PLOD1

Lysyl hydroxylase is a membrane-bound homodimeric protein localized to the cisternae of the endoplasmic reticulum. The enzyme (cofactors iron and ascorbate) catalyzes the hydroxylation of lysyl residues in collagen-like peptides. The resultant hydroxylysyl groups are attachment sites for carbohydrates in collagen and thus are critical for the stability of intermolecular crosslinks. Some patients with Ehlers-Danlos syndrome type VI have deficiencies in lysyl hydroxylase activity. Two transcript variants encoding different isoforms have been observed for this gene.

Full Name

procollagen-lysine, 2-oxoglutarate 5-dioxygenase 1

Function

Part of a complex composed of PLOD1, P3H3 and P3H4 that catalyzes hydroxylation of lysine residues in collagen alpha chains and is required for normal assembly and cross-linkling of collagen fibrils (By similarity).
Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens (PubMed:8621606, PubMed:10686424, PubMed:15854030).
These hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links (Probable).

Biological Process

Epidermis developmentManual Assertion Based On ExperimentIMP:UniProtKB
Peptidyl-lysine hydroxylationManual Assertion Based On ExperimentIDA:UniProtKB
Response to hypoxiaManual Assertion Based On ExperimentIEP:UniProtKB

Cellular Location

Rough endoplasmic reticulum membrane

Involvement in disease

Ehlers-Danlos syndrome, kyphoscoliotic type, 1 (EDSKSCL1):
A form of Ehlers-Danlos syndrome, a group of connective tissue disorders characterized by skin hyperextensibility, articular hypermobility, and tissue fragility. EDSKSCL1 is an autosomal recessive form characterized by severe muscle hypotonia at birth, generalized joint laxity, scoliosis at birth, and scleral fragility and rupture of the ocular globe.