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2-decalol + NAD+
? + NADH + H+
-
-
-
?
5alpha-androstan-3,17-dione + NADH + H+
androsterone + NAD+
-
-
-
?
5alpha-androstane-3,17-dione + NADH + H+
androsterone + NAD+
-
-
-
?
5beta-androstane-3,17-dione + NADH + H+
5beta-androstan-3alpha-ol-17-one + NAD+
-
-
-
?
a 3alpha-hydroxysteroid + NAD+
a 3-oxosteroid + NADH + H+
-
-
-
r
androstenol + NAD+
? + NADH + H+
-
-
-
?
androsterone + NAD+
5alpha-androstan-3,17-dione + NADH + H+
androsterone + NAD+
5alpha-androstane-3,17-dione + NADH + H+
-
-
-
?
androsterone + NAD+
androstanedione + NADH
androsterone + NAD+
androstanedione + NADH + H+
cyclohexanol + NAD+
? + NADH + H+
-
-
-
?
deoxycholic acid + NADH
12alpha-hydroxy-3-oxo-5beta-cholan-24-oic acid + NAD+
-
-
-
r
5alpha-dihydrotestosterone + NAD(P)H + H+
(3beta,5alpha,17beta)-androstane-3,17-diol + NAD(P)+
-
-
-
-
r
5alpha-dihydrotestosterone + NAD(P)H + H+
5alpha-androstan-3alpha,17beta-diol + NAD(P)+
-
-
-
-
r
5beta-androstan-3,17-dione + NAD(P)H
5beta-androstan-17one-3-ol + NAD(P)+
-
-
-
-
r
androsterone + NAD(P)+
5alpha-androstan-3,17-dione + NAD(P)H
androsterone + NAD+
5alpha-androstane-3,17-dione + NADH
-
-
-
-
r
androsterone + NAD+
androstanedione + NADH
-
-
-
-
?
cholic acid + NAD(P)+
7alpha,12alpha-dihydroxy-3-oxo-5beta-cholan-24-oic acid + NAD(P)H
-
-
-
-
r
fusidic acid + NAD+
?
-
-
-
-
r
metapyrone + NADH
?
-
-
-
-
?
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)+
-
synthetic compound with fluorophore core
-
-
r
p-nitrobenzaldehyde + NAD(P)H
p-nitrobenzylalcohol + NAD(P)+
-
-
-
r
p-nitrobenzylalcohol + NAD+
p-nitrobenzaldehyde + NADH
-
-
-
r
progesterone + NADH
?
-
-
-
-
r
testosterone + NAD(P)+
androstenedione + NAD(P)H + H+
-
-
-
-
r
additional information
?
-
androsterone + NAD+
5alpha-androstan-3,17-dione + NADH + H+
-
-
-
?
androsterone + NAD+
5alpha-androstan-3,17-dione + NADH + H+
-
-
-
r
androsterone + NAD+
5alpha-androstan-3,17-dione + NADH + H+
rate-limiting step in the reaction is the release of NADH
-
-
r
androsterone + NAD+
androstanedione + NADH
-
-
-
r
androsterone + NAD+
androstanedione + NADH
the intramolecular proton transfer is a rate-limiting step, with a concomitant releasing of protons to bulk solvent
-
-
r
androsterone + NAD+
androstanedione + NADH + H+
-
-
-
?
androsterone + NAD+
androstanedione + NADH + H+
the enzyme uses remote binding interactions to accelerate the reaction of androsterone with NAD+. The remote non-reacting sites of androsterone may induce a conformational change of the substrate binding loop with an entropic cost for better interaction with the transition state to decrease the enthalpy of activation, significantly increasing catalytic efficiency
-
-
?
androsterone + NAD+
androstanedione + NADH + H+
the rate limiting step is the release of NADH
-
-
?
androsterone + NAD+
androstanedione + NADH + H+
thermodynamic analysis of remote substrate binding energy. The remote non-reacting sites of androsterone may induce a conformational change of the substrate binding loop with an entropic cost for better interaction with the transition state to decrease the enthalpy of activation, significantly increasing catalytic efficiency
-
-
?
androsterone + NAD(P)+
5alpha-androstan-3,17-dione + NAD(P)H
-
-
-
-
r
androsterone + NAD(P)+
5alpha-androstan-3,17-dione + NAD(P)H
-
i.e. 3alpha-hydroxy-5alpha-androstan-17-one
-
-
r
androsterone + NAD(P)+
5alpha-androstan-3,17-dione + NAD(P)H
-
i.e. 3alpha-hydroxy-5alpha-androstan-17-one
-
r
additional information
?
-
the enzyme catalyzes reversibly the oxidoreduction of 3alpha-hydroxyl groups of steroid hormones
-
-
?
additional information
?
-
-
bifunctional enzyme also catalyzing the reaction of carbonyl reductase, EC 1.1.1.184
-
-
?
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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
0.007 - 0.0223
5alpha-dihydrotestosterone
0.0422
androstanedione
-
-
0.00044 - 0.1
androsterone
additional information
additional information
-
0.0012
5alpha-androstan-3,17-dione
wild-type, pH 7.5, 25°C
0.0012
5alpha-androstan-3,17-dione
wild type enzyme, in 0.1 M HEPES at pH 7.5
0.0022
5alpha-androstan-3,17-dione
mutant N86A, pH 7.5, 25°C
0.0031
5alpha-androstan-3,17-dione
mutant enzyme S114A, in 0.1 M HEPES at pH 7.5
0.005
5alpha-androstan-3,17-dione
mutant Y155F, pH 7.5, 25°C
0.007
5alpha-androstan-3,17-dione
mutant K159A, pH 7.5, 25°C
0.0012
5alpha-androstane-3,17-dione
wild-type, pH 7.5, 25°C
0.0031
5alpha-androstane-3,17-dione
mutant S114A, pH 7.5, 25°C
0.0012
5beta-androstane-3,17-dione
wild-type, pH 7.5, 25°C
0.0022
5beta-androstane-3,17-dione
mutant N86A, pH 7.5, 25°C
0.005
5beta-androstane-3,17-dione
mutant Y155F, pH 7.5, 25°C
0.007
5beta-androstane-3,17-dione
mutant K159A, pH 7.5, 25°C
0.0051
androsterone
pH 10.4, 25°C, recombinant wild-type enzyme
0.033
androsterone
pH 10.4, 25°C, recombinant mutant K159A
0.00305
NAD+
mutant D249S, pH 10.2, 25°C
0.0038
NAD+
wild type enzyme, in 0.1 M CAPS buffer, at pH 10.2, at 25°C
0.0038
NAD+
wild-type, pH 10.2, 25°C
0.005
NAD+
mutant enzyme D249S, in 0.1 M CAPS buffer, at pH 10.2, at 25°C
0.009
NAD+
mutant enzyme D249K, in 0.1 M CAPS buffer, at pH 10.2, at 25°C
0.009
NAD+
mutant D249K, pH 10.2, 25°C
0.016
NAD+
mutant enzyme D249A, in 0.1 M CAPS buffer, at pH 10.2, at 25°C
0.016
NAD+
mutant D249A, pH 10.2, 25°C
0.004
NADH
wild-type, pH 7.5, 25°C
0.004
NADH
wild type enzyme, in 0.1 M HEPES at pH 7.5
0.0065
NADH
mutant enzyme S114A, in 0.1 M HEPES at pH 7.5
0.0065
NADH
mutant S114A, pH 7.5, 25°C
0.01
NADH
mutant N86A, pH 7.5, 25°C
0.029
NADH
mutant Y155F, pH 7.5, 25°C
0.007 - 0.0083
5alpha-dihydrotestosterone
-
also in this range: androstanedione
0.0223
5alpha-dihydrotestosterone
-
-
0.00044
androsterone
-
pH 9.0, 25°C, recombinant His-tagged mutant S114A/Y155F
0.0055
androsterone
-
pH 9.0, 25°C, recombinant His-tagged wild-type
0.007
androsterone
-
pH 9.0, 25°C, recombinant His-tagged mutant S114A
0.065
androsterone
-
pH 9.0, 25°C, recombinant His-tagged mutant K159A
0.074
androsterone
-
pH 9.0, 25°C, recombinant His-tagged mutant Y155F
0.1
androsterone
-
pH 9.0, 25°C, recombinant His-tagged mutant Y155F/K159A
additional information
additional information
kinetics of wild-type and mutant enzymes in presence or absence of CAPS and methylamine, overview
-
additional information
additional information
steady-state kinetics, and stopped-flow study, kinetics of enzyme mutants P185A, P185G, T188A, and T188S showing an increase in kcat, Ka drosterone and KiNAD and equal primary isotope effects of DV and D(V/K)
-
additional information
additional information
-
steady-state kinetics
-
additional information
additional information
-
kinetics in absence and presence of co-solvents, overview
-
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homodimer
non-covalent homodimer , 2 * 23000, about, recombinant enzyme, SDS-PAGE
monomer
-
1 * 47100, concentration dependent monomer-dimer association
dimer
x-ray crystallography
dimer
the dimerization takes place via an interface axis. The formation of a tetramer is blocked in 3alpha-HSD/CR by the presence of a predominantly alpha-helical subdomain which is missing in all other SDRs of known structure, overview
dimer
-
2 * 47100, concentration dependent monomer-dimer association
dimer
-
2 * 26400, SDS-PAGE and sequence analysis
dimer
-
2 * 28349-28425, recombinant His-tagged wild-type and mutant enzymes, mass spectrometry
additional information
domain structure, the enzyme possessses a 28 amino acids insertion into the classical Rossmann-fold motif between strand betaE and helix alphaF, preventing the formation of a four helix bundle and enables the dimerization via a P-axis interface, structure homology modelling and simulation, structure comparison, overview
additional information
concentration-dependent dimerization. The calculated molecular masses through gel filtration chromatography for wild-type, mutants D249A, D249K, and D249S at the concentration of 1 mg/ml are 52, 42, 43, and 50 kDa, and change to 47, 25, 26, and 34 kDa at 0.01 mg/ml, respectively
additional information
secondary structures of the wild-type and mutants of P185A, P185G, T188A and T188S 3alpha-HSD/CRs are assessed by CD spectroscopy by measuring the ellipticity in the 190-250 nm range at room temperature
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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
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
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
D249A
the mutation leads to 2fold increased Km value compared to the wild type, the mutant shows increased retention time, suggesting a smaller molecule size than dimeric wild type enzyme
D249A
mutation interrupts salt bridge between residues D249 and R167, secondary structure similar to wild-type. 30fold decrease in catalytic efficiency, decrease in melting temperature
D249K
he mutation leads to 4fold increased Km value compared to the wild type, the mutant shows increased retention time, suggesting a smaller molecule size than dimeric wild type enzyme
D249K
mutation interrupts salt bridge between residues D249 and R167, secondary structure similar to wild-type. 1.4fold decrease in catalytic efficiency, decrease in melting temperature
D249S
the mutant has similar kinetic parameters to wild type enzyme
D249S
mutation interrupts salt bridge between residues D249 and R167, secondary structure similar to wild-type. 1400fold decrease in catalytic efficiency, decrease in melting temperature
K159A
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
K159A
decrease in the catalytic constant by 56fold and increase in the dissociation constant by 75fold. The enzyme-bound NADH decreases the fluorescence anisotropy value in the decreasing order WT, N86A, Y155F, K159A, indicating an increase in the mobility of the bound NADH for the mutants. Hydrogen bonding with the hydroxyl group of nicotinamide ribose by K159 and Y155 is important to maintain the orientation of NADH and contributes greatly to the transition-state binding energy to facilitate the catalysis
K159A
decrease in catalytic constant and increase in the dissociation constant. The enzyme-bound NADH decreases the fluorescence anisotropy value in the decreasing order WT, N86A, Y155F, K159A, indicating an increase in the mobility of the bound NADH for the mutants. Hydrogen bonding with the hydroxyl group of nicotinamide ribose by residues K159 and Y155 is important to maintain the orientation of NADH and contributes greatly to the transition-state binding energy to facilitate the catalysis. Residue N86 is important for stabilizing the position of K159
N86A
decrease in the catalytic constant by 37fold and increase in the dissociation constant by 8fold. The enzyme-bound NADH decreases the fluorescence anisotropy value in the decreasing order WT, N86A, Y155F, K159A, indicating an increase in the mobility of the bound NADH for the mutants. Residue N86 is important for stabilizing the position of K159
N86A
decrease in catalytic constant and increase in the dissociation constant. The enzyme-bound NADH decreases the fluorescence anisotropy value in the decreasing order WT, N86A, Y155F, K159A, indicating an increase in the mobility of the bound NADH for the mutants. Hydrogen bonding with the hydroxyl group of nicotinamide ribose by residues K159 and Y155 is important to maintain the orientation of NADH and contributes greatly to the transition-state binding energy to facilitate the catalysis. Residue N86 is important for stabilizing the position of K159
S114A
the mutation eliminates the hydrogen bonding interaction with P185, causing a conformational change in a nonproductive binding of NADH and a significant loss of activity, the mutant enzyme decreases 3100fold in V/Et value with no apparent change in Km value for substrates
S114A
mutant enzyme exhibits a pronounced increase in the magnitude of ellipticity at 222 nm. S114A mutant enzyme decreases 3100fold in catalytic efficiency with no apparent change in Km for substrates. Addition of NADH to S114A mutant enzyme induces a secondary structural change
Y155F
decrease in the catalytic constant by 220fold and increase in the dissociation constant by 3fold. The enzyme-bound NADH decreases the fluorescence anisotropy value in the decreasing order WT, N86A, Y155F, K159A, indicating an increase in the mobility of the bound NADH for the mutants. Hydrogen bonding with the hydroxyl group of nicotinamide ribose by K159 and Y155 is important to maintain the orientation of NADH and contributes greatly to the transition-state binding energy to facilitate the catalysis
Y155F
decrease in catalytic constant and increase in the dissociation constant. The enzyme-bound NADH decreases the fluorescence anisotropy value in the decreasing order WT, N86A, Y155F, K159A, indicating an increase in the mobility of the bound NADH for the mutants
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Skalhegg, B.A.
On the 3alpha-hydroxysteroid dehydrogenase from Pseudomonas testosteroni. Purification and properties
Eur. J. Biochem.
46
117-125
1974
Comamonas testosteroni
brenda
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
brenda
Jarabak, J.; Talalay, P.
Stereospecificity of hydrogen transfer by pyridine nucleotide-linked hydroxysteroid dehydrogenase
J. Biol. Chem.
235
2147-2151
1960
Comamonas testosteroni
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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)
brenda
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)
brenda
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)
brenda
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)
brenda
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
brenda
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)
brenda
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)
brenda
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)
brenda
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)
brenda
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)
brenda
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)
brenda
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)
brenda