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1.14.14.14: aromatase

This is an abbreviated version!
For detailed information about aromatase, go to the full flat file.

Word Map on EC 1.14.14.14

Reaction

19-hydroxyandrost-4-ene-3,17-dione
+
O2
+
[reduced NADPH-hemoprotein reductase]
=
19-oxo-androst-4-ene-3,17-dione
+ 2 H2O +
[oxidized NADPH-hemoprotein reductase]

Synonyms

AROM, Cyp19a, CYP19A1, Cyp19a1a, Cyp19a1b, Cyp19A3, cytochrome P450 aromatase, P450arom

ECTree

     1 Oxidoreductases
         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
             1.14.14 With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor
                1.14.14.14 aromatase

Crystallization

Crystallization on EC 1.14.14.14 - aromatase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
free energy simulations of the entry/exit routes preferentially followed by substrate androstenedione and inhibitor letrozole. Two channels appear accessible to their entrance, while only one exit route appears to be preferential, ligand channeling is associated with large enzyme structural rearrangements
molecular docking studies with inhibitors based on PDB entry 3EQM. The 2-arylindoles prefer binding with the 2-aryl group toward a small hydrophobic pocket within the active site. The C-5 electron withdrawing group on indole may have an important role and form a hydrogen bond with Ser478 (OH). Meta-pyridyl analogs may orient with the pyridyl 3'-nitrogen coordinating with the heme group
molecular dynamics simulations of the dimeric interfaces, i.e.residues 45-496
to 1.8 A resolution, in complex with its natural substrate androst-4-ene-3,17-dione. Aromatase has an androgen-specific cleft that binds the androstenedione molecule snugly. Hydrophobic and polar residues complement the steroid backbone
molecular modeling of structure