cholesten-3-one
-
-
0.0091
7alpha-hydroxy-4-cholesten-3-one
-
-
0.0025
aldosterone
-
pH 6.0, 37°C
0.022
androst-4-en-3,17-dione
-
-
0.0022
androst-4-ene-3,17-dione
-
-
0.00037 - 0.01629
androstenedione
0.0003
cholestenone
-
pH 6.0, 37°C
0.0022
corticosterone
-
pH 6.0, 37°C
0.0029
Epitestosterone
-
pH 6.0, 37°C
0.00219 - 0.362
progesterone
0.0016 - 0.0127
testosterone
additional information
additional information
-
0.116
2-cyclohexen-1-one
pH 8.0, 40°C, recombinant wild-type enzyme
0.175
2-cyclohexen-1-one
-
pH 8.0, 40°C, recombinant mutant N205A
0.196
2-cyclohexen-1-one
-
pH 8.0, 40°C, recombinant mutant N205M
0.333
2-cyclohexen-1-one
-
pH 8.0, 40°C, recombinant wild-type enzyme
0.334
2-cyclohexen-1-one
-
pH 8.0, 40°C, recombinant mutant Y156V/N205M
0.358
2-cyclohexen-1-one
mutant R63K/R64H, cofactor NADPH, pH 6, 40°C
0.443
2-cyclohexen-1-one
wild-type, cofactor NADPH, pH 6, 40°C
0.541
2-cyclohexen-1-one
mutant R63K/R64H, cofactor NADH, pH 6, 40°C
1.15
2-cyclohexen-1-one
-
pH 8.0, 40°C, recombinant mutant Y156V
0.0009
4-androstene-3,17-dione
-
pH 6.0, 37°C
0.0022
4-androstene-3,17-dione
-
-
0.00485
4-androstene-3,17-dione
-
-
0.0057
4-androstene-3,17-dione
isoform AKR1D4L, pH 7, 37°C
0.008
4-androstene-3,17-dione
isoform AKR1D4S, pH 7, 37°C
0.228
4-androstene-3,17-dione
-
2.193
4-androstene-3,17-dione
-
0.00037
androstenedione
pH 7.4, 37°C, wild-type enzyme
0.00094
androstenedione
pH 7.4, 37°C, mutant Y132F
0.01629
androstenedione
pH 7.4, 37°C, mutant V309F
1.597
cortexone
-
0.0071
cortisol
isoform AKR1D4L, pH 7, 37°C
0.0114
cortisol
isoform AKR1D4S, pH 7, 37°C
0.0131
cortisol
-
pH 6.0, 37°C
0.0013
cortisone
mutant P133R, pH not specified in the publication, temperature not specified in the publication
0.0013
cortisone
pH 6.0, 37°C, mutant P133R
0.0151
cortisone
-
pH 6.0, 37°C
0.0151
cortisone
pH 6.0, 37°C, wild-type enzyme
0.0151
cortisone
wild-type, pH not specified in the publication, temperature not specified in the publication
0.003
NADPH
-
-
0.00219
progesterone
-
-
0.0063
progesterone
-
wild-type, pH 7.4, 37°C
0.0105
progesterone
-
mutant Y132G, pH 7.4, 37°C
0.063
progesterone
-
pH 8.0, 40°C, recombinant mutant N205M
0.072
progesterone
-
pH 8.0, 40°C, recombinant mutant Y156V
0.085
progesterone
-
pH 8.0, 40°C, recombinant mutant N205A
0.09
progesterone
-
pH 8.0, 40°C, recombinant mutant Y156V/N205M
0.12
progesterone
purified wild type enzyme
0.268
progesterone
pH 8.0, 40°C, recombinant wild-type enzyme
0.362
progesterone
-
pH 8.0, 40°C, recombinant wild-type enzyme
0.0016
testosterone
-
-
0.0027
testosterone
-
pH 6.0, 37°C
0.0027
testosterone
pH 6.0, 37°C, wild-type enzyme
0.0027
testosterone
-
in 100 mM potassium phosphate buffer (pH 6.0), at 37°C
0.0027
testosterone
wild-type, pH not specified in the publication, temperature not specified in the publication
0.0127
testosterone
mutant P133R, pH not specified in the publication, temperature not specified in the publication
0.0127
testosterone
pH 6.0, 37°C, mutant P133R
additional information
additional information
Michaelis-Menten kinetics for the reduction of androstenedione, overview
-
additional information
additional information
-
Michaelis-Menten kinetics for the reduction of androstenedione, overview
-
additional information
additional information
-
Henri-Michaelis-Menten steady-state kinetics of mutant enzyme P133R
-
additional information
additional information
Henri-Michaelis-Menten steady-state kinetics of mutant enzyme P133R
-
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0.035
1,4-androstadien-17beta-ol-3-one
-
pH 6.0, 37°C
0.23 - 1.11
2-cyclohexen-1-one
0.0337 - 0.1
4-androstene-3,17-dione
0.033
4-cholesten-7alpha-ol-3-one
-
pH 6.0, 37°C
0.045
4-estren-17beta-ol-3-one
-
pH 6.0, 37°C
0.0128
7alpha,12alpha-dihydroxy-4-cholesten-3-one
-
-
0.01
7alpha-hydroxy-4-cholesten-3-one
-
-
0.15
aldosterone
-
pH 6.0, 37°C
0.013 - 0.0425
androstenedione
0.01
cholestenone
-
pH 6.0, 37°C
0.032
corticosterone
-
pH 6.0, 37°C
0.1
Epitestosterone
-
pH 6.0, 37°C
0.00197 - 1.8
progesterone
additional information
additional information
-
-
-
0.23
2-cyclohexen-1-one
wild-type, cofactor NADPH, pH 6, 40°C
0.28
2-cyclohexen-1-one
mutant R63K/R64H, cofactor NADPH, pH 6, 40°C
0.4
2-cyclohexen-1-one
-
pH 8.0, 40°C, recombinant mutant Y156V/N205M
0.475
2-cyclohexen-1-one
-
pH 8.0, 40°C, recombinant mutant N205M
0.49
2-cyclohexen-1-one
-
pH 8.0, 40°C, recombinant wild-type enzyme
0.68
2-cyclohexen-1-one
-
pH 8.0, 40°C, recombinant mutant Y156V
0.81
2-cyclohexen-1-one
mutant R63K/R64H, cofactor NADH, pH 6, 40°C
1.1
2-cyclohexen-1-one
-
pH 8.0, 40°C, recombinant mutant N205A
1.11
2-cyclohexen-1-one
pH 8.0, 40°C, recombinant wild-type enzyme
0.0337
4-androstene-3,17-dione
-
-
0.05
4-androstene-3,17-dione
isoform AKR1D4L, pH 7, 37°C
0.09
4-androstene-3,17-dione
isoform AKR1D4S, pH 7, 37°C
0.1
4-androstene-3,17-dione
-
pH 6.0, 37°C
0.013
androstenedione
pH 7.4, 37°C, wild-type enzyme
0.0405
androstenedione
pH 7.4, 37°C, mutant Y132F
0.0425
androstenedione
pH 7.4, 37°C, mutant V309F
0.00817
cortisol
-
-
0.045
cortisol
-
pH 6.0, 37°C
0.08
cortisol
isoform AKR1D4L, pH 7, 37°C
0.13
cortisol
isoform AKR1D4S, pH 7, 37°C
0.01
cortisone
mutant P133R, pH not specified in the publication, temperature not specified in the publication
0.01
cortisone
pH 6.0, 37°C, mutant P133R
0.165
cortisone
pH 6.0, 37°C, wild-type enzyme
0.17
cortisone
wild-type, pH not specified in the publication, temperature not specified in the publication
0.195
cortisone
-
pH 6.0, 37°C
0.00197
progesterone
-
wild-type, pH 7.4, 37°C
0.00348
progesterone
-
mutant Y132G, pH 7.4, 37°C
0.0075
progesterone
-
pH 8.0, 40°C, recombinant mutant Y156V
0.011
progesterone
-
pH 8.0, 40°C, recombinant mutant Y156V/N205M
0.019
progesterone
-
pH 8.0, 40°C, recombinant wild-type enzyme
0.03
progesterone
-
pH 8.0, 40°C, recombinant mutant N205M
0.037
progesterone
-
pH 8.0, 40°C, recombinant mutant N205A
0.17
progesterone
pH 8.0, 40°C, recombinant wild-type enzyme
0.012
testosterone
pH 6.0, 37°C, wild-type enzyme
0.045
testosterone
pH 6.0, 37°C, mutant P133R
0.05
testosterone
mutant P133R, pH not specified in the publication, temperature not specified in the publication
0.12
testosterone
wild-type, pH not specified in the publication, temperature not specified in the publication
0.14
testosterone
-
pH 6.0, 37°C
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10.94
1,4-androstadien-17beta-ol-3-one
-
pH 6.0, 37°C
0.52 - 9.607
2-cyclohexen-1-one
0.93 - 2.77
4-androstene-3,17-dione
41.25
4-cholesten-7alpha-ol-3-one
-
pH 6.0, 37°C
15
4-estren-17beta-ol-3-one
-
pH 6.0, 37°C
60
aldosterone
-
pH 6.0, 37°C
2.609 - 43.08
androstenedione
33.33
cholestenone
-
pH 6.0, 37°C
14.54
corticosterone
-
pH 6.0, 37°C
34.48
Epitestosterone
-
pH 6.0, 37°C
0.052 - 0.628
progesterone
0.52
2-cyclohexen-1-one
wild-type, cofactor NADPH, pH 6, 40°C
0.588
2-cyclohexen-1-one
-
pH 8.0, 40°C, recombinant mutant Y156V
0.611
2-cyclohexen-1-one
mutant R63K/R64H, cofactor NADPH, pH 6, 40°C
1.19
2-cyclohexen-1-one
-
pH 8.0, 40°C, recombinant mutant Y156V/N205M
1.464
2-cyclohexen-1-one
-
pH 8.0, 40°C, recombinant wild-type enzyme
1.5
2-cyclohexen-1-one
mutant R63K/R64H, cofactor NADH, pH 6, 40°C
2.425
2-cyclohexen-1-one
-
pH 8.0, 40°C, recombinant mutant N205M
6.266
2-cyclohexen-1-one
-
pH 8.0, 40°C, recombinant mutant N205A
9.607
2-cyclohexen-1-one
pH 8.0, 40°C, recombinant wild-type enzyme
0.93
4-androstene-3,17-dione
isoform AKR1D4L, pH 7, 37°C
1
4-androstene-3,17-dione
isoform AKR1D4S, pH 7, 37°C
2.77
4-androstene-3,17-dione
-
pH 6.0, 37°C
2.609
androstenedione
pH 7.4, 37°C, mutant V309F
35.13
androstenedione
pH 7.4, 37°C, wild-type enzyme
43.08
androstenedione
pH 7.4, 37°C, mutant Y132F
3.44
cortisol
-
pH 6.0, 37°C
10.5
cortisol
isoform AKR1D4S, pH 7, 37°C
13
cortisol
isoform AKR1D4L, pH 7, 37°C
7.69
cortisone
pH 6.0, 37°C, mutant P133R
7.7
cortisone
mutant P133R, pH not specified in the publication, temperature not specified in the publication
10.93
cortisone
pH 6.0, 37°C, wild-type enzyme
11
cortisone
wild-type, pH not specified in the publication, temperature not specified in the publication
12.91
cortisone
-
pH 6.0, 37°C
0.052
progesterone
-
pH 8.0, 40°C, recombinant wild-type enzyme
0.105
progesterone
-
pH 8.0, 40°C, recombinant mutant Y156V
0.122
progesterone
-
pH 8.0, 40°C, recombinant mutant Y156V/N205M
0.313
progesterone
-
wild-type, pH 7.4, 37°C
0.35
progesterone
-
mutant Y132G, pH 7.4, 37°C
0.432
progesterone
-
pH 8.0, 40°C, recombinant mutant N205A
0.473
progesterone
-
pH 8.0, 40°C, recombinant mutant N205M
0.628
progesterone
pH 8.0, 40°C, recombinant wild-type enzyme
3.5
testosterone
mutant P133R, pH not specified in the publication, temperature not specified in the publication
3.54
testosterone
pH 6.0, 37°C, mutant P133R
4.44
testosterone
pH 6.0, 37°C, wild-type enzyme
43.8
testosterone
wild-type, pH not specified in the publication, temperature not specified in the publication
51.85
testosterone
-
pH 6.0, 37°C
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Y132G
-
10% increase in catalytic efficiency
Y132G/V309K
-
loss of activity
Y132G/V309W
-
loss of activity
R63K
mutant is able to use NADH as cofactor
R63K/R64H
increases enzymatic activity by 13.8fold with NADH as cofactor
R64G
mutant exhibits significantly improved activity with NADH
R64H
mutant exhibits significantly improved activity with NADH
R64S
mutant exhibits significantly improved activity with NADH
R64T
mutant exhibits significantly improved activity with NADH
C352G
-
site-directed mutagenesis, mutation at the substrate binding site, the mutant shows reduced activity compared to the wild-type enzyme
D181T/L182Q
-
site-directed mutagenesis, mutation at motif V, the mutant shows reduced activity compared to the wild-type enzyme
F353M
-
site-directed mutagenesis, mutation at the substrate binding site, the mutant shows similar activity as the wild-type enzyme
F353P
-
site-directed mutagenesis, mutation at the substrate binding site, the mutant shows similar activity as the wild-type enzyme
G204N
-
site-directed mutagenesis, mutation at motif IV, the mutant shows reduced activity compared to the wild-type enzyme
L182Q
-
site-directed mutagenesis, mutation at motif V, the mutant shows similar activity as the wild-type enzyme
M150L
-
site-directed mutagenesis, mutation at motif IV, the mutant shows similar activity as the wild-type enzyme
N205A
-
site-directed mutagenesis, mutation at the substrate binding site, the mutant shows increased activity compared to the wild-type enzyme
N205M
-
site-directed mutagenesis, mutation at the substrate binding site, the mutant shows increased activity compared to the wild-type enzyme
N205M/Y156V
-
site-directed mutagenesis, double mutation at the substrate binding site, the mutant shows increased activity compared to the wild-type enzyme
R146T
-
site-directed mutagenesis, mutation at motif IV, the mutant shows similar activity as the wild-type enzyme
S248M
-
site-directed mutagenesis, mutation near the substrate binding site, inactive mutant
T65P
-
site-directed mutagenesis, mutation at near motif II, the mutant shows similar activity as the wild-type enzyme
Y156V
-
site-directed mutagenesis, mutation at the substrate binding site, the mutant shows increased activity compared to the wild-type enzyme
Y302F
-
site-directed mutagenesis, mutation at motif IV, the mutant shows similar activity as the wild-type enzyme
E120A
-
mutant is devoid of activity
R217stop
the naturally occuring mutation of gene SRD5B1 are involved in hyper-3-oxo-DELTA4 bile aciduria from primary 3-oxo-DELTA4-steroid 5beta-reductase deficiency, phenotypes, overview
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
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
Y58F
-
mutant is devoid of activity
G223E
the naturally occuring mutation of gene SRD5B1 are involved in hyper-3-oxo-DELTA4 bile aciduria from primary 3-oxo-DELTA4-steroid 5beta-reductase deficiency, phenotypes, overview
G223E
-
naturally occuring mutation, identified in patients with functional bile acid deficiency, a non-synonymous point mutations in highly conserved portions of the AKR1D1 gene
G223E
naturally occuring mutation, identified in patients with functional bile acid deficiency, inactive mutant
L106F
mutant identified in patient with reduced enzymic activity
L106F
-
naturally occuring mutation, identified in patients with functional bile acid deficiency, a non-synonymous point mutations in highly conserved portions of the AKR1D1 gene
L106F
naturally occuring mutation, identified in patients with functional bile acid deficiency, almost inactive mutant
P133R
mutant identified in patient with reduced enzymic activity
P133R
mutant identified in patient with reduced enzymic activity. Mutant displays a highly reduced Km and Vmax reminiscent of uncompetitive kinetics with 4-cholesten-7alpha-ol-3-one as substrate. Mutant displays no change in cofactor affinity but is more thermolabile in the absence of NADPH
P133R
-
naturally occuring mutation, identified in patients with functional bile acid deficiency, a non-synonymous point mutations in highly conserved portions of the AKR1D1 gene. The mutant exhibits reduced Km and kcat with the bile acid intermediate DELTA4-cholesten-7alpha-ol-3-one as substrate reminiscent of uncompetitive inhibition
P133R
naturally occuring mutation, identified in patients with functional bile acid deficiency, AKR1D1-P133R activity is significantly reduced compared with wild-type enzyme
P198L
662C -T missense mutation in AKR1D1 causing an almost total absence of 5beta-reduced metabolites of corticosteroids and severely reduced production of 5beta-reduced metabolites of other steroids leading to hepatic failure of the homozygous mutant person, phenotype, overview. Heterozygous persons for the mutation show no phenotype or attenuated 5beta-reduction of cortisol, serum bile acid contents of mutant persons, overview
P198L
mutant identified in patient with reduced enzymic activity
P198L
-
naturally occuring mutation, identified in patients with functional bile acid deficiency, a non-synonymous point mutations in highly conserved portions of the AKR1D1 gene
P198L
naturally occuring mutation, identified in patients with functional bile acid deficiency, inactive mutant
R261C
mutant identified in patient with reduced enzymic activity
R261C
-
naturally occuring mutation, identified in patients with functional bile acid deficiency, a non-synonymous point mutations in highly conserved portions of the AKR1D1 gene
R261C
naturally occuring mutation, identified in patients with functional bile acid deficiency, almost inactive mutant
additional information
determination of AKR1D1 reaction mechanism by mutational analysis revealing that the 4-pro-R hydride is transferred from the re-face of the nicotinamide ring to C5 of the steroid substrate. E120, a unique substitution in the AKR catalytic tetrad, permits a deeper penetration of the steroid substrate into the active site to promote optimal reactant positioning. It participates with Y58 to create a superacidic oxyanion hole for polarization of the C3 ketone, no role for K87 in the proton relay, overview
additional information
-
determination of AKR1D1 reaction mechanism by mutational analysis revealing that the 4-pro-R hydride is transferred from the re-face of the nicotinamide ring to C5 of the steroid substrate. E120, a unique substitution in the AKR catalytic tetrad, permits a deeper penetration of the steroid substrate into the active site to promote optimal reactant positioning. It participates with Y58 to create a superacidic oxyanion hole for polarization of the C3 ketone, no role for K87 in the proton relay, overview
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Furuebisu, M.; Deguchi, S.; Okuda, K.
Identification of cortisone 5beta-reductase as DELTA4-3-ketosteroid 5beta-reductase
Biochim. Biophys. Acta
912
110-114
1987
Rattus norvegicus
brenda
Okuda, A.; Okuda, K.
Purification and characterization of DELTA 4-3-ketosteroid 5beta-reductase
J. Biol. Chem.
259
7519-7524
1984
Rattus norvegicus
brenda
Wilton, D.C.
Is a Schiff base involved in the mechanism of the DELTA4-3-oxo steroid 5alpha- or 5beta-reductases from mammalian liver?
Biochem. J.
155
487-491
1976
Rattus norvegicus
brenda
Collins, W.; Cameron, E.H.D.
Subcellular localization and properties of mouse adrenal C19-steroid 5beta-reductase
Biochem. J.
147
165-174
1975
Mus musculus
brenda
Forchielli, E.; Dorfmann, R.I.
Separation of DELTA4-5alpha- and DELTA4-5beta-hydrogenases from rat liver homogenates
J. Biol. Chem.
223
443-448
1956
Rattus norvegicus
brenda
Nduaguba, J.C.; Clark, A.F.
Steroid DELTA4-reductases of pig liver: partial purification of testosterone 5beta-reductase
Can. J. Biochem.
49
385-392
1971
Sus scrofa
brenda
Van Doorn, E.J.; Nduaguba, J.C.; Clark, A.F.
Studies on partially purified pig liver steroid DELTA4-5beta-reductase activity
Can. J. Biochem.
51
1661-1668
1973
Sus scrofa
brenda
Charbonneau, A.; The, V.L.
Genomic organization of a human 5beta-reductase and its pseudogene and substrate selectivity of the expressed enzyme
Biochim. Biophys. Acta
1517
228-235
2001
Homo sapiens
brenda
Dauphin-Villemant, C.; Blais, C.; Lafont, R.
Towards the elucidation of the ecdysteroid biosynthetic pathway
Ann. N. Y. Acad. Sci.
839
306-310
1998
Pancrustacea
-
brenda
Brown-Grant, K.; Forchielli, E.; Dorfman, R.I.
The DELTA4-hydrogenases of guinea pig adrenal gland
J. Biol. Chem.
235
1317-1320
1960
Cavia porcellus, Rattus norvegicus
brenda
Tomkins, G.M.
The enzymatic reduction of DELTA4-3-ketosteroids
J. Biol. Chem.
225
13-24
1957
Bos taurus, Cavia porcellus, Columba sp., Oryctolagus cuniculus, Rattus norvegicus, Sus scrofa
brenda
Ozon, R.; Fouchet, C.; Perin, F.
Transformation of testosterone into 17beta-hydroxy-5beta-androstan-3-one by Rana esculenta skeletal muscle
Biochim. Biophys. Acta
348
425-437
1974
Pelophylax lessonae
brenda
Jez, J.M.; Penning, T.M.
Engineering steroid 5beta-reductase activity into rat liver 3alpha-hydroxysteroid dehydrogenase
Biochemistry
37
9695-9703
1998
Rattus norvegicus
brenda
Egerer-Sieber, C.; Herl, V.; Mller-Uri, F.; Kreis, W.; Muller, Y.A.
Crystallization and preliminary crystallographic analysis of selenomethionine-labelled progesterone 5beta-reductase from Digitalis lanata Ehrh
Acta Crystallogr. Sect. F
62
186-188
2006
Digitalis lanata
brenda
Gavidia, I.; Tarrio, R.; Rodriguez-Trelles, F.; Perez-Bermudez, P.; Ulrich Seitz, H.
Plant progesterone 5beta-reductase is not homologous to the animal enzyme. Molecular evolutionary characterization of P5betaR from Digitalis purpurea
Phytochemistry
68
853-864
2007
Digitalis purpurea
brenda
Herl, V.; Fischer, G.; Mller-Uri, F.; Kreis, W.
Molecular cloning and heterologous expression of progesterone 5beta-reductase from Digitalis lanata Ehrh.
Phytochemistry
67
225-231
2006
Digitalis lanata (Q6PQJ9), Digitalis lanata
brenda
Herl, V.; Fischer, G.; Btsch, R.; Mller-Uri, F.; Kreis, W.
Molecular cloning and expression of progesterone 5beta-reductase (5beta-POR) from Isoplexis canariensis
Planta Med.
72
1163-1165
2006
Digitalis canariensis (Q078S6), Digitalis canariensis
brenda
Faucher, F.; Cantin, L.; Luu-The, V.; Labrie, F.; Breton, R.
The crystal structure of human DELTA4-3-ketosteroid 5beta-reductase defines the functional role of the residues of the catalytic tetrad in the steroid double bond reduction mechanism
Biochemistry
47
8261-8270
2008
Homo sapiens (P51857), Homo sapiens
brenda
Di Costanzo, L.; Drury, J.E.; Penning, T.M.; Christianson, D.W.
Crystal structure of human liver DELTA4-3-ketosteroid 5beta-reductase (AKR1D1) and implications for substrate binding and catalysis
J. Biol. Chem.
283
16830-16839
2008
Homo sapiens
brenda
Di Costanzo, L.; Penning, T.M.; Christianson, D.W.
Aldo-keto reductases in which the conserved catalytic histidine is substituted
Chem. Biol. Interact.
178
127-133
2009
Digitalis lanata
brenda
Thorn, A.; Egerer-Sieber, C.; Jaeger, C.; Herl, V.; Mueller-Uri, F.; Kreis, W.; Muller, Y.
The crystal structure of progesterone 5beta-reductase from Digitalis lanata defines a novel class of short chain dehydrogenases/reductases
J. Biol. Chem.
283
17260-17269
2008
Digitalis lanata (Q6PQJ9), Digitalis lanata
brenda
Faucher, F.; Cantin, L.; Luu-The, V.; Labrie, F.; Breton, R.
Crystal structures of human Delta4-3-ketosteroid 5beta-reductase (AKR1D1) reveal the presence of an alternative binding site responsible for substrate inhibition
Biochemistry
47
13537-13546
2008
Homo sapiens (P51857), Homo sapiens
brenda
Ueki, I.; Kimura, A.; Chen, H.L.; Yorifuji, T.; Mori, J.; Itoh, S.; Maruyama, K.; Ishige, T.; Takei, H.; Nittono, H.; Kurosawa, T.; Kage, M.; Matsuishi, T.
SRD5B1 gene analysis needed for the accurate diagnosis of primary 3-oxo-Delta4-steroid 5beta-reductase deficiency
J. Gastroenterol. Hepatol.
24
776-785
2009
Homo sapiens (P51857)
brenda
Di Costanzo, L.; Drury, J.E.; Christianson, D.W.; Penning, T.M.
Structure and catalytic mechanism of human steroid 5beta-reductase (AKR1D1)
Mol. Cell. Endocrinol.
301
191-198
2009
Homo sapiens (P51857), Homo sapiens
brenda
Palermo, M.; Marazzi, M.G.; Hughes, B.A.; Stewart, P.M.; Clayton, P.T.; Shackleton, C.H.
Human Delta4-3-oxosteroid 5beta-reductase (AKR1D1) deficiency and steroid metabolism
Steroids
73
417-423
2008
Homo sapiens (P51857), Homo sapiens
brenda
Mindnich, R.; Drury, J.E.; Penning, T.M.
The effect of disease associated point mutations on 5beta-reductase (AKR1D1) enzyme function
Chem. Biol. Interact.
191
250-254
2011
Homo sapiens
brenda
Drury, J.E.; Mindnich, R.; Penning, T.M.
Characterization of disease-related 5beta-reductase (AKR1D1) mutations reveals their potential to cause bile acid deficiency
J. Biol. Chem.
285
24529-24537
2010
Homo sapiens, Homo sapiens (P51857)
brenda
McNeilly, A.D.; Macfarlane, D.P.; OFlaherty, E.; Livingstone, D.E.; Mitic, T.; McConnell, K.M.; McKenzie, S.M.; Davies, E.; Reynolds, R.M.; Thiesson, H.C.; Skott, O.; Walker, B.R.; Andrew, R.
Bile acids modulate glucocorticoid metabolism and the hypothalamic-pituitary-adrenal axis in obstructive jaundice
J. Hepatol.
52
705-711
2010
Rattus norvegicus
brenda
Bauer, P.; Rudolph, K.; Mueller-Uri, F.; Kreis, W.
Vein patterning 1-encoded progesterone 5beta-reductase: activity-guided improvement of catalytic efficiency
Phytochemistry
77
53-59
2012
Digitalis lanata, Arabidopsis thaliana (Q9STX2)
brenda
Chen, M.; Drury, J.E.; Penning, T.M.
Substrate specificity and inhibitor analyses of human steroid 5beta-reductase (AKR1D1)
Steroids
76
484-490
2011
Homo sapiens
brenda
Chen, M.; Wangtrakuldee, P.; Zang, T.; Duan, L.; Gathercole, L.L.; Tomlinson, J.W.; Penning, T.M.
Human and murine steroid 5beta-reductases (AKR1D1 and AKR1D4) insights into the role of the catalytic glutamic acid
Chem. Biol. Interact.
305
163-170
2019
Mus musculus (Q8VCX1), Mus musculus
brenda
Li, Y.; Pan, H.; Chang, Y.; Dong, N.; Zou, L.; Liang, P.; Tian, W.; Chang, Z.
Identification of key sites determining the cofactor specificity and improvement of catalytic activity of a steroid 5beta-reductase from Capsella rubella
Enzyme Microb. Technol.
134
109483
2020
Capsella rubella (R0F4W3)
brenda
Zhang, Y.; Li, X.; Xu, D.; Wu, M.; Dai, Y.; Xia, M.; Wang, D.
Cloning and characterization of steroid 5beta-reductase from the venom gland of Bufo bufo gargarizans
Int. J. Biol. Macromol.
175
67-78
2021
Bufo gargarizans
brenda
Appanna, N.; Gibson, H.; Gangitano, E.; Dempster, N.J.; Morris, K.; George, S.; Arvaniti, A.; Gathercole, L.L.; Keevil, B.; Penning, T.M.; Storbeck, K.H.; Tomlinson, J.W.; Nikolaou, N.
Differential activity and expression of human 5beta-reductase (AKR1D1) splice variants
J. Mol. Endocrinol.
66
181-194
2021
Homo sapiens (P51857), Homo sapiens
brenda
Valanejad, L.; Nadolny, C.; Shiffka, S.; Chen, Y.; You, S.; Deng, R.
Differential feedback regulation of Delta4-3-oxosteroid 5beta-reductase expression by bile acids
PLoS ONE
12
e0170960
2017
Homo sapiens (P51857), Homo sapiens, Mus musculus (Q8VCX1)
brenda