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

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