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
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1.14.14.14
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estrogen
-
women
-
androgen
-
steroid
-
postmenopausal
-
ovarian
-
tamoxifen
-
ovary
-
progesterone
-
letrozole
-
granulosa
-
follicle
-
gonad
-
anastrozole
-
receptor-positive
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fsh
-
steroidogenic
-
exemestane
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androstenedione
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gonadotropin
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steroidogenesis
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endometrial
-
lutein
-
follicular
-
testicular
-
antiestrogens
-
fulvestrant
-
er-positive
-
nonsteroidal
-
endometriosis
-
neoadjuvant
-
preoptic
-
third-generation
-
hormone-dependent
-
follicle-stimulating
-
gnrh
-
estrogen-dependent
-
oestradiol
-
dihydrotestosterone
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premenopausal
-
mastectomy
-
arthralgia
-
17beta-hydroxysteroid
-
everolimus
-
5alpha-reductase
-
cyp17a1
-
raloxifene
-
medicine
-
virilization
-
progestin
-
her2-negative
- 1.14.14.14
- estrogen
- women
- androgen
- steroid
-
postmenopausal
- ovarian
- tamoxifen
- ovary
- progesterone
- letrozole
-
granulosa
- follicle
- gonad
- anastrozole
-
receptor-positive
- fsh
-
steroidogenic
- exemestane
- androstenedione
- gonadotropin
- steroidogenesis
- endometrial
- lutein
- follicular
- testicular
-
antiestrogens
-
fulvestrant
-
er-positive
-
nonsteroidal
- endometriosis
-
neoadjuvant
-
preoptic
-
third-generation
-
hormone-dependent
-
follicle-stimulating
- gnrh
-
estrogen-dependent
- oestradiol
- dihydrotestosterone
-
premenopausal
-
mastectomy
- arthralgia
-
17beta-hydroxysteroid
-
everolimus
-
5alpha-reductase
- cyp17a1
- raloxifene
- medicine
-
virilization
- progestin
-
her2-negative
Reaction
Synonyms
AROM, Cyp19a, CYP19A1, Cyp19a1a, Cyp19a1b, Cyp19A3, cytochrome P450 aromatase, P450arom
ECTree
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Crystallization
Crystallization on EC 1.14.14.14 - aromatase
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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