Peptidyl Prolyl Hydroxylase is an enzyme that plays a crucial role in the post-translational modification of proteins. Specifically, it is involved in the hydroxylation of proline residues in peptides and proteins. This enzymatic process is essential for the stabilization and regulation of protein structure and function.
The primary function of Peptidyl Prolyl Hydroxylase is to catalyze the hydroxylation of proline residues present in peptide or protein chains. This hydroxylation reaction occurs by incorporating a hydroxyl group (-OH) onto the carbon atom adjacent to the proline nitrogen, resulting in the formation of hydroxyproline. This modification is essential for various physiological processes, including collagen biosynthesis, protein folding, and cell signaling.
Peptidyl Prolyl Hydroxylase is widely distributed in both eukaryotic and prokaryotic organisms, and its activity is dependent on the presence of oxygen, iron ions, and ascorbate (vitamin C) as a co-factor. The enzyme achieves its catalytic activity through the intrinsic iron-binding domain known as the 2-oxoglutarate-dependent dioxygenase or 2OGD family.
Deficiencies or dysregulation of Peptidyl Prolyl Hydroxylase can lead to various pathological conditions, including connective tissue disorders, impaired wound healing, and cardiovascular diseases, among others. Consequently, this enzyme has become an important target for drug development and therapeutic interventions.
In summary, Peptidyl Prolyl Hydroxylase is an essential enzyme involved in the hydroxylation of proline residues in peptides and proteins. Through this enzymatic process, it plays a critical role in protein stability, folding, and function, and its
