1.14.14.14: aromatase
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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
1.14.14.14 aromataseAdvanced search results
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results (Engineering
Engineering on EC 1.14.14.14 - aromatase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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
R264C
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
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
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
