1.1.1.213: 3alpha-hydroxysteroid 3-dehydrogenase (Re-specific)

This is an abbreviated version, for detailed information about 3alpha-hydroxysteroid 3-dehydrogenase (Re-specific), go to the full flat file.

Reaction

a 3alpha-hydroxysteroid
+
NAD(P)+
=
a 3-oxosteroid
+
NAD(P)H
+
H+

Synonyms

17beta-hydroxysteroid dehydrogenase type 5, 3-alpha hydroxysteroid oxidoreductase, 3-alpha-HSO, 3alpha-HSD, 3alpha-HSD type 3, 3alpha-HSD/CR, 3alpha-HSD3, 3alpha-HSOR, 3alpha-hydroxysteroid dehydrogenase, 3alpha-hydroxysteroid dehydrogenase (B-specific), 3alpha-hydroxysteroid dehydrogenase type 2, 3alpha-hydroxysteroid dehydrogenase/carbonyl reductase, 3alpha-hydroxysteroid oxido-reductase, 3alpha-hydroxysteroid oxidoreductase, 3alpha-hydroxysteroid:NAD(P) oxidoreductase, 3alphaHSD, A-specific 3alpha-hydroxysteroid dehydrogenase, AKR1C17, AKR1C2, AKR1C3, AKR1C4, AKR1C9, alpha-HSD/CR, B-specific 3alpha-hydroxysteroid dehydrogenase, bile acid-binding protein, DD2, dihydrodiol dehydrogenase, HSDH, More, NAD+-dependent 3alpha-HSD, NADP(H)-dependent 3alpha-HSD, type 2 3alpha-hydroxysteroid dehydrogenase/type 5 17beta-hydroxysteroid dehydrogenase, type 3 3-alpha-hydroxysteroid dehydrogenase, type 3 3alpha-HSD, type 3 3alpha-hydroxysteroid dehydrogenase, type 5 beta-hydroxysteroid dehydrogenase

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.213 3alpha-hydroxysteroid 3-dehydrogenase (Re-specific)

Engineering

Engineering on EC 1.1.1.213 - 3alpha-hydroxysteroid 3-dehydrogenase (Re-specific)

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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
S114A
-
site-directed mutagenesis, altered kinetics in comparison to the wild-type enzyme
S114A/Y155F
-
site-directed mutagenesis, altered kinetics in comparison to the wild-type enzyme
Y155F
-
site-directed mutagenesis, altered kinetics in comparison to the wild-type enzyme
Y155F/K159A
-
site-directed mutagenesis, altered kinetics in comparison to the wild-type enzyme
R301L
-
site-directed mutagenesis, the mutation greatly affects the 3alpha-hydroxysteroid dehydrogenase activity towards 5alpha-dihydrotestosterone and almost completely abolishes the 17beta-hydroxysteroid dehydrogenase activity of the enzyme
R304L
-
site-directed mutagenesis, the mutation greatly affects the 3alpha-hydroxysteroid dehydrogenase activity towards 5alpha-dihydrotestosterone and abolishes the 17beta-hydroxysteroid dehydrogenase activity of the enzyme
C217A
-
resistant to inactivation by secosteroids, therefore Cys217 is the point of covalent attachment of acetylenic ketones
D50E
-
1/30th catalytic efficiency of wild type, unlikely to be the general amino acid for catalysis
D50N
-
1/30th catalytic efficiency of wild type, unlikely to be the general amino acid for catalysis
E276R
-
site-directed mutagenesis, the mutation alters the cofactor specificity of AKR1C17 from NAD+ to NADP+, the switch is analogy th the residues of AKRc9 and its cofactor specificity, overview
H117A
-
1/500th catalytic efficiency of wild type, unlikely to be the general amino acid for catalysis
K84M
-
inactive, unable to bind steroids
K84R
-
inactive, unable to bind steroids
N167A
-
site-directed mutagenesis, most impaired enzyme
Q190A
-
site-directed mutagenesis, decreased binding affinity to NADP(H), only binding of cofactor is affected, residue is located at the catalytic cente
Q270K
-
site-directed mutagenesis, the mutation alters the cofactor specificity of AKR1C17 from NAD+ to NADP+, the switch is analogy th the residues of AKRc9 and its cofactor specificity, overview
Q270K/E276R
-
site-directed mutagenesis, the mutation alters the cofactor specificity of AKR1C17 from NAD+ to NADP+, the switch is analogy th the residues of AKRc9 and its cofactor specificity, overview
R276E
-
site-directed mutagenesis, the mutant shows increased preference for the oxidation reaction compared to the wild-type enzyme
R276G
-
site-directed mutagenesis, the mutant shows slightly increased preference for the reduction reaction compared to the wild-type enzyme
S166A
-
site-directed mutagenesis, decreased binding affinity to NADP(H), only binding of cofactor is affected, residue is located at the catalytic center
Y205F
-
kinetically indistinguishable from the wild type, no general amino acid for catalysis in 3alpha-hydroxysteroid dehydrogenase
Y216S
-
site-directed mutagenesis, decreased binding affinity to NADP(H), only binding of cofactor is affected, residue is located at the catalytic cente
Y55F
-
inactive, unable to perform steroid oxidoreduction, strongest candidate for the general amino acid
Y55S
-
inactive, strongest candidate for the general amino acid
additional information