Dolichyldiphosphatase

Dolichyldiphosphatase (also known as Dolichyl-diphosphatase) is an enzyme that catalyzes the hydrolysis of dolichyl diphosphate (Dol-P-P) to dolichol and inorganic phosphate. This enzyme plays a crucial role in the protein glycosylation pathway, specifically in the synthesis of the lipid-linked oligosaccharide (LLO) precursor.

Function

Dolichyldiphosphatase is involved in the N-glycosylation pathway, a critical process in protein folding and stability. The enzyme catalyzes the dephosphorylation of Dol-P-P, a key intermediate in the synthesis of the LLO precursor. This reaction is essential for the recycling of dolichol, allowing it to participate in multiple rounds of LLO synthesis.

Structure

The structure of dolichyldiphosphatase is not fully understood. However, it is known to be an integral membrane protein located in the endoplasmic reticulum (ER). The enzyme is believed to have multiple transmembrane domains, which allow it to interact with its lipid substrate within the hydrophobic environment of the ER membrane.

Clinical significance

Mutations in the gene encoding dolichyldiphosphatase can lead to disorders of protein glycosylation. These include congenital disorders of glycosylation (CDG), a group of genetic diseases characterized by defective glycosylation of proteins and lipids. CDG patients often present with a wide range of symptoms, including developmental delay, intellectual disability, and organ dysfunction.

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Dolichyldiphosphatase catalyzes the hydrolysis of dolichyl diphosphate.

See also

• Dolichol kinase
• Dolichol phosphate mannose synthase
• Dolichol phosphate