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
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women
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androgen
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steroid
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postmenopausal
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ovarian
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tamoxifen
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ovary
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progesterone
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letrozole
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granulosa
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follicle
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gonad
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anastrozole
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receptor-positive
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fsh
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steroidogenic
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exemestane
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androstenedione
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gonadotropin
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steroidogenesis
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endometrial
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lutein
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follicular
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testicular
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antiestrogens
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fulvestrant
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er-positive
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nonsteroidal
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endometriosis
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neoadjuvant
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preoptic
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third-generation
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hormone-dependent
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follicle-stimulating
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gnrh
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estrogen-dependent
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oestradiol
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dihydrotestosterone
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premenopausal
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mastectomy
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arthralgia
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17beta-hydroxysteroid
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everolimus
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5alpha-reductase
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cyp17a1
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raloxifene
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medicine
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virilization
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progestin
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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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Engineering
Engineering on EC 1.14.14.14 - aromatase
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D309N
mutant retains its ability to bind to androstenedione across the entire pH range studied
R192H
homozygous CYP19A1 mutation identified in two siblings of consanguineous parents. Mutation causes a severe phenotype of aromatase deficiency in a 46,XX newborn and maybe hypospadias and cryptorchidism in a 46,XY, but no maternal androgen excess during pregnancy
R264C
R264H
single nuclotide polymorphism, impairs the correct binding of both substrate and inhibitor molecules. contrary to wild-type, mutant undergoes a less efficient packing process, suggesting a minor flexibility of the mobile segments
R264C
with the wild-type cytochrome P450 oxidoreductase POR as a redox partner, polymorphism R264C shows only 15% of wild-type aromatase activity. With variant P284L-POR as a redox partner, R264C loses all activity but retains 6.7% of activity with P284T-POR
single nuclotide polymorphism, impairs the correct binding of both substrate and inhibitor molecules. contrary to wild-type, mutant undergoes a less efficient packing process, suggesting a minor flexibility of the mobile segments
R264H
with the wild-type cytochrome P450 oxidoreductase POR as a redox partner, polymorphism R264H shows 87% of wild-type aromatase activity but low activities with both the POR-P284L as well as the POR-P284T variants. The R264H variant has more than threefold higher activity compared to wild-type when the POR-Y607C variant is used as the redox partner