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1.1.1.50: 3alpha-hydroxysteroid 3-dehydrogenase (Si-specific)

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

Word Map on EC 1.1.1.50

Reaction

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

Synonyms

3 alpha-hydroxysteroid dehydrogenase, 3 alphaHD, 3-alpha hydroxysteroid dehydrogenase type 3, 3-alpha-HSD, 3alpha-HSD, 3alpha-HSD/CR, 3alpha-HSD3, 3alpha-HSOR, 3alpha-hydroxysteroid dehydrogenase, 3alpha-hydroxysteroid dehydrogenase type 3, 3alpha-hydroxysteroid dehydrogenase/carbonyl reductase, 3alpha-hydroxysteroid oxido-reductase, 3alpha-hydroxysteroid oxidoreductase, 3alpha-hydroxysteroid-5beta-oxidoreductase, 3alpha-OR, 3alpha-oxidoreductase, 3alpha/3beta-hydroxysteroid dehydrogenase, 3alphaHSD, 3HSD, 5alpha-dihydroprogesterone 3alpha-hydroxysteroid oxidoreductase, AKR1C, AKR1C1, AKR1C1-4, AKR1C14, AKR1C17, AKR1C2, AKR1C3, AKR1C4, AKR1C9, aldo-keto reductase 1C2, bile-acid binding protein, chlordecone reductase, DD2, DD21, dihydrodiol dehydrogenase, HSD, HSD28, HSD29, hsdA, HSDH, hydroxyprostaglandin dehydrogenase, More, NAD(P)+-3alpha-hydroxysteroid dehydrogenase, NAD+-dependent 3alpha-HSD, NADP(H)-dependent 3alpha-HSD, NADPH:5alpha-dihydroprogesterone 3alpha-hydroxysteroid oxidoreductase, prostaglandin F2alpha-synthase, Ps3alphaHSD, PT3HSD, sterognost 3alpha dehydrogenase, 3alpha-hydroxy steroid, type 2 3alpha-hydroxysteroid dehydrogenase/type 5 17beta-hydroxysteroid dehydrogenase, type 3 3alpha-hydroxysteroid dehydrogenase, type 5 17beta-hydroxysteroid dehydrogenase, type I 3alpha-HSD

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.50 3alpha-hydroxysteroid 3-dehydrogenase (Si-specific)

Engineering

Engineering on EC 1.1.1.50 - 3alpha-hydroxysteroid 3-dehydrogenase (Si-specific)

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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
S114A/Y155F
-
site-directed mutagenesis, the mutant shows altered kinetics and pH profile, and 200000fold reduced activity compared to the wild-type
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
Y155F/K159A
-
site-directed mutagenesis, the mutant shows altered kinetics and pH profile, and 9400fold reduced activity compared to the wild-type
V54L
site-directed mutagenesis, the change renders the sequence identical to that of human 20-alpha hydroxysteroid dehydrogenase. The V54L mutation directly restricts the steroid binding modes to a unique one, which resembles the orientation of 20alpha-OHProg within human 20alpha-HSD. The kinetic study shows that the V54L mutation significantly decreases the 3alpha-HSD activity for the reduction of 5alpha-dihydrotestosterone, while this mutation enhances the 20alpha-HSD activity to convert progesterone
K157A
the NADH binding affinity of K157A mutant is much lower than that of the wild-type, mainly due to loss of a hydrogen bond
S114A
mutant shows higher Km and lower kcat values in both oxidation and reduction reactions
S114A/Y153F
double mutation results in a significant decrease in kcat relative to the single mutant Y153F
Y153F
mutant shows higher Km and lower kcat values in both oxidation and reduction reactions. Loss of hydrogen bonding with NADH upon the Y153F mutation results in increased enthalpy change
E276R
-
site-directed mutagenesis, the mutation alters the cofactor specificity of AKR1C17 from NAD+ to NADP+, the switch is analogy th the residues of AKR1C9 and its cofactor specificity, overview
F118A
F129A
-
site-directed mutagenesis, mutation of a substrate binding residue, altered steroid recognition and kinetics compared to the wild-type enzyme, highly reduced activity
N306A
Q270K
-
site-directed mutagenesis, the mutation alters the cofactor specificity of AKR1C17 from NAD+ to NADP+, the switch is analogy th the residues of AKR1C9 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 AKR1C9 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
R276M
-
site-directed mutagenesis, the mutant shows slightly increased preference for the reduction reaction compared to the wild-type enzyme
T226A
W227A
Y310A
additional information