St6 beta-galactoside alpha-2,6-sialyltransferase 2

St6 beta-galactoside alpha-2,6-sialyltransferase 2 (ST6GAL2) is an enzyme that in humans is encoded by the ST6GAL2 gene. This enzyme is a member of the glycosyltransferase family, specifically the sialyltransferases, which are responsible for the addition of sialic acid residues to various glycoproteins and glycolipids.

Function

ST6GAL2 is involved in the synthesis of the carbohydrate moieties of glycoconjugates. It transfers sialic acid from cytidine monophosphate (CMP)-sialic acid to the terminal beta-galactose residues of glycoconjugates, producing alpha-2,6-sialylated products. This enzyme is predominantly found in the golgi apparatus, where it is involved in the post-translational modification of proteins.

Clinical significance

Alterations in the expression of ST6GAL2 have been implicated in various diseases. For example, increased expression of this enzyme has been associated with cancer progression, as it can contribute to the altered glycosylation patterns observed in many cancer cells. Additionally, mutations in the ST6GAL2 gene have been linked to certain genetic disorders, although further research is needed to fully understand these associations.

See also

• Sialyltransferase
• Glycosyltransferase
• Glycosylation

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