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Information on EC 1.3.1.3 - DELTA4-3-oxosteroid 5beta-reductase and Organism(s) Homo sapiens
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1.3.1.3 DELTA4-3-oxosteroid 5beta-reductaseIUBMB Comments
The enzyme from human efficiently catalyses the reduction of progesterone, androstenedione, 17alpha-hydroxyprogesterone and testosterone to 5beta-reduced metabolites; it can also act on aldosterone, corticosterone and cortisol, but to a lesser extent . The bile acid intermediates 7alpha,12alpha-dihydroxy-4-cholesten-3-one and 7alpha-hydroxy-4-cholesten-3-one can also act as substrates .
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The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
akr1d1, 5beta-por, h5beta-red, progesterone 5beta-reductase, p5betar, steroid 5beta-reductase, srd5beta, aldo-keto reductase 1d1, 3-oxo-delta4-steroid 5beta-reductase, akr1d4, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
4,5beta-dihydrocortisone:NADP+ DELTA4-oxidoreductase
-
-
-
-
5-beta-reductase
-
-
-
-
AKR1D1
androstenedione 5beta-reductase
-
-
-
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cortisone 5beta-reductase
-
-
-
-
cortisone beta-reductase
-
-
-
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DELTA 4-5beta-reductase
-
-
-
-
DELTA4-3-ketosteroid 5beta-reductase
DELTA4-hydrogenase
-
-
-
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reductase, cholestenone 5beta.-
-
-
-
-
reductase, cortisone DELTA4-5beta-
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-
-
-
steroid 5beta-reductase
steroid 5beta.-reductase
-
-
-
-
testosterone 5-beta-reductase
-
-
-
-
testosterone 5beta-reductase
-
-
-
-
additional information
human 5beta-red belongs to the aldo-keto reductase, AKR, superfamily and is the first member of the 1D subfamily, AKR1D1
DELTA4-3-ketosteroid 5beta-reductase
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-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
5beta-cholestan-3-one + NADP+ = cholest-4-en-3-one + NADPH + H+
reaction mechanism, overview
17,21-dihydroxy-5beta-pregnane-3,11,20-trione + NADP+ = cortisone + NADPH + H+
reaction mechanism, overview
17,21-dihydroxy-5beta-pregnane-3,11,20-trione + NADP+ = cortisone + NADPH + H+
catalyzes the reduction of the DELTA4 double bond of DELTA4-3-ketosteroids, converting those steroids into 5beta-dihydro-3-ketosteroids
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
reduction
redox reaction
-
-
-
-
reduction
-
-
-
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PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
5beta-cholestan-3-one:NADP+ 4,5-oxidoreductase
The enzyme from human efficiently catalyses the reduction of progesterone, androstenedione, 17alpha-hydroxyprogesterone and testosterone to 5beta-reduced metabolites; it can also act on aldosterone, corticosterone and cortisol, but to a lesser extent [8]. The bile acid intermediates 7alpha,12alpha-dihydroxy-4-cholesten-3-one and 7alpha-hydroxy-4-cholesten-3-one can also act as substrates [9].
CAS REGISTRY NUMBER
COMMENTARY
37255-35-9
-
9029-08-7
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
7alpha,12beta-dihydroxy-4-cholesten-3-one + NADPH + H+
(5beta,7alpha,12beta)-7,12-dihydroxycholestan-3-one + NADP+
-
-
-
?
7alpha-hydroxy-4-cholesten-3-one + NADPH
(5beta,7alpha)-7-hydroxycholestan-3-one + NADP+
-
-
-
?
cortisone + NADPH + H+
5beta-17,21dihydroxy-pregnan-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
-
-
?
dexamethasone + NADPH + H+
? + NADP+
substrate of splice variant AKR1D1-002
-
-
?
prednisolone + NADPH + H+
? + NADP+
substrate of splice variant AKR1D1-002
-
-
?
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+
-
-
-
-
?
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
-
-
?
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
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-
?
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
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?
additional information
?
-
the enzyme catalyzes stereo-specifically reduces the DELTA4 double bond in 3-keto steroids and sterols to yield the 5beta-hydrogenated product
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?
additional information
?
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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
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-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
?
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
-
-
?
cortisone + NADPH + H+
17,21-dihydroxy-5beta-pregnane-3,11,20-trione + NADP+
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-
-
?
cortisone + NADPH + H+
17,21-dihydroxy-5beta-pregnane-3,11,20-trione + NADP+
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-
-
-
?
testosterone + NADPH + H+
(5beta,17beta)-17-hydroxyandrostan-3-one + NADP+
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-
-
-
?
testosterone + NADPH + H+
(5beta,17beta)-17-hydroxyandrostan-3-one + NADP+
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-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
progesterone
the enzyme is rapidly inhibited by the substrate once its concentration reaches 2times the Km value
testosterone
substrate inhibition; substrate inhibition of the wild-type enzyme
additional information
structural features of substrate inhibition of h5beta-red by C19- and C21-steroids, overview
-
additional information
-
structural features of substrate inhibition of h5beta-red by C19- and C21-steroids, overview
-
additional information
-
substrate inhibition is observed with C18 to C21 steroids provided that the C11 position is unsubstituted
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0013
cortisone
mutant P133R, pH not specified in the publication, temperature not specified in the publication
0.0151
cortisone
wild-type, pH not specified in the publication, temperature not specified in the publication
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
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
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.01
cortisone
mutant P133R, pH not specified in the publication, temperature not specified in the publication
0.17
cortisone
wild-type, pH not specified in the publication, temperature not specified in the publication
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
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
7.7
cortisone
mutant P133R, pH not specified in the publication, temperature not specified in the publication
11
cortisone
wild-type, pH not specified in the publication, temperature not specified in the publication
3.5
testosterone
mutant P133R, pH not specified in the publication, temperature not specified in the publication
43.8
testosterone
wild-type, pH not specified in the publication, temperature not specified in the publication
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0145
testosterone
wild-type, pH not specified in the publication, temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
deficient 5beta-reductase activity can lead to cholestasis and neo-natal liver failure and is often lethal if it remains untreated
physiological function
additional information
physiological function
the enzyme is responsible for steroid hormone 5beta-reduction, as well as for cholic acid and chenodeoxycholic bile-acid synthesis
physiological function
-
human steroid 5beta-reductase, i.e. aldo-keto reductase 1D1, catalyzes the stereospecific NADPH-dependent reduction of the C4-C5 double bond of DELTA4-ketosteroids to yield an A/B cis-ring junction. This cis configuration is crucial for bile acid biosynthesis and plays important roles in steroid metabolism. AKR1D1 is the only enzyme necessary for all the 5-steroid metabolites present in humans
physiological function
-
the human enzyme, AKR1D1, plays an essential role in bile-acid biosynthesis since the 5beta-configuration is required for the emulsifying properties of bile
additional information
-
existence of a small alternative substrate binding pocket, structure-activity relationship, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). AK1D1_HUMAN
326
0
37377
Swiss-Prot
other Location (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
steroid-binding cavity structure of h5 beta-red, structure comparison
additional information
-
steroid-binding cavity structure of h5 beta-red, structure comparison
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme in binary complex with product NADP+, containing two monomers of AKR1D1, each of which consists of a 325-residue polypeptide chain that adopts an (alpha/beta)8-barrel fold, the AKR1D1-NADP+ complex adopts an extended anti-conformation, X-ray diffraction structure determination and analysis at 1.79 A resolution, comparison with other enzyme binary and tertiary ligand complex structures, overview
hanging drop vapour diffusion method in 20% (w/v) PEG-4K, 0.1 M sodium cacodylate (pH 6.5), 0.2 M sodium citrate, 0.5 M (NH4)2SO4
hanging drop vapour diffusion method, in 0.1 M Tris/HEPES (pH 7.5), 10-20% (w/v) polyethylene glycol 4000, and 10% isopropyl alcohol
-
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
G223E
L106F
P133R
P198L
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
R261C
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
additional information
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
-
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. 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
-
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
-
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
glutathione-Sepharose column chromatography and Sephacryl-S100 gel filtration
recombinant AKR1D1 enzyme mutant P133R from HEK-293 cells, the other expressed mutants cannot be purified
recombinant GST-tagged enzyme from Escherichia coli by glutathione affinity and anion exchange chromatography, and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene SRD5B1, DNA and amino acid sequence determination and analysis of wild-type and mutant enzymes
recombinant expression of AKR1D1 enzyme mutants in HEK-293 cells only at low levels possible and with low activities
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
chenodeoxycholic acid markedly represses AKR1D1 expression in vitro in human hepatoma Hep-G2 cells, regulation occurs through the mitogen-activated protein kinases/c-Jun Nterminal kinases (MAPK/JNK) signaling pathway
cholic acid significantly upregulates AKR1D1 expression in HepG2 cells, regulation occurs through the mitogen-activated protein kinases/c-Jun Nterminal kinases (MAPK/JNK) signaling pathway
treatment of cells with proteasomal inhibitor, MG-132 increases expression of splice variants AKR1D1-001 and AKR1D1-006
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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
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
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
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)
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
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
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
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)
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
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
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