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Glycosyltransferase is a subcategory of EC 2.4 transferases that is involved in biosynthesis of disaccharides and polysaccharides through transfer of monosaccharides to other molecules. [40] An example of a prominent glycosyltransferase is lactose synthase which is a dimer possessing two protein subunits.
Toggle Category:Transferases (EC 2) (Transferase) subsection 2.1 Category:EC 2.1 (transfer one-carbon groups, Methylase) 2.2 Category:EC 2.2 (transfer aldehyde or ketone groups)
All CoA-transferases have alternating layers of α helices and β sheets, and thus they belong to the α/β class of proteins. [1] The number and arrangement of these layers differs by family. The Gct family, for example, has extra layers of α helices and β sheets compared to Cat1 and OXCT1 families. Further, all enzymes have two different ...
Transferases transfer a functional group (e.g. a methyl or phosphate group). They are classified as EC 2 in the EC number classification. Wikimedia Commons has media related to Transferases .
Most glycosyltransferase enzymes form one of two folds: GT-A or GT-B. Glycosyltransferases (GTFs, Gtfs) are enzymes that establish natural glycosidic linkages.They catalyze the transfer of saccharide moieties from an activated nucleotide sugar (also known as the "glycosyl donor") to a nucleophilic glycosyl acceptor molecule, the nucleophile of which can be oxygen- carbon-, nitrogen-, or sulfur ...
Examples: RCC1, an important mitotic protein, is methylated so that it can interact with centromeres of chromosomes. This is an example of regulation of protein-protein interaction, as methylation regulates the attachment of RCC1 to histone proteins H2A and H2B. The RCC1-chromatin interaction is also an example of a protein-DNA interaction, as ...
An acetyltransferase (also referred to as a transacetylase) is any of a class of transferase enzymes that transfers an acetyl group in a reaction called acetylation.In biological organisms, post-translational modification of a protein via acetylation can profoundly transform its functionality by altering various properties like hydrophobicity, solubility, and surface attributes. [1]
Transamination is mediated by several types of aminotransferase enzymes. An aminotransferase may be specific for an individual amino acid, or it may be able to process any member of a group of similar ones, for example the branched-chain amino acids, which comprises valine, isoleucine, and leucine.