PLOD2

PLOD2 is a membrane-bound homodimeric enzyme that is localized to the cisternae of the rough 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 VIB have deficiencies in lysyl hydroxylase activity. Mutations in the coding region of this gene are associated with Bruck syndrome.

Procollagen-Lysine,2-Oxoglutarate 5-Dioxygenase 2

Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. These hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links.

Hydroxylysine biosynthetic processManual Assertion Based On ExperimentIDA:CAFA
Peptidyl-lysine hydroxylationManual Assertion Based On ExperimentIDA:CAFA
Protein modification processManual Assertion Based On ExperimentTAS:ProtInc
Response to hypoxiaManual Assertion Based On ExperimentIEP:UniProtKB

Rough endoplasmic reticulum membrane

Bruck syndrome 2 (BRKS2):
An autosomal recessive disease characterized by generalized osteopenia, congenital joint contractures, fragile bones with onset of fractures in infancy or early childhood, short stature, severe limb deformity, progressive scoliosis, and pterygia. It is distinguished from osteogenesis imperfecta by the absence of hearing loss and dentinogenesis imperfecta, and by the presence of clubfoot and congenital joint limitations.