What does 17 alpha hydroxylase do?
The enzyme has 17 alpha(α)-hydroxylase activity, which is important for production of glucocorticoids and sex hormones. CYP17A1 also has 17,20-lyase activity, which is integral to the production of sex hormones. 17α-hydroxylase/17,20-lyase deficiency results from a shortage (deficiency) of both enzyme activities.
Why is aldosterone low in 17a hydroxylase deficiency?
Most 17OHD patients have low aldosterone levels caused by increased levels of DOCs leading to suppression of renin angiotensin system. However, some cases reported high aldosterone levels [7,8].
What does the cyp17 gene do?
The CYP17A1 gene provides instructions for making a member of the cytochrome P450 enzyme family. Like other cytochrome P450 enzymes, CYP17A1 is involved in the formation (synthesis) of steroid hormones.
Is aldosterone increased in 17 alpha hydroxylase deficiency?
Prevalence may be more common in Brazil, where there appears to be a founder effect, with more than 80% of the gene mutations identified being due to 2 specific mutations. In Japan, several cases of 17-alpha hydroxylase deficiency associated with elevated aldosterone levels have been reported.
What does a hydroxylase do?
Hydroxylases are enzymes which add an hydroxyl group to organic compounds. This addition is the first step of aerobic oxidative degradation.
Why is my 17 hydroxyprogesterone so low?
Low values of 17-OHP are found in adrenal hypofunction, whether of adrenal or hypothalamic/pituitary origin. The most frequent cause of a low 17-OHP concentration is suppression of the pituitary–adrenal axis by synthetic glucocorticoids given therapeutically.
What is a 17 hydroxyprogesterone blood test for?
17-OHP is made as part of the process of producing cortisol. A 17-OHP test helps diagnose a rare genetic disorder called congenital adrenal hyperplasia (CAH). In CAH, a genetic change, known as a mutation, prevents the adrenal gland from making enough cortisol.
Is hydroxylase a protein?
Protein hydroxylation is a post-translational modification catalyzed by 2-oxoglutarate-dependent dioxygenases. The hydroxylation modification can take place on various amino acids, including but not limited to proline, lysine, asparagine, aspartate and histidine.