Peptide-O-fucosyltransferase
Peptide-O-fucosyltransferase is an enzyme that catalyzes the transfer of fucose, a monosaccharide, from GDP-fucose to a serine or threonine residue in a peptide substrate. This process is known as O-fucosylation, a type of protein glycosylation that plays a crucial role in various biological processes.
Function[edit | edit source]
Peptide-O-fucosyltransferase is involved in the O-fucosylation of Notch proteins, which are critical for cell-cell communication during animal development. The enzyme adds a fucose sugar to specific serine or threonine residues in the extracellular domain of Notch proteins. This modification is necessary for the proper function of Notch proteins.
Structure[edit | edit source]
Peptide-O-fucosyltransferase is a type II membrane protein located in the endoplasmic reticulum. The enzyme consists of a short N-terminal cytoplasmic tail, a single transmembrane domain, and a large C-terminal catalytic domain located in the lumen of the endoplasmic reticulum.
Clinical significance[edit | edit source]
Mutations in the gene encoding peptide-O-fucosyltransferase can lead to a variety of disorders. For example, Dowling-Degos disease is associated with mutations in this gene. This is a rare genetic skin disorder characterized by reticulate hyperpigmentation of the flexures.
See also[edit | edit source]
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Contributors: Prab R. Tumpati, MD