PLOD3
PLOD3 (procollagen-lysine,2-oxoglutarate 5-dioxygenase 3, also known as LH3) is a multifunctional enzyme of the endoplasmic reticulum that modifies lysine residues in procollagen. It hydroxylates lysine and adds sugar groups to the resulting hydroxylysine. Browse Assay Genie's current range of PLOD3 research reagents below, or read on for the biology behind the target.
PLOD3 is a multifunctional enzyme that catalyses a series of essential post-translational modifications on lysine residues in procollagen. It plays a redundant role in forming hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens, and a redundant role in transferring galactose onto hydroxylysine to give galactosyl 5-hydroxylysine. Its essential contribution is the subsequent transfer of glucose moieties, which produces 1,2-glucosylgalactosyl-5-hydroxylysine residues. PLOD3 also hydroxylates and glycosylates lysine residues in the collagen-like domain of MBL1, giving the same hydroxylysine and 1,2-glucosylgalactosyl-5-hydroxylysine products.
According to the NCBI Gene summary, the PLOD3 protein is a membrane-bound homodimeric enzyme localised to the cisternae of the rough endoplasmic reticulum. Its lysyl hydroxylase activity depends on the cofactors iron and ascorbate. UniProt records the protein in the rough endoplasmic reticulum, the endoplasmic reticulum lumen and membrane, and in secreted and extracellular forms. The hydroxylysyl groups it generates are attachment sites for carbohydrates in collagen and are therefore critical for the stability of intermolecular crosslinks.
Functionally, PLOD3 is essential for normal biosynthesis and secretion of type IV collagens and for normal formation of basement membranes. Some patients with Ehlers-Danlos syndrome type VIB have deficiencies in lysyl hydroxylase activity. The PLOD3 gene belongs to the procollagen-lysine,2-oxoglutarate 5-dioxygenase family, alongside PLOD1 and PLOD2, and has orthologues named Plod3 in mouse and rat.
PLOD3 catalyses lysine hydroxylation and glycosylation of procollagen, making it a key enzyme for studying collagen post-translational modification.
PLOD3 is essential for normal basement membrane formation and for the biosynthesis and secretion of type IV collagens.
Hydroxylysyl groups made by PLOD3 are carbohydrate attachment sites that are critical for the stability of intermolecular collagen crosslinks.
Deficient lysyl hydroxylase activity is seen in some patients with Ehlers-Danlos syndrome type VIB, linking this enzyme family to disease research.
PLOD3 catalyses post-translational modification of lysine residues in procollagen. It forms hydroxylysine, transfers galactose to hydroxylysine, and has an essential role in transferring glucose to give 1,2-glucosylgalactosyl-5-hydroxylysine. It is needed for type IV collagen biosynthesis and secretion and for basement membrane formation.
PLOD3 is the HGNC symbol for procollagen-lysine,2-oxoglutarate 5-dioxygenase 3. It is also called LH3 (lysyl hydroxylase 3), and UniProt lists the protein as multifunctional procollagen lysine hydroxylase and glycosyltransferase LH3. Searching under either name should find the same target.
Mouse and rat both have a Plod3 orthologue, so the gene is studied in rodent models; check the datasheet of any product for its validated reactivity. Some patients with Ehlers-Danlos syndrome type VIB have deficiencies in lysyl hydroxylase activity, a family-level link to connective tissue disease.
Other members of the procollagen-lysine,2-oxoglutarate 5-dioxygenase family involved in collagen modification.
Gene and protein annotations from HGNC, NCBI Gene and UniProt O60568; product specifications from Assay Genie datasheets.