Alpha-L-fucosyltransferase

From WikiMD's Wellness Encyclopedia

Alpha-L-fucosyltransferase is an enzyme that catalyzes the transfer of fucose residues to N-linked type complex glycoproteins. This enzyme plays a crucial role in the synthesis of glycan structures, which are essential components of many biological systems, including the immune system, cell adhesion, and signal transduction.

Structure of Alpha-L-fucosyltransferase

Function[edit | edit source]

Alpha-L-fucosyltransferase is responsible for the addition of fucose to the N-acetylglucosamine residue of glycoproteins. This process is known as fucosylation, and it is a type of glycosylation that is critical for the function of many proteins. Fucosylation can affect protein stability, trafficking, and interactions with other molecules.

Structure[edit | edit source]

The structure of alpha-L-fucosyltransferase is complex, with multiple domains that contribute to its function. The enzyme contains a catalytic domain, which is responsible for the transfer of fucose, and a substrate-binding domain, which recognizes and binds to the glycoprotein substrate.

Clinical significance[edit | edit source]

Abnormalities in the function of alpha-L-fucosyltransferase can lead to a variety of diseases. For example, defects in fucosylation can result in congenital disorders of glycosylation, a group of rare genetic disorders that affect a person's ability to produce properly glycosylated proteins. Additionally, changes in the levels of fucosylation have been associated with cancer, inflammatory diseases, and infectious diseases.


See also[edit | edit source]

References[edit | edit source]

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