Any feedback?
Information on EC 5.3.3.1 - steroid DELTA-isomerase and Organism(s) Homo sapiens and UniProt Accession P26439
for references in articles please use BRENDA:EC5.3.3.1Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
5.3.3.1 steroid DELTA-isomeraseIUBMB Comments
This activity is catalysed by several distinct enzymes (cf. EC 1.1.3.6, cholesterol oxidase and EC 1.1.1.145, 3-hydroxy-5-steroid dehydrogenase).
Specify your search results
Word Map
- 5.3.3.1
-
steroidogenic
- progesterone
- adrenal
-
steroidogenesis
- androgen
- p450scc
- leydig
- star
- testicular
- pregnenolone
- 17beta-hsd
- lh
- aromatase
-
5-3-ketosteroids
- gonad
- testosteroni
-
granulosa
- dehydroepiandrosterone
- luteal
- androstenedione
-
17beta-hydroxysteroid
- dheas
-
theca
- p450arom
- 17alpha-hydroxylase
-
neurosteroids
- cyp11a1
- trilostane
- 19-nortestosterone
-
dienolate
-
5alpha-reductase
- equilenin
-
low-barrier
- 17alpha-hydroxylase/17,20-lyase
-
interna
- 3betahsd
- delta5-3beta-hydroxysteroid
-
intracrine
-
double-bond
- hsd3b1
-
talalay
- 20alpha-hsd
-
beta-proton
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
3beta-hsd, ketosteroid isomerase, delta 5-3-ketosteroid isomerase, steroid isomerase, 3beta-hydroxysteroid dehydrogenase/isomerase, steroid delta-isomerase, gst a3-3, 3beta-hydroxysteroid dehydrogenase/delta5-delta4 isomerase, 3beta-hsd/isomerase, 5-ene-4-ene isomerase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3-Keto-DELTA5-steroid isomerase
-
-
-
-
3-Ketosteroid DELTA5-->DELTA4-isomerase
-
-
-
-
3-Oxo steroid DELTA4-DELTA5-isomerase
-
-
-
-
3-Oxo-delta5 steroid isomerase
-
-
-
-
3-Oxosteroid DELTA4-DELTA5-isomerase
-
-
-
-
3-Oxosteroid DELTA5-DELTA4-isomerase
3-Oxosteroid isomerase
-
-
-
-
3beta-HSD
5-Ene-4-ene isomerase
-
-
-
-
5-Pregnene-3,20-dione isomerase
-
-
-
-
delta 5-3-ketosteroid isomerase
-
-
-
-
DELTA-3-ketosteroid isomerase
-
-
-
-
Delta-5-3-ketosteroid isomerase
-
-
-
-
DELTA5(or DELTA4)-3-keto steroid isomerase
-
-
-
-
DELTA5-3-keto steroid isomerase
-
-
-
-
DELTA5-3-ketosteroid isomerase
DELTA5-3-oxosteroid isomerase
-
-
-
-
DELTA5-ketosteroid isomerase
-
-
-
-
DELTA5-steroid isomerase
-
-
-
-
Hydroxysteroid isomerase
-
-
-
-
Isomerase, steroid DELTA
-
-
-
-
Steroid 5-->4-isomerase
-
-
-
-
Steroid isomerase
-
-
-
-
additional information
3-Oxosteroid DELTA5-DELTA4-isomerase
-
-
-
-
DELTA5-3-ketosteroid isomerase
-
-
-
-
additional information
the enzyme is a member of the short chain dehydrogenase/reductase family, cf. EC 1.1.1.51
additional information
-
3beta-hydroxysteroid dehydrogenase/5-ene--4-ene isomerase
additional information
-
beta-hydroxysteroid dehydrogenase/DELTA5-DELTA4 isomerase
additional information
the enzyme is a member of the short chain dehydrogenase/reductase family, cf. EC 1.1.1.51
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
isomerization
intramolecular oxidoreduction
-
-
-
-
isomerization
-
-
-
-
PATHWAY SOURCE
PATHWAYS
KEGG
-
-, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
3-oxosteroid DELTA5-DELTA4-isomerase
This activity is catalysed by several distinct enzymes (cf. EC 1.1.3.6, cholesterol oxidase and EC 1.1.1.145, 3-hydroxy-5-steroid dehydrogenase).
CAS REGISTRY NUMBER
COMMENTARY
9031-36-1
-
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
additional information
?
-
the bifunctional enzyme possesses 3beta-hydroxysteroid dehydrogenase activity, EC 1.1.1.51, and steroid DELTA-isomerase activity, the enzyme is a key steroidogenic enzyme that catalyzes the first step of the multienzyme pathway conversion of circulating dehydroepiandrosterone and pregnenolone to active steroid hormones
-
-
?
additional information
?
-
the bifunctional enzyme possesses 3beta-hydroxysteroid dehydrogenase activity, EC 1.1.1.51, and steroid DELTA-isomerase activity, the enzyme is a key steroidogenic enzyme that catalyzes the first step of the multienzyme pathway conversion of circulating dehydroepiandrosterone and pregnenolone to active steroid hormones
-
-
?
additional information
?
-
-
the bifunctional enzyme possesses 3beta-hydroxysteroid dehydrogenase activity, EC 1.1.1.51, and steroid DELTA-isomerase activity, the enzyme is a key steroidogenic enzyme that catalyzes the first step of the multienzyme pathway conversion of circulating dehydroepiandrosterone and pregnenolone to active steroid hormones
-
-
?
additional information
?
-
-
in pregnancy placental 3beta-hydroxy-5-ene-steroid dehydrogenase and steroid 5--4 isomerase produce progesterone from pregnenolone and metabolize fetal dehydroepiandrosterone sulfate to androstenedione, an estrogen precursor
-
-
?
additional information
?
-
-
the conversion of 3beta-hydroxy-5-ene steroids by the enzyme complex 3beta-hydroxysteroid dehydrogenase/DELTA5-DELTA4 isomerase is an obligatory step in the biosynthesis of all classes of hormonal steroids in classical steroidogenic as well as in peripheral tissues
-
-
?
additional information
?
-
the bifunctional enzyme possesses 3beta-hydroxysteroid dehydrogenase activity, EC 1.1.1.51, and steroid DELTA-isomerase activity, the enzyme is a key steroidogenic enzyme that catalyzes the first step of the multienzyme pathway conversion of circulating dehydroepiandrosterone and pregnenolone to active steroid hormones
-
-
?
additional information
?
-
the bifunctional enzyme possesses 3beta-hydroxysteroid dehydrogenase activity, EC 1.1.1.51, and steroid DELTA-isomerase activity, the enzyme is a key steroidogenic enzyme that catalyzes the first step of the multienzyme pathway conversion of circulating dehydroepiandrosterone and pregnenolone to active steroid hormones
-
-
?
additional information
?
-
-
the bifunctional enzyme possesses 3beta-hydroxysteroid dehydrogenase activity, EC 1.1.1.51, and steroid DELTA-isomerase activity, the enzyme is a key steroidogenic enzyme that catalyzes the first step of the multienzyme pathway conversion of circulating dehydroepiandrosterone and pregnenolone to active steroid hormones
-
-
?
additional information
?
-
structure-function relations, analysis of three dimensional model of a ternary complex of human 3beta-HSD type 1 with an NAD+ cofactor and androstenedione product, reaction of EC 1.1.1.51, to elucidate the key substrate binding residues in the active site as well as the basis for dual function of the 3beta-HSD_1 enzyme, Asn100 and Glu126 residues are key residues that participate in the dehydrogenase and isomerization reactions, respectively, isomerase substrate binding structure, overview
-
-
?
additional information
?
-
structure-function relations, analysis of three dimensional model of a ternary complex of human 3beta-HSD type 1 with an NAD+ cofactor and androstenedione product, reaction of EC 1.1.1.51, to elucidate the key substrate binding residues in the active site as well as the basis for dual function of the 3beta-HSD_1 enzyme, Asn100 and Glu126 residues are key residues that participate in the dehydrogenase and isomerization reactions, respectively, isomerase substrate binding structure, overview
-
-
?
additional information
?
-
-
structure-function relations, analysis of three dimensional model of a ternary complex of human 3beta-HSD type 1 with an NAD+ cofactor and androstenedione product, reaction of EC 1.1.1.51, to elucidate the key substrate binding residues in the active site as well as the basis for dual function of the 3beta-HSD_1 enzyme, Asn100 and Glu126 residues are key residues that participate in the dehydrogenase and isomerization reactions, respectively, isomerase substrate binding structure, overview
-
-
?
additional information
?
-
human GST A3-3 does not stabilize a dienolate by an oxyanion hole in the active site
-
-
?
additional information
?
-
-
human GST A3-3 does not stabilize a dienolate by an oxyanion hole in the active site
-
-
?
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
additional information
?
-
the bifunctional enzyme possesses 3beta-hydroxysteroid dehydrogenase activity, EC 1.1.1.51, and steroid DELTA-isomerase activity, the enzyme is a key steroidogenic enzyme that catalyzes the first step of the multienzyme pathway conversion of circulating dehydroepiandrosterone and pregnenolone to active steroid hormones
-
-
?
additional information
?
-
the bifunctional enzyme possesses 3beta-hydroxysteroid dehydrogenase activity, EC 1.1.1.51, and steroid DELTA-isomerase activity, the enzyme is a key steroidogenic enzyme that catalyzes the first step of the multienzyme pathway conversion of circulating dehydroepiandrosterone and pregnenolone to active steroid hormones
-
-
?
additional information
?
-
-
the bifunctional enzyme possesses 3beta-hydroxysteroid dehydrogenase activity, EC 1.1.1.51, and steroid DELTA-isomerase activity, the enzyme is a key steroidogenic enzyme that catalyzes the first step of the multienzyme pathway conversion of circulating dehydroepiandrosterone and pregnenolone to active steroid hormones
-
-
?
additional information
?
-
-
in pregnancy placental 3beta-hydroxy-5-ene-steroid dehydrogenase and steroid 5--4 isomerase produce progesterone from pregnenolone and metabolize fetal dehydroepiandrosterone sulfate to androstenedione, an estrogen precursor
-
-
?
additional information
?
-
-
the conversion of 3beta-hydroxy-5-ene steroids by the enzyme complex 3beta-hydroxysteroid dehydrogenase/DELTA5-DELTA4 isomerase is an obligatory step in the biosynthesis of all classes of hormonal steroids in classical steroidogenic as well as in peripheral tissues
-
-
?
additional information
?
-
the bifunctional enzyme possesses 3beta-hydroxysteroid dehydrogenase activity, EC 1.1.1.51, and steroid DELTA-isomerase activity, the enzyme is a key steroidogenic enzyme that catalyzes the first step of the multienzyme pathway conversion of circulating dehydroepiandrosterone and pregnenolone to active steroid hormones
-
-
?
additional information
?
-
the bifunctional enzyme possesses 3beta-hydroxysteroid dehydrogenase activity, EC 1.1.1.51, and steroid DELTA-isomerase activity, the enzyme is a key steroidogenic enzyme that catalyzes the first step of the multienzyme pathway conversion of circulating dehydroepiandrosterone and pregnenolone to active steroid hormones
-
-
?
additional information
?
-
-
the bifunctional enzyme possesses 3beta-hydroxysteroid dehydrogenase activity, EC 1.1.1.51, and steroid DELTA-isomerase activity, the enzyme is a key steroidogenic enzyme that catalyzes the first step of the multienzyme pathway conversion of circulating dehydroepiandrosterone and pregnenolone to active steroid hormones
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADPH
-
D36A/K37R mutation shifts the cofactor preference of both 3-beta-hydroxysteroid dehydrogenase and isomerase from NAD(H) to NADP(H)
NADH
-
the isomerase activity of the wild-type enzyme and the deletion mutant enzyme DELTA283-310 requires allosteric activation by NADH, Km for wild-type enzyme and deletion mutant enzyme is 0.0046 mM
NADH
-
wild-type 1 isomerase is activated only by NADH with NADPH producing no isomerase activity. D36A/K37R mutation shifts the cofactor preference of both 3-beta-hydroxysteroid dehydrogenase and isomerase from NAD(H) to NADP(H)
NADH
-
isomerase activity of enzyme requires NADH, Km- and kcat-value of isoform 1 wild-type are 0.0046 mM and 45 per min, resp. Km- and kcat-value of isoform 2 wild-type are 0.0126 mM and 99.1 per min, resp
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
N,N-Dimethyl-4-methyl-3-oxo-4-aza-5alpha-androstane-17beta-carboxamide
-
non-competitive inhibition of isomerase, competitive inhibition of 3beta-hydroxysteroid dehydrogenase
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0252
5-androstene-3,17-dione
-
22°C, pH 7.4, truncated cytosolic enzyme DEALTA283-310
additional information
additional information
kinetics of wild-type and mutant enzymes
-
additional information
additional information
kinetics of wild-type and mutant enzymes
-
additional information
additional information
-
kinetics of wild-type and mutant enzymes
-
additional information
additional information
kinetics of wild-type and mutant enzymes
-
additional information
additional information
kinetics of wild-type and mutant enzymes
-
additional information
additional information
-
kinetics of wild-type and mutant enzymes
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.622
-
reaction with 5-androsten-3,17-dione, truncated cytosolic enzyme DELTA283-310
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 8
6.5 - 8
-
pH 6.5: about 60% of maximal activity, pH 8.0: about 40% of maximal activity, pH 6.3: no activity
6.5 - 8
-
pH 6.5: about 55% of maximal activity, wild-type enzyme and mutant enzyme D265N, about 65% of maximal activity, mutant enzyme D241N, about 85% of maximal activity mutant enzyme D257L and D258L. pH 8.0: about 50% of maximal activity, wild-type enzyme and mutant enzymes D241N, 95% of maximal activity, mutant enzyme D258L
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22 - 42
-
22°C: about 60% of maximal activity, 40°C: about 40% of maximal activity
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
modified enzyme in which the membrane-spanning domain, residues 283-310, of the enzyme protein is deleted in the cDNA is expressed by baculovirus in the cytosol instead of in the microsomes and mitochondria of the Sf9 cells
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). 3BHS2_HUMAN
372
1
42052
Swiss-Prot
other Location (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
19000
-
4 * 19000, enzyme complex of 3beta-hydroxy-5-ene-steroid dehydrogenase and steroid DELTA-isomerase, SDS-PAGE
76000
-
enzyme complex of 3beta-hydroxy-5-ene-steroid dehydrogenase and steroid DELTA-isomerase, gel filtration
77000
-
enzyme complex of 3beta-hydroxy-5-ene-steroid dehydrogenase and steroid DELTA-isomerase gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
active enzyme, interface is composed of two pairs of helices related by a 2fold symmetry axis, involved residues, overview
dimer
tetramer
-
4 * 19000, enzyme complex of 3beta-hydroxy-5-ene-steroid dehydrogenase and steroid DELTA-isomerase, SDS-PAGE
dimer
active enzyme, interface is composed of two pairs of helices related by a 2fold symmetry axis, involved residues, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
GST A3-3 in complex with DELTA5-androstene-3,17-dione, using 100 mM Tris-HCl pH 7.8, 18% (v/v) PEG 4000, and 2 mM dithiothreitol
hanging-drop vapor diffusion method. The inability to crystallize the detergent-solubilized, wild-type microsomal enzyme is overcome by engineering a cytosolic form of this protein. Modified enzyme in which the membrane-spanning domain, residues 283-310 of the enzyme protein is deleted in the cDNA is expressed by baculovirus in the cytosol instead of in the microsomes and mitochondria of the Sf9 cells
-
identification of potentially critical residues M187 and S124 by docking of trilostane or 4alpha,5alpha-epoxy-testosterone into the active site
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H156Y
site-directed mutagenesis, leads to destabilization of interactions at the dimer interface and a dramatic increase in the substrate Km and inhibitor Ki values of 3beta-HSD isozyme 1 to equal those measured for 3beta-HSD isozyme 2
Q105M
site-directed mutagenesis, leads to destabilization of interactions at the dimer interface and a dramatic increase in the substrate Km and inhibitor Ki values of 3beta-HSD isozyme 1 to equal those measured for 3beta-HSD isozyme 2
D241N
-
mutant enzyme nearly has full isomerase activity, substantial decrease in 3beta-hydroxysteroid dehydrogenase activity. Mutant enzyme has a basal isomerase activity in the absence of coenzyme that is 10% of the NADH-stimulated turnover number
D257L
-
complete lack of isomerase activity in absence of coenzyme, substantial decrease in 3beta-hydroxysteroid dehydrogenase activity
D258L
-
complete lack of isomerase activity in absence of coenzyme, substantial decrease in 3beta-hydroxysteroid dehydrogenase activity
D265N
-
complete lack of isomerase activity in absence of coenzyme, substantial decrease in 3beta-hydroxysteroid dehydrogenase activity
D36A/K37R
-
mutation shifts the cofactor preference of both 3-beta-hydroxysteroid dehydrogenase and isomerase from NAD(H) to NADP(H)
DELTA283-310
-
the molecular weight of the subunit is 38800 Da compared to 42000 Da for the wild-type enzyme
E126L
site-directed mutagenesis, altered kinetics compared to the wild-type enzyme
H156Y
site-directed mutagenesis, leads to destabilization of interactions at the dimer interface and a dramatic increase in the substrate Km and inhibitor Ki values of 3beta-HSD isozyme 1 to equal those measured for 3beta-HSD isozyme 2
H232A
site-directed mutagenesis, altered kinetics compared to the wild-type enzyme
K158Q
site-directed mutagenesis, results in the complete loss of dehydrogenase activity and a reduction in isomerase activity, probably due to partial destabilization of cofactor binding, in which the catalytic triad is actively involved, and associated substrate binding
N100A
site-directed mutagenesis, altered kinetics compared to the wild-type enzyme
N100S
site-directed mutagenesis, altered kinetics compared to the wild-type enzyme
N323L
site-directed mutagenesis, altered kinetics compared to the wild-type enzyme
Q105M
site-directed mutagenesis, leads to destabilization of interactions at the dimer interface and a dramatic increase in the substrate Km and inhibitor Ki values of 3beta-HSD isozyme 1 to equal those measured for 3beta-HSD isozyme 2
S124A
site-directed mutagenesis, results in the complete loss of dehydrogenase activity and a reduction in isomerase activity, probably due to partial destabilization of cofactor binding, in which the catalytic triad is actively involved, and associated substrate binding
S322A
site-directed mutagenesis, altered kinetics compared to the wild-type enzyme
Y154F
site-directed mutagenesis, results in the complete loss of dehydrogenase activity and a reduction in isomerase activity, probably due to partial destabilization of cofactor binding, in which the catalytic triad is actively involved, and associated substrate binding
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme complex of 3beta-hydroxy-5-ene-steroid dehydrogenase and steroid 5 to 4 isomerase
-
modified enzyme in which the membrane-spanning domain, residues 283-310, of the enzyme protein is deleted in the cDNA is expressed by baculovirus in the cytosol instead of in the microsomes and mitochondria of the Sf9 cells
-
mutant enzymes D36A/K37R, D241N, D257L, D258L and D265N are expressed in a baculovirus/Sf9 cell system
-
recombinant type 1 isozyme, wild-type and mutant enzymes, from Spodoptera frugiperda Sf9 cells
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of type 1 isozyme, wild-type and mutant enzymes, in Spodoptera frugiperda Sf9 cells via baculovirus infection
mutant enzymes D36A/K37R, D241N, D257L, D258L and D265N are expressed in a baculovirus/Sf9 cell system
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Thomas, J.L.; Berko, E.A.; Faustino, A.; Myers, R.P.; Strickler, R.C.
Human placental 3beta-hydroxy-5-ene-steroid dehydrogenase and steroid 5-->4-ene-isomerase: purification from microsomes, substrate kinetics, and inhibition by product steroids
J. Steroid Biochem.
31
785-793
1988
Homo sapiens
Thomas, J.L.; Myers, R.P.; Strickler, R.C.
Human placental 3beta-hydroxy-5-ene-steroid dehydrogenase and steroid 5-->4-ene-isomerase: purification from mitochondria and kinetic profiles, biophysical characterization of the purified mitochondrial and microsomal enzymes
J. Steroid Biochem.
33
209-217
1989
Homo sapiens
Van Luu-The; Takahashi, M.; Labrie, F.
Differential inhibition of dehydrogenase and 5ene->4-ene isomerase activities of purified 3beta-hydroxysteroid dehydrogenase. Evidence for two distinct sites
J. Steroid Biochem. Mol. Biol.
40
545-548
1991
Homo sapiens
Dumont, M.; van Luu-The; Dupont, E.; Pelletier, G.; Llabrie, F.
Characterization, expression, and immunohistochemical localization of 3beta-hydroxysteroid dehydrogenase/DELTA5-DELTA4 isomerase in human skin
J. Invest. Dermatol.
99
415-421
1992
Homo sapiens
Thomas, J.L.; Mason, J.I.; Blanco, G.; Veisaga, M.L.
The engineered, cytosolic form of human type I 3beta-hydroxysteroid dehydrogenase/isomerase: purification, characterization and crystallization
J. Mol. Endocrinol.
27
77-83
2001
Homo sapiens
Thomas, J.L.; Duax, W.L.; Addlagatta, A.; Brandt, S.; Fuller, R.R.; Norris, W.
Structure/function relationships responsible for coenzyme specificity and the isomerase activity of human type 1 3 beta-hydroxysteroid dehydrogenase/isomerase
J. Biol. Chem.
278
35483-35490
2003
Homo sapiens
Thomas, J.L.; Boswell, E.L.; Scaccia, L.A.; Pletnev, V.; Umland, T.C.
Identification of key amino acids responsible for the substantially higher affinities of human type 1 3beta-hydroxysteroid dehydrogenase/isomerase (3b-HSD1) for substrates, coenzymes, and inhibitors relative to human 3b-HSD2
J. Biol. Chem.
280
21321-21328
2005
Homo sapiens
Pletnev, V.Z.; Thomas, J.L.; Rhaney, F.L.; Holt, L.S.; Scaccia, L.A.; Umland, T.C.; Duax, W.L.
Rational proteomics V: structure-based mutagenesis has revealed key residues responsible for substrate recognition and catalysis by the dehydrogenase and isomerase activities in human 3beta-hydroxysteroid dehydrogenase/isomerase type 1
J. Steroid Biochem. Mol. Biol.
101
50-60
2006
Homo sapiens (P14060), Homo sapiens (P26439), Homo sapiens
Thomas, J.L.; Mack, V.L.; Glow, J.A.; Moshkelani, D.; Terrell, J.R.; Bucholtz, K.M.
Structure/function of the inhibition of human 3beta-hydroxysteroid dehydrogenase type 1 and type 2 by trilostane
J. Steroid Biochem. Mol. Biol.
111
66-73
2008
Homo sapiens
EXTERNAL LINKS (specific for EC-Number 5.3.3.1)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
