EC Number   |
General Information |
Reference |
|---|
    1.14.14.14 | metabolism |
CYP19A1 protein structure is organized in two main clusters, whose connectivity is altered by ligand binding. Upon substrate or inhibitor binding, the wild-type enzyme undergoes a conformational change leading to a more compact tertiary structure. In single-nucleotide polymorphisms R264C and R264H the exchange rates in the ligand-free and -bound forms are similar, and the quenching effect on tryptophan-224 observed upon ligand binding in the wild-type, is absent in both variants. Helices F and G between the two clusters that form the substrate channel to the active site have a connecting role |
764251 |
| 1.14.14.14 | metabolism |
in a male mouse model overexpressing the aromatase enzyme, adipose tissue estradiol levels are increased while circulating sex steroid levels are unaffected. The overexpressing male mice are more insulin sensitive compared with wild-type mice and exhibit increased serum adiponectin levels and upregulated expression of Glut4 and Irs1 in white adipose tissue. The expression of markers of macrophages and immune cell infiltration is markedly decreased in their white adipose tissue |
743988 |
| 1.14.14.14 | physiological function |
a decrease or an increase in male brain aromatase activity relative to controls is associated with decreased egg production and is also correlated with significant changes in gonadosomatic index in both sexes |
744150 |
| 1.14.14.14 | physiological function |
cerebrovascular endothelial aromatase plays an important and sexually dimorphic role in cerebrovascular function |
743990 |
| 1.14.14.14 | physiological function |
dimerization of the human P450arom, primarily via salt bridges at the I-H loop, leads to greater activity and reduced release of intermediates compared to porcine aromatase |
745643 |
| 1.14.14.14 | physiological function |
dimerization of the human P450arom, primarily via salt bridges at the IĀH loop, leads to greater activity and reduced release of intermediates compared to porcine aromatase.The porcine gonadal P450arom has no ionic interaction at the I-H loop but forms a new intra-molecular salt bridge at the N termini of the I-helix that leads to locking of the substrate |
745643 |
