Testosterone 1 beta-hydroxylation by human cytochrome P450 3A4

Autor: Joel A, Krauser, Markus, Voehler, Li-Hong, Tseng, Alexandre B, Schefer, Markus, Godejohann, F Peter, Guengerich
Rok vydání: 2004
Předmět:
Zdroj: European journal of biochemistry. 271(19)
ISSN: 0014-2956
Popis: Human cytochrome P450 3A4 forms a series of minor testosterone hydroxylation products in addition to 6 beta-hydroxytestosterone, the major product. One of these, formed at the next highest rate after the 6 beta- and 2 beta-hydroxy products, was identified as 1 beta-hydroxytestosterone. This product was characterized from a mixture of testosterone oxidation products using an HPLC-solid phase extraction-cryoprobe NMR/time-of-flight mass spectrometry system, with an estimated total of approximately 6 microg of this product. Mass spectrometry established the formula as C(19)H(29)O(3) (MH(+) 305.2080). The 1-position of the added hydroxyl group was established by correlated spectroscopy and heteronuclear spin quantum correlation experiments, and the beta-stereochemistry of the added hydroxyl group was assigned with a nuclear Overhauser correlated spectroscopy experiment (1 alpha-H). Of several human P450s examined, only P450 3A4 formed this product. The product was also formed in human liver microsomes.
Databáze: OpenAIRE