Leprecan is part of a superfamily of 2OG-Fe(II) dioxygenase, along with DNA repair protein AlkB, and disease resistant EGL-9. The enzyme was found to be a type of hydroxylases used in the substrate formation of protein glycosylation.[2]
Activities
Leprecan, a
proteoglycan, has demonstrated prolyl hydroxylase activity; prolyl hydroxylases hydroxylate
proline residues.[3] Prolyl 3-hydroxylase 1, P3H1, forms a larger complex with
CRTAP and
cyclophilin B, CyPB, in the
endoplasimic reticulum. The complex hydroxylates a single proline residue, Pro986, on
collagen chains.[4] Recessive forms of
Osteogenesis Imperfecta are partly caused by a mutation in the LEPRE1 gene. The mutation in the gene encodes prolyl 3-hydroxylase 1. The malfunctioning prolyl 3-hydroxylase in leprecan leads to inappropriate collagen folding. This is due to the instability caused by the absence of
hydroxyproline. Hydroxyproline is the product of hydroxylating a proline residue.[5]