1.1.1.149: 20alpha-hydroxysteroid dehydrogenase

This is an abbreviated version, for detailed information about 20alpha-hydroxysteroid dehydrogenase, go to the full flat file.

Reaction

17alpha,20alpha-dihydroxypregn-4-en-3-one
+
NAD(P)+
=
17alpha-hydroxyprogesterone
+
NAD(P)H
+
H+

Synonyms

20-alpha-HSD, 20-alpha-hydroxysteroid dehydrogenase, 20alpha-HSD, 20alpha-HSDH, 20alpha-hydroxy steroid dehydrogenase, 20alpha-hydroxysteroid dehydrogenase, 20alpha-hydroxysteroid oxidoreductase, 20alpha-OH-SDH, AKR1C1, AKR1C23, AKR1C3, aldo-keto reductase family 1 member C1, HSD1

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.149 20alpha-hydroxysteroid dehydrogenase

Crystallization

Crystallization on EC 1.1.1.149 - 20alpha-hydroxysteroid dehydrogenase

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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure of AKR1C1 complexed with the first structure-based designed inhibitor 3-chloro-5-phenylsalicylic acid bound in the active site is reported. The binding of 3-chloro-5-phenylsalicylic acid to AKR1C1 results in a conformational change in the side chain of Phe311 to accommodate the bulky phenyl ring substituent at the 5-position of the inhibitor
-
docking model with substrates 5alpha-pregnane-3alpha,20alpha-diol and 5beta-pregnan-3alpha-ol-20-one. In the docked model of 5alpha-pregnane-3alpha,20alpha-diol the conformation of the steroid molecule is similar to that of 20alpha-hydroxyprogesterone in the crystal structure of the AKR1C1 complex where the steroid does not interact with the catalytic residues Tyr55 and His117. In the case of 5beta-pregnan-3alpha-ol-20-one the steroid interacts with the catalytic residue His117 and forms close contacts with Leu308
-
in complex with NADP+ and progesterone; purified recombinant enzyme in complex with cofactor and several substrates, hanging drop vapour diffusion method, 4°C, HEPES or sodium acetate buffer, CaCl2, precipitant is PEG 4000, X-ray diffraction structure determination and analysis at 2.4-2.5 A resolution
-
in ternary complex with NADP+ and 3,5-dichlorosalicylic acid, hanging drop vapour diffusion method, using 25% (v/v) polyethylene glycol monomethyl ether 550, 0.02 M zinc sulfate in 0.1 M MES buffer (pH 6.5)
-
mutant L308V in complex with the inhibitor 3,5-dichlorosalicylic acid, to 1.9 A resolution. The inhibitor molecule is anchored from its carboxylate group that forms hydrogen bonds with the catalytic residues His117 and Tyr55, while the hydroxyl group is hydrogen bonded to His222. Van der Waals contacts are present between the inhibitor and residues Leu54, Leu306, and Phe311. Unlike the WT enzyme, the side-chain of the mutated Val308 makes long contacts with the inhibitor, the closest point of contact being 3.9 A
-
ternary complex with NADP+ and 20alpha-hydroxyprogesterone
-
in complex with NADP+ and progesterone, with NADP+ and dihydrotestosterone, with NADP+ and 4-androstenedione; purified recombinant enzyme in complex with cofactor and several substrates, hanging drop vapour diffusion method, 4°C, HEPES or sodium acetate buffer, CaCl2, precipitant is PEG 4000, X-ray diffraction structure determination and analysis at 1.7-1.9 A resolution
-
isozyme HSD1, HSD2
-