What is the function of prolyl 4 hydroxylase within your own body?

Prolyl 4 hydroxylases (P4H) are iron- and 2-oxoglutamate-dependent dioxygenase enzymes and hypoxia-inducible transcription factor (HIF)-P4Hs play a critical role in the regulating oxygen homeostasis in the local tissues as well in the systemic circulation.

What does peptidyl prolyl hydroxylase do?

Prolyl hydroxylase (proline,2-oxoglutarate dioxygenase, EC 1.14. 11.2) is a mixed-function oxygenase that hydroxylates peptidyl proline with the simultaneous and stoichiometric decarboxylation of alpha-ketoglutarate to succinate and CO2.

What does prolyl hydroxylase Catalyse in collagen?

Biological function Prolyl hydroxylase catalyzes the formation of hydroxyproline. The modification has a significant impact on the stability of collagen, the major connective tissue of the human body.

Which cofactor is essential for prolyl hydroxylase during the collagen synthesis?

L-ascorbic acid
L-ascorbic acid is an essential cofactor for lysyl hydroxylase and prolyl hydroxylase, enzymes essential for collagen biosynthesis.

How does vitamin C regulate prolyl hydroxylase?

In scurvy, collagen prolyl hydroxylase is inhibited by ascorbate (vitamin C) deficiency, resulting in defective collagen formation and the characteristic signs of swollen, bleeding gums, widespread hemorrhages, poor wound healing, and ultimately, death (2).

What is the name for P4H9?

P4H9 – Probable prolyl 4-hydroxylase 9 – Arabidopsis thaliana (Mouse-ear cress) – P4H9 gene & protein.

Does lysyl hydroxylase require vitamin C?

Vitamin C. Vitamin C, oxygen, ketoglutarate, and iron are essential cofactors for the enzymes prolyl hydroxylase and lysyl hydroxylase, both of which are required for normal collagen metabolism. Vitamin C is important in aerobic metabolism.

What are the steps in synthesis of collagen?

Synthesis. First, a three-dimensional stranded structure is assembled, with the amino acids glycine and proline as its principal components. This is not yet collagen but its precursor, procollagen. Procollagen is then modified by the addition of hydroxyl groups to the amino acids proline and lysine.

How collagen is synthesized?

Collagen is composed of 3 chains. The chains are wound together to form a triple helix. The process of collagen synthesis occurs mainly in the cells of fibroblasts which are specialized cells with the main function of synthesizing collagen and stroma. Collagen synthesis occurs both intracellularly and extracellularly.

How does ascorbic acid vitamin C affect prolyl hydroxylase function?

Ascorbic acid is an essential cofactor for the enzyme prolyl hydroxylase, and a deficiency of this vitamin results in accumulation of abnormal collagen. Ascorbic acid may also function to reduce tocopheroxyl radicals, and synergistic antioxidant effects between vitamins C and E are well established.

What is the role of prolyl 4-hydroxylase?

Prolyl 4-hydroxylase catalyzes the formation of 4-hydroxyproline in collagens and other proteins with collagen-like amino acid sequences by the hydroxylation of proline residues in -X-Pro-Glysequences. The reaction products, 4-hydroxyproline residues, serve to stabilize the collagen triple helices under physiological conditions.

What is the role of 4 hydroxyproline in collagen synthesis?

The reaction products, 4-hydroxyproline residues, serve to stabilize the collagen triple helices under physiological conditions. Conversely, collagen chains that contain no 4-hydroxyproline cannot fold into triple helical molecules that are stable at body temperature.

Where are prolyl hydroxylase domains found in proteins?

Hyp is also found in proteins with collagen-like domains, as well as elastin, conotoxins, and argonaute 2. A prolyl hydroxylase domain protein acts on the hypoxia inducible factor alpha, which plays a key role in sensing molecular oxygen, and could act on inhibitory kappaB kinase and RNA polymerase II.

What is the role of Hyp in collagen?

The best known role for Hyp is in stabilizing the collagen triple helix. Hyp is also found in proteins with collagen-like domains, as well as elastin, conotoxins, and argonaute 2.