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1.3.99.5: 3-oxo-5alpha-steroid 4-dehydrogenase (acceptor)

This is an abbreviated version!
For detailed information about 3-oxo-5alpha-steroid 4-dehydrogenase (acceptor), go to the full flat file.

Word Map on EC 1.3.99.5

Reaction

a 3-oxo-5alpha-steroid
+
acceptor
=
a 3-oxo-DELTA4-steroid
+
reduced acceptor

Synonyms

3-keto-DELTA4-steroid-5 alpha-reductase, 3-ketosteroid-DELTA4(5alpha)-dehydrogenase, 3-oxo-5alpha-steroid DELTA4-dehydrogenase, 3-oxo-steroid-4-ene dehydrogenase, 3-oxosteroid DELTA4-dehydrogenase, 4-ene-3-ketosteroid-5alpha-oxidoreductase, 5 alpha-SR2, 5-alpha reductase II, 5alpha reductase, 5alpha-R, 5alpha-R1, 5alpha-reductase, 5alpha-reductase II, 5alpha-reductase type 1, 5alpha-reductase type 2, 5alpha-reductase type II, 5alpha-reductase type1, 5alpha-reductase type2, 5alphaR1, 5alphaR2, 5AR2, dehydrogenase, 3-oxo-5alphasteroid DELTA4-, DELTA4(5alpha)DH, DELTA4-3-keto steroid 5alpha-reductase, DELTA4-3-ketosteroid 5alpha-oxidoreductase, DELTA4-3-oxo steroid reductase, DELTA4-3-oxosteroid-5alpha-reductase, DELTA4-5alpha-dehydrogenase, NADPH-dependent 5alpha-reductase enzyme, r5alphaR1, S5alphaRI, S5alphaRII, S5AR, SRD5A1, SRD5A2, SRD5alpha, steroid 5-alpha reductase type 2, steroid 5-alpha-reductase type 2, steroid 5alpha-reductase, steroid 5alpha-reductase type 1, steroid 5alpha-reductase type 2, steroid DELTA4-5alpha-reductase, steroid-5alpha-reductase, testosterone 5alpha-reductase, type 1 5alpha-reductase, type 2 5alpha-reductase, type I 5alpha-reductase, type II 5alpha-reductase

ECTree

     1 Oxidoreductases
         1.3 Acting on the CH-CH group of donors
             1.3.99 With unknown physiological acceptors
                1.3.99.5 3-oxo-5alpha-steroid 4-dehydrogenase (acceptor)

Crystallization

Crystallization on EC 1.3.99.5 - 3-oxo-5alpha-steroid 4-dehydrogenase (acceptor)

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
to 1.6 A resolution, structure reveals three conserved residues, Y319, Y466, and S468 in a pocket near the isoalloxazine ring system of the FAD co-factor. Crystal structure with bound product 4-androstene-3,17-dione shows that residue S468 is in a position in which it can serve as the base abstracting the 4beta-proton from the C4 atom of the substrate. S468 is assisted by Y319, which possibly is involved in shuttling the proton to the solvent. Y466 is at hydrogen bonding distance to the C3 oxygen atom of the substrate and can stabilize the keto-enol intermediate occurring during the reaction. The FAD N5 atom is in a position to be able to abstract the 5alpha-hydrogen of the substrate as a hydride ion