Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

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)

Crystallization

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

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
3alpha-HSD3-NADP+-progesterone complex and 3alpha-HSD3 mutant V54L-NADP+-progesterone complex, sitting drop vapor diffusion method, room temperature, the reservoir solution contains 100 mM sodium cacodylate, pH 6.0, 200 mM ammonium sulfate, 24-26% w/v PEG 3350, with 0.8 mM progesterone, 3-14 days, X-ray diffraction structure determination and analysis at 2.0-2.2 A resolution, molecular replacement with search model, PDB ID 1J96. Progesterone adopts two different binding modes to form complexes within the wild-type enzyme, with one binding mode similar to the orientation of a bile acid (ursodeoxycholate) in the reported ternary complex of human 3alpha-HSD3-NADP+-ursodeoxycholate and the other binding mode resembling the orientation of 20alpha-OHProg in the ternary complex of human 20alpha-HSD-NADP+-20alpha-OHProg
alpha/beta-barrel, NADP+ is bound in an extended conformation, type III isoform
-
crystal structure of human 3alpha-HSD3-NADP(+)/5alpha-androstane-3,17-dione/epiandrosterone complex obtained by co-crystallization with 5alpha-androstane-3,17-dione (5alpha-DHT) in the presence of NADP+. Although 5alpha-DHT is introduced during the crystallization, oxidoreduction of 5alpha-DHT occurs. The locations of 5alpha-androstane-3,17-dione and epiandrosterone are identified in the steroid-binding sites of two 3alpha-HSD3 molecules per crystal asymmetric unit. An overlay shows that 5alpha-androstane-3,17-dione and epiandrosterone are oriented upside-down and flipped relative to each other, providing structural clues for 5alpha-DHT reverse binding in the enzyme with the generation of different products
isozyme AKR1C2 in ternary complex with NADP+ and ursodeoxycholate, X-ray diffraction structure determination and analysis at 3.0 A resolution, molecular replacement
-
recombinant type 3 isozyme AKR1C2 in complex with NADP+ and ursodeoxycholate, X-ray structure determination and analysis at 3.0 A resolution
-
type III isoform
-
association to dimer during crystallization
-
purified enzyme with NADH, hanging drop vapour diffusion method, 4°C, in presence of 1.4 M ammonium sulfate, 0.14 M NaCl, and 0.1 M Tris, pH 9.0, rod cluster crystals appear within 1 week, X-ray diffraction structure determination and analysis at 1.8 A resolution, modeling
purified recombinant enzyme in complex with NADH, hanging drop vapour diffusion method and microseeding, 0.002 ml of protein solution with 0.3 mM 3alpha-HSD and 0.4 mM NADH in 10 mM Tris–HCl pH 8.0, are mixed with 0.002 ml reservoir solution optimally containing 0.1 M Tris–HCl, pH 9.0, 0.14 M sodium chloride and 1.4 M ammonium sulfate, 4°C, X-ray diffraction structure determination and analysis at 1.8 A resolution
-
isozyme AKR1C9 in ternary complex with NADP+ and ursodeoxycholate, X-ray diffraction structure determination and analysis at 2.8 A resolution
-