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Information on EC 1.1.1.50 - 3alpha-hydroxysteroid 3-dehydrogenase (Si-specific) and Organism(s) Comamonas testosteroni and UniProt Accession P80702

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EC Tree
IUBMB Comments
The enzyme acts on androsterone and other 3alpha-hydroxysteroids and on 9-, 11- and 15-hydroxyprostaglandin. Si-specific with respect to NAD+ or NADP+. cf. EC 1.1.1.213, 3alpha-hydroxysteroid 3-dehydrogenase (Re-specific).
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Comamonas testosteroni
UNIPROT: P80702
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Word Map
The taxonomic range for the selected organisms is: Comamonas testosteroni
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
3 alpha-hydroxysteroid dehydrogenase, akr1c, hydroxyprostaglandin dehydrogenase, akr1c1-4, type i 3alpha-hsd, ps3alphahsd, bile-acid binding protein, 3alpha-hydroxysteroid dehydrogenase type 3, 3alpha-oxidoreductase, 3alpha-or, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3alpha-hydroxysteroid dehydrogenase
-
3alpha-hydroxysteroid dehydrogenase/carbonyl reductase
-
3-alpha-HSD
-
-
-
-
3alpha-hydroxysteroid dehydrogenase
-
-
3alpha-hydroxysteroid dehydrogenase/carbonyl reductase
-
-
HSD28
-
-
-
-
HSD29
-
-
-
-
hydroxyprostaglandin dehydrogenase
-
-
-
-
sterognost 3alpha dehydrogenase, 3alpha-hydroxy steroid
-
-
-
-
additional information
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a 3alpha-hydroxysteroid + NAD(P)+ = a 3-oxosteroid + NAD(P)H + H+
show the reaction diagram
a 3alpha-hydroxysteroid + NAD(P)+ = a 3-oxosteroid + NAD(P)H + H+
show the reaction diagram
the catalytic triad is composed of Ser-114, Tyr-155, and Lys-159, structural analysis and sequence alignment of the short chain dehydrogenase/reductase family
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
3alpha-hydroxysteroid:NAD(P)+ 3-oxidoreductase (Si-specific)
The enzyme acts on androsterone and other 3alpha-hydroxysteroids and on 9-, 11- and 15-hydroxyprostaglandin. Si-specific with respect to NAD+ or NADP+. cf. EC 1.1.1.213, 3alpha-hydroxysteroid 3-dehydrogenase (Re-specific).
CAS REGISTRY NUMBER
COMMENTARY hide
9028-56-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-decalol + NAD+
? + NADH + H+
show the reaction diagram
-
-
-
?
5alpha-androstan-3,17-dione + NADH + H+
androsterone + NAD+
show the reaction diagram
-
-
-
?
5alpha-androstane-3,17-dione + NADH + H+
androsterone + NAD+
show the reaction diagram
-
-
-
?
5beta-androstane-3,17-dione + NADH + H+
5beta-androstan-3alpha-ol-17-one + NAD+
show the reaction diagram
-
-
-
?
a 3alpha-hydroxysteroid + NAD+
a 3-oxosteroid + NADH + H+
show the reaction diagram
-
-
-
r
androstenol + NAD+
? + NADH + H+
show the reaction diagram
-
-
-
?
androsterone + NAD+
5alpha-androstan-3,17-dione + NADH + H+
show the reaction diagram
androsterone + NAD+
5alpha-androstane-3,17-dione + NADH + H+
show the reaction diagram
-
-
-
?
androsterone + NAD+
androstanedione + NADH
show the reaction diagram
androsterone + NAD+
androstanedione + NADH + H+
show the reaction diagram
cyclohexanol + NAD+
? + NADH + H+
show the reaction diagram
-
-
-
?
deoxycholic acid + NADH
12alpha-hydroxy-3-oxo-5beta-cholan-24-oic acid + NAD+
show the reaction diagram
-
-
-
r
5alpha-dihydrotestosterone + NAD(P)H + H+
(3beta,5alpha,17beta)-androstane-3,17-diol + NAD(P)+
show the reaction diagram
-
-
-
-
r
5alpha-dihydrotestosterone + NAD(P)H + H+
5alpha-androstan-3alpha,17beta-diol + NAD(P)+
show the reaction diagram
-
-
-
-
r
5beta-androstan-3,17-dione + NAD(P)H
5beta-androstan-17one-3-ol + NAD(P)+
show the reaction diagram
-
-
-
-
r
androsterone + NAD(P)+
5alpha-androstan-3,17-dione + NAD(P)H
show the reaction diagram
androsterone + NAD+
5alpha-androstane-3,17-dione + NADH
show the reaction diagram
-
-
-
-
r
androsterone + NAD+
androstanedione + NADH
show the reaction diagram
-
-
-
-
?
cholic acid + NAD(P)+
7alpha,12alpha-dihydroxy-3-oxo-5beta-cholan-24-oic acid + NAD(P)H
show the reaction diagram
-
-
-
-
r
fusidic acid + NAD+
?
show the reaction diagram
-
-
-
-
r
metapyrone + NADH
?
show the reaction diagram
-
-
-
-
?
oxidized 8-acetyl-2,3,5,6-tetrahydro-1H,4H-11-oxa-3a-azabenzo[de]anthracen-10-one + NAD(P)H
reduced 8-acetyl-2,3,5,6-tetrahydro-1H,4H-11-oxa-3a-azabenzo[de]anthracen-10-one + NAD(P)+
show the reaction diagram
-
synthetic compound with fluorophore core
-
-
r
p-nitrobenzaldehyde + NAD(P)H
p-nitrobenzylalcohol + NAD(P)+
show the reaction diagram
-
-
-
r
p-nitrobenzylalcohol + NAD+
p-nitrobenzaldehyde + NADH
show the reaction diagram
-
-
-
r
progesterone + NADH
?
show the reaction diagram
-
-
-
-
r
testosterone + NAD(P)+
androstenedione + NAD(P)H + H+
show the reaction diagram
-
-
-
-
r
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
a 3alpha-hydroxysteroid + NAD+
a 3-oxosteroid + NADH + H+
show the reaction diagram
-
-
-
r
androsterone + NAD+
5alpha-androstan-3,17-dione + NADH + H+
show the reaction diagram
-
-
-
r
androsterone + NAD+
androstanedione + NADH
show the reaction diagram
-
-
-
r
androsterone + NAD+
androstanedione + NADH + H+
show the reaction diagram
-
-
-
?
androsterone + NAD+
5alpha-androstane-3,17-dione + NADH
show the reaction diagram
-
-
-
-
r
additional information
?
-
the enzyme catalyzes reversibly the oxidoreduction of 3alpha-hydroxyl groups of steroid hormones
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
product inhibition
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-butyl-3-methylimidazolium L-lactate
1-ethyl-3-methylimidazolium trifluoromethanesulfonate
-
addition of the co-solvent leads to slightly enhanced enzyme activity n an aqueous-organic solvent system with Tris-HCl buffer, overview
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0012 - 0.007
5alpha-androstan-3,17-dione
0.0012 - 0.0031
5alpha-androstane-3,17-dione
0.0012 - 0.007
5beta-androstane-3,17-dione
0.0051 - 0.033
androsterone
0.00305 - 0.016
NAD+
0.004 - 0.029
NADH
0.007 - 0.0223
5alpha-dihydrotestosterone
0.0422
androstanedione
-
-
0.00044 - 0.1
androsterone
0.0184
cholic acid
-
-
0.0061
Fusidic acid
-
-
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.2
2-decalol
pH 10.5, 25°C
230
androstenol
pH 10.5, 25°C
500
androsterone
pH 10.5, 25°C
2.5
Cyclohexanol
pH 10.5, 25°C
0.02 - 63
NADH
0.0028 - 318
androsterone
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6.5 - 54000
5alpha-androstane-3,17-dione
3.8 - 15000
NADH
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0034 - 0.585
NADH
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0034 - 0.585
NADH
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15.4
recombinant untagged enzyme purified via deoxycholic acid affinity chromatography, pH 11.0, 25°C
3.94
recombinant His-tagged enzyme purified via Ni2+ affinity chromatography, pH 11.0, 25°C
119
-
androsteone, oxidation
2.5
-
fusidic acid, oxidation
27.4
-
cholic acid, oxidation
64.5
-
5alpha-dihydrotestosterone, reduction
7
-
commercially purified enzyme in Tris-HCl/co-solvent 1-butyl-3-methylimidazolium L-lactate at pH 7.6 and 25°C
85.7
-
androstanedione, reduction
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 11
-
pH profile, recombinant His-tagged wild-type and mutant enzymes
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
enzyme 3alpha-HSD/CR belongs to the short chain dehydrogenase/reductase (SDR) superfamily
malfunction
mutation at P185 in the hinge region and T188 in the loop causes a significant increase in the Kd value for NADH. Mutants P185A, P185G, T188A, and T188S show an increase the dissociation of the nucleotide cofactor, thereby increasing the rate of release of the product and producing the rate-limiting step in the hydride transfer
physiological function
replacement of hsdA gene by the green fluorescent protein gene inserted downstream from the hsdA regulatory region and use of the resulting strain as fluorescence based biosensor system for steroid determination. With this cell-based system testosterone can be determined in a range between 57 and 450 ng/ml, estradiol between 1.6 and 12.8 ng/ml, and cholesterol between 19.3 and 154.4 ng/nl. The sensitivity of this bioassay can be further increased by using only the cytosol of the mutant. With the resulting cell-free system testosterone is determined in a range between 28 and 219 pg/ml, estradiol between 0.029 and 0.430 fg/ml, and cholesterol between 9.7 and 77.2 fg/ml. The recovery ratio of the extraction is around 95% and the maximum fluorescence signals are obtained as early as after 30 min. Limitations of the established steroid biosensor system are quenching at higher steroid concentrations and the relatively high background of fluorescence
additional information
catalytic tetrad N86-S114-Y155-K159, catalytic roles of P185 and T188 and substrate-binding loop flexibility in 3alpha-hydroxysteroid dehydrogenase/carbonyl reductase. Structurally the substrate-binding loop of the residues, T188-K208, is unresolved, while binding with NAD+ causes the appearance of T188-P191 in the binary complex, functional roles of the flexible substrate-binding loop in conformational changes and enzyme catalysis, overview. Simulated molecular modeling gives results that are consistent with the conformational change in the substrate-binding loop after NAD+ binding. These results indicate that P185, T188 and the flexible substrate-binding loop are involved in binding with the nucleotide cofactor and with androsterone and are also involved in catalysis. Homology structure modeling, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DIDH_COMTE
257
0
26392
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
52000
calculated from amino acid sequence
56000
about, gel filtration, recombinant enzyme
100000
-
gel filtration, concentration dependent monomer-dimer association
26400
-
2 * 26400, SDS-PAGE and sequence analysis
47100
49400
-
gel filtration
70000
-
about, recombinant His-tagged wild-type and mutant enzymes, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
homodimer
non-covalent homodimer , 2 * 23000, about, recombinant enzyme, SDS-PAGE
dimer
monomer
-
1 * 47100, concentration dependent monomer-dimer association
additional information
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D249A
D249K
D249S
K159A
K159M
site-directed mutagenesis, the mutation changes the rate-limiting step to the hydride transfer, proton transfer is blocked in the mutant but can be rescued using exogenous proton acceptors, such as buffers, small primary amines, and azide, overview
P185A
site-directed mutagenesis, analysis of kinetics and structure compared to the wild-type enzyme
P185G
site-directed mutagenesis, analysis of kinetics and structure compared to the wild-type enzyme
S114A
T188A
site-directed mutagenesis, analysis of kinetics and structure compared to the wild-type enzyme
T188S
site-directed mutagenesis, analysis of kinetics and structure compared to the wild-type enzyme
W173F/P185W
site-directed mutagenesis, analysis of kinetics and structure compared to the wild-type enzyme
W173F/T188W
site-directed mutagenesis, analysis of kinetics and structure compared to the wild-type enzyme
Y155F
K159A
-
site-directed mutagenesis, the mutant shows altered kinetics and pH profile, and 200fold reduced activity compared to the wild-type
S114A
-
site-directed mutagenesis, the mutant shows altered kinetics and pH profile, and 3400fold reduced activity compared to the wild-type
S114A/Y155F
-
site-directed mutagenesis, the mutant shows altered kinetics and pH profile, and 200000fold reduced activity compared to the wild-type
Y155F
-
site-directed mutagenesis, the mutant shows altered kinetics and pH profile, and 2800fold reduced activity compared to the wild-type
Y155F/K159A
-
site-directed mutagenesis, the mutant shows altered kinetics and pH profile, and 9400fold reduced activity compared to the wild-type
additional information
construction of insertion mutants, overview
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
47.2
melting temperature, mutant D249S
47.9
melting temperature, mutant D249A
49.41
melting temperature, mutant D249K
54
the melting temperature of the wild type enzyme is at 54.76°C
54.8
melting temperature, wild-type
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
metal-chelate chromatography
Ni-NTA column chromatography
recombinant His-tagged and untagged enzyme from Escherchia coli strain BL21(DE3) nickel affinity chromatography, and by deoxycholic acid affinity chromatography, respectively, the latter to 94-98% purity. Deoxycholic acid is linked to the resin Sepharose 4B with the aid of the spacers as cyanuric chloride and ethanediamine. Adsorption analysis by adapting the adsorption isotherm to a specific binding model, the Scatchard analysis model, overview. Comparison of purification methods between synthetic affinity medium and Ni2+-Sepharose column
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli by nickel affinity chromatography
recombinant wild-type and mutant enzymes
recombinant wild-type and mutant enzymes ifrom Escherichia coli strain BL21(DE3)
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, and gel filtration to homogeneity
-
recombinant, His-tagged from Escherichia coli
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
D249A, D249S, and D249K mutants are expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21 (DE3) cells
expression in Escherichia coli
expression in Escherichia coli BL21 (DE3)
expression of His-tagged wild-type and mutant enzymes in Escherichia coli
expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
gene hsdA, recombinant expression of His-tagged and untagged enzyme in Escherchia coli strain BL21(DE3)
overexpression in Escherichia coli
recombinant expression of wild-type and mutant enzymes
overexpression as His-tagged fusion protein in Escherichia coli
-
overexpression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
several fold induction of expression in the presence of steroid substrates
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
thermal and urea-induced unfolding profiles for wild-type and mutant enzymes appear as a two-state transition and three-state transition, respectively
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
environmental protection
the mutant Comamonas testosteroni strain CT-GFP5-1 can be used as a sensitive biosensor system for steroid determination in the environment
synthesis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Skalhegg, B.A.
On the 3alpha-hydroxysteroid dehydrogenase from Pseudomonas testosteroni. Purification and properties
Eur. J. Biochem.
46
117-125
1974
Comamonas testosteroni
Manually annotated by BRENDA team
Skalhegg, B.A.
3alpha-Hydroxysteroid dehydrogenase from Pseudomonas testosteroni: kinetic properties with NAD and its thionicotinamide analogue
Eur. J. Biochem.
50
603-609
1975
Comamonas testosteroni
Manually annotated by BRENDA team
Jarabak, J.; Talalay, P.
Stereospecificity of hydrogen transfer by pyridine nucleotide-linked hydroxysteroid dehydrogenase
J. Biol. Chem.
235
2147-2151
1960
Comamonas testosteroni
Manually annotated by BRENDA team
Squire, P.G.; Dehlin, S.; Porath, J.
Physical and chemical characterization of hydroxysteroid dehydrogenases from Pseudomonas testosteroni
Biochim. Biophys. Acta
89
409-421
1964
Comamonas testosteroni
Manually annotated by BRENDA team
Maser, E.; Mobus, E.; Xiong, G.
Functional expression, purification, and characterization of 3alpha-hydroxysteroid dehydrogenase/Carbonyl reductase from Comamonas testosteroni
Biochem. Biophys. Res. Commun.
272
622-628
2000
Comamonas testosteroni
Manually annotated by BRENDA team
Yee, D.J.; Balsanek, V.; Sames, D.
New tools for molecular imaging of redox metabolism: development of a fluorogenic probe for 3a-hydroxysteroid dehydrogenases
J. Am. Chem. Soc.
126
2282-2283
2004
Comamonas testosteroni, Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Hwang, C.; Chang, Y.; Hsu, C.; Hsu, H.; Li, C.; Pon, H.
Mechanistic roles of Ser-114, Tyr-155, and Lys-159 in 3alpha-hydroxysteroid dehydrogenase/carbonyl reductase from Comamonas testosteroni
J. Biol. Chem.
280
3522-3528
2005
Comamonas testosteroni
Manually annotated by BRENDA team
Okochi, M.; Nakagawa, I.; Kobayashi, T.; Hayashi, S.; Furusaki, S.; Honda, H.
Enhanced activity of 3alpha-hydroxysteroid dehydrogenase by addition of the co-solvent 1-butyl-3-methylimidazolium (l)-lactate in aqueous phase of biphasic systems for reductive production of steroids
J. Biotechnol.
128
376-382
2006
Comamonas testosteroni
Manually annotated by BRENDA team
Chang, Y.H.; Chuang, L.Y.; Hwang, C.C.
Mechanism of proton transfer in the 3alpha-hydroxysteroid dehydrogenase/carbonyl reductase from Comamonas testosteroni
J. Biol. Chem.
282
34306-34314
2007
Comamonas testosteroni (P80702)
Manually annotated by BRENDA team
Hoffmann, F.; Sotriffer, C.; Evers, A.; Xiong, G.; Maser, E.
Understanding oligomerization in 3alpha-hydroxysteroid dehydrogenase/carbonyl reductase from Comamonas testosteroni: an in silico approach and evidence for an active protein
J. Biotechnol.
129
131-139
2007
Comamonas testosteroni (P80702)
Manually annotated by BRENDA team
Hwang, C.C.; Hsu, C.N.; Huang, T.J.; Chiou, S.J.; Hong, Y.R.
Interactions across the interface contribute the stability of homodimeric 3alpha-hydroxysteroid dehydrogenase/carbonyl reductase
Arch. Biochem. Biophys.
490
36-41
2009
Comamonas testosteroni (P80702)
Manually annotated by BRENDA team
Chang, Y.H.; Huang, T.J.; Chuang, L.Y.; Hwang, C.C.
Role of S114 in the NADH-induced conformational change and catalysis of 3alpha-hydroxysteroid dehydrogenase/carbonyl reductase from Comamonas testosteroni
Biochim. Biophys. Acta
1794
1459-1466
2009
Comamonas testosteroni (P80702)
Manually annotated by BRENDA team
Xiong, G.; Draus, E.; Luo, Y.; Maser, E.
3alpha-Hydroxysteroid dehydrogenase/carbonyl reductase as a tool for isolation and characterization of a new marine steroid degrading bacterial strain
Chem. Biol. Interact.
178
206-210
2009
Comamonas testosteroni
Manually annotated by BRENDA team
Xiong, G.; Luo, Y.; Jin, S.; Maser, E.
Cis- and trans-regulatory elements of 3alpha-hydroxysteroid dehydrogenase/carbonyl reductase as biosensor system for steroid determination in the environment
Chem. Biol. Interact.
178
215-220
2009
Comamonas testosteroni, Comamonas testosteroni (P80702)
Manually annotated by BRENDA team
Chang, Y.H.; Wang, C.Z.; Chiu, C.C.; Chuang, L.Y.; Hwang, C.C.
Contributions of active site residues to cofactor binding and catalysis of 3alpha-hydroxysteroid dehydrogenase/carbonyl reductase
Biochim. Biophys. Acta
1804
235-241
2010
Comamonas testosteroni (P80702)
Manually annotated by BRENDA team
Mundaca, R.A.; Moreno-Guzman, M.; Eguilaz, M.; Yanez-Sedeno, P.; Pingarron, J.M.
Enzyme biosensor for androsterone based on 3alpha-hydroxysteroid dehydrogenase immobilized onto a carbon nanotubes/ionic liquid/NAD+ composite electrode
Talanta
99
697-702
2012
Comamonas testosteroni (P80702)
Manually annotated by BRENDA team
Yang, H.; Fang, Y.; Wang, Z.; Zhang, L.
One step affinity recovery of 3alpha-hydroxysteroid dehydrogenase from cloned Escherichia coli
J. Chromatogr. B
991
79-84
2015
Comamonas testosteroni (P80702), Comamonas testosteroni ATCC 11996 (P80702)
Manually annotated by BRENDA team
Hwang, C.C.; Chang, Y.H.; Lee, H.J.; Wang, T.P.; Su, Y.M.; Chen, H.W.; Liang, P.H.
The catalytic roles of P185 and T188 and substrate-binding loop flexibility in 3alpha-hydroxysteroid dehydrogenase/carbonyl reductase from Comamonas testosteroni
PLoS ONE
8
e63594
2013
Comamonas testosteroni (P80702)
Manually annotated by BRENDA team
Hwang, C.C.; Chang, P.R.; Wang, T.P.
Contribution of remote substrate binding energy to the enzymatic rate acceleration for 3alpha-hydroxysteroid dehydrogenase/carbonyl reductase
Chem. Biol. Interact.
276
133-140
2017
Comamonas testosteroni (P80702)
Manually annotated by BRENDA team
Hwang, C.C.; Chang, P.R.; Hsieh, C.L.; Chou, Y.H.; Wang, T.P.
Thermodynamic analysis of remote substrate binding energy in 3alpha-hydroxysteroid dehydrogenase/carbonyl reductase catalysis
Chem. Biol. Interact.
302
183-189
2019
Comamonas testosteroni (P80702)
Manually annotated by BRENDA team