1.1.1.239: 3alpha(17beta)-hydroxysteroid dehydrogenase (NAD+)

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For detailed information about 3alpha(17beta)-hydroxysteroid dehydrogenase (NAD+), go to the full flat file.

Reaction

Synonyms

17-ketoreductase, 17beta-HSD, 17beta-hydroxysteroid dehydrogenase type 5, 3,17beta-HSD, 3,17beta-hydroxysteroid dehydrogenase, 3alpha(17beta)-HSD, 3alpha(17beta)-hydroxysteroid dehydrogenase, AKR1C26, AKR1C27, AKR1C28, AKR1C3, AKR1C34, aldo-keto reductase 1C3, dehydrogenase, 3alpha,17beta-hydroxy steroid, EC 1.1.1.63, More, NAD+-dependent 3alpha(17beta)-hydroxysteroid dehydrogenase, NAD+-dependent 3beta(17beta)-hydroxysteroid dehydrogenase, NAD+-linked S-tetralol dehydrogenase, PGER6, type 2 3alpha-HSD, type 2 3alpha-hxdroxysteroid dehydrogenase/type 5 17beta-hydroxysteroid dehydrogenase, type 2 3alppha-hydroxysteroid dehydrogenase/type 5 17beta-hydroxysteroid dehydrogenase, type 3 17beta-hydroxysteroid dehydrogenase, type 5 17beta-HSD, type 5 17beta-hydroxysteroid dehydrogenase, type 5 17beta-hydroxysteroid dehydrogenase/prostaglandin F synthase, 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

                1.1.1.239 3alpha(17beta)-hydroxysteroid dehydrogenase (NAD+)

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Results	in table
44	AA Sequence
8	Application
2	CAS Registry Number
11	Cloned(Commentary)
39	Cofactor
6	Crystallization (Commentary)
344	Disease/ Diagnostics
7	Expression
16	General Information
1	General Stability
139	IC50 Value
160	Inhibitors
19	kcat/KM [mM/s]
8	Ki Value [mM]
147	KM Value [mM]
12	Localization
8	Molecular Weight [Da]
22	Natural Substrates/ Products (Substrates)
46	Organism
4	Pathway
39	PDB ID
15	pH Optimum
5	pH Range
7	Protein Variants
8	Purification (Commentary)
2	Reaction
3	Reaction Type
43	Reference
88	Source Tissue
17	Specific Activity [micromol/min/mg]
5	Storage Stability
165	Substrates and Products (Substrate)
3	Subunits
53	Synonyms
1	Systematic Name
7	Temperature Optimum [°C]
4	Temperature Stability [°C]
115	Turnover Number [1/s]

Crystallization

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Crystallization on EC 1.1.1.239 - 3alpha(17beta)-hydroxysteroid dehydrogenase (NAD+)

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

10 ns molecular dynamics simulations of inhibitor bound to isofrom AKR1C3. Binding could induce conformational changes to both inhibitor and enzyme. The compound presumably assumes a stable, energetically favored, planar conformation, with an estimated free energy of binding of ?5 kcal/mol

Homo sapiens

P42330

725671

docking of inhibitors (2E)-3-(4-methylphenyl)-2-[4-(methylsulfonyl)phenyl]prop-2-enoic acid, (2E)-3-(4-ethylphenyl)-2-[4-(methylsulfonyl)phenyl]prop-2-enoic acid, (2E)-3-(4-bromophenyl)-2-[4-(methylsulfonyl)phenyl]prop-2-enoic acid and (2E)-3-[4-(methylsulfanyl)phenyl]-2-[4-(methylsulfonyl)phenyl]prop-2-enoic acid to crystal structure. Compounds occupy a similar position of the active site as the co-crystallized indomethacin, with the Aryl1 overlapping with the p-chlorobenzoyl moiety of the indomethacin and the Aryl2 overlapping with an indole part of the indomethacin

Homo sapiens

P42330

724916

in complex with 3-phenoxybenzoic acid, to 1.68 A resolution, space group P212121

Homo sapiens

P42330

723866

in complex with inhibitor 1-(4-[[(2R)-2-methylpiperidin-1-yl]sulfonyl]phenyl)-1,3-dihydro-2H-pyrrol-2-one. The 2-pyrrolidinone does not interact directly with residues in the oxyanion hole

Homo sapiens

P42330

724915

in complex with inhibitor 3-[[4-(trifluoromethyl)phenyl]amino]benzoic acid. Compound adopts a similar binding orientation as flufenamic acid, however, its phenylamino ring projects deeper into a subpocket and confers selectivity over the other AKR1C isoforms

Homo sapiens

P42330

724533

NADP+ and 2'-des-methyl-indomethacin is determined at a resolution of 1.8 A by molecular replacement. The cofactor binding cavity of AKR1C3 is not perturbed upon binding of the inhibitor

Homo sapiens

P42330

725674