Structure and role of the linker domain of the iron surface-determinant protein IsdH in heme transportation in Staphylococcus aureus.

Staphylococcus aureus is a major cause of deadly nosocomial infections, a severe problem fueled by the steady increase of resistant bacteria. The iron surface determinant (Isd) system is a family of proteins that acquire nutritional iron from the host organism, helping the bacterium to proliferate during infection, and therefore represents a promising antibacterial target. In particular, the surface protein IsdH captures hemoglobin (Hb) and acquires the heme moiety containing the iron atom.

Genetics, structure, function, mode of actions and role in cancer development of CYP17.

Most prostate and breast cancers are hormone dependent. The inhibition of steroid 17α-hydroxylase/17,20- lyase (CYP17), which is a crucial enzyme for steroid hormone biosynthesis, is widely used to treat androgen-dependent prostate cancer (PC). CYP17 has dual enzymatic activity: 17alpha-hydroxylase activity (utilizing delta4- C21 steroids as substrates) and the 17,20-lyase activity (using delta5- C21 steroids as substrates).

At the crossroads of steroid hormone biosynthesis: the role, substrate specificity and evolutionary development of CYP17.

Cytochrome P450s play critical roles in the metabolism of various bioactive compounds. One of the crucial functions of cytochrome P450s in Chordata is in the biosynthesis of steroid hormones. Steroid 17alpha-hydroxylase/17,20-lyase (CYP17) is localized in endoplasmic reticulum membranes of steroidogenic cells.