Dolichyl-phosphate beta-glucosyltransferase

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Dolichyl-phosphate beta-glucosyltransferase
Identifiers
EC number2.4.1.117
CAS number62213-38-3
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO


Dolichyl-phosphate beta-glucosyltransferase is an enzyme that plays a crucial role in the process of glycosylation, specifically in the synthesis of glycoproteins. This enzyme is responsible for transferring a glucose molecule from UDP-glucose to dolichyl phosphate, forming dolichyl-phosphate-glucose.

Function[edit | edit source]

Dolichyl-phosphate beta-glucosyltransferase is involved in the N-linked glycosylation pathway, which is essential for the proper folding and stability of many proteins. The enzyme catalyzes the following reaction:

UDP-glucose + dolichyl phosphate → UDP + dolichyl-phosphate-glucose

This reaction is a key step in the assembly of the dolichol-linked oligosaccharide precursor, which is subsequently transferred to nascent proteins in the endoplasmic reticulum.

Structure[edit | edit source]

The structure of dolichyl-phosphate beta-glucosyltransferase has not been fully elucidated. However, it is known to be a membrane-bound enzyme located in the endoplasmic reticulum.

Clinical Significance[edit | edit source]

Mutations or deficiencies in dolichyl-phosphate beta-glucosyltransferase can lead to disorders in glycosylation, which can result in various congenital disorders of glycosylation (CDGs). These disorders often present with a wide range of symptoms, including developmental delays, neurological issues, and other systemic problems.

Related Enzymes[edit | edit source]

Dolichyl-phosphate beta-glucosyltransferase is part of a larger family of glycosyltransferases, which are enzymes that facilitate the transfer of sugar moieties to various substrates. Other related enzymes include:

See Also[edit | edit source]

References[edit | edit source]

External Links[edit | edit source]

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Contributors: Prab R. Tumpati, MD