Pentosyltransferase: Difference between revisions
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Latest revision as of 22:26, 17 March 2025
Pentosyltransferase is a type of enzyme that plays a crucial role in the biochemical processes of living organisms. It belongs to the class of glycosyltransferase enzymes, which are responsible for the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.
Function[edit]
Pentosyltransferases are involved in the biosynthesis of glycoconjugates, which are compounds consisting of a carbohydrate covalently linked to a non-carbohydrate molecule. These enzymes catalyze the transfer of a pentose sugar, such as ribose or deoxyribose, from a donor molecule to an acceptor molecule. This process is essential for the synthesis of various biomolecules, including nucleic acids and certain types of antibiotics.
Structure[edit]
Like other glycosyltransferases, pentosyltransferases have a highly conserved core structure, which is typically composed of two domains: a catalytic domain and a sugar-binding domain. The catalytic domain is responsible for the enzymatic reaction, while the sugar-binding domain recognizes and binds to the sugar moiety of the donor molecule.
Clinical Significance[edit]
Abnormalities in the function of pentosyltransferases can lead to various health conditions. For instance, defects in the enzyme hypoxanthine-guanine phosphoribosyltransferase (HGPRT), a type of pentosyltransferase, can cause Lesch-Nyhan syndrome, a rare genetic disorder characterized by overproduction of uric acid, neurological disabilities, and self-injurious behavior.
See Also[edit]
References[edit]
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