|procollagen-lysine 1, 2-oxoglutarate 5-dioxygenase 1|
|Alt. symbols||LLH, PLOD|
|Locus||Chr. 1 p36.3-36.2|
|procollagen-lysine, 2-oxoglutarate 5-dioxygenase 2|
|Locus||Chr. 3 q24|
Lysyl hydroxylase (or procollagen-lysine 5-dioxygenase) is an oxygenase enzyme that catalyzes the hydroxylation of lysine to hydroxylysine. This reaction is necessary to the formation and stabilization of collagen. It takes place following protein synthesis (as a post-translational modification). The protein is a membrane-bound homodimeric enzyme that is localized to the cisternae (lumen) of the rough endoplasmic reticulum.
A deficiency in its cofactor, Vitamin C, is associated with Scurvy.
- Hausmann, E. (1967). "Cofactor requirements for the enzymatic hydroxylation of lysine in a polypeptide precursor of collagen". Biochim. Biophys. Acta 133 (3): 591–598. PMID 6033801.
- Rhoads, R.E. and Udenfriend, S. (1968). "Decarboxylation of α-ketoglutarate coupled to collagen proline hydroxylase". Proc. Natl. Acad. Sci. USA 60 (4): 1473–1478. PMC 224943. PMID 5244754.
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