N-glycosyltransferase
| Glycosyl transferase family 41 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | GT41 | ||||||||
| Pfam | PF13844 | ||||||||
| CAZy | GT41 | ||||||||
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N-glycosyltransferase is an enzyme in prokaryotes which transfers individual hexoses onto asparagine sidechains in substrate proteins, using a nucleotide-bound intermediary, within the cytoplasm. They are distinct from regular N-glycosylating enzymes, which are oligosaccharyltransferases that transfer pre-assembled oligosaccharides. Both enzyme families however target a shared amino acid sequence asparagine—-any amino acid except proline—serine or threonine (N–x–S/T), with some variations.
Such enzymes have been found in the bacteria Actinobacillus pleuropneumoniae (whose N-glycosyltransferase is the best researched member of this enzyme family) and Haemophilus influenzae, and later in other bacterial species such as Escherichia coli. N-glycosyltransferases usually target adhesin proteins, which are involved in the attachment of bacterial cells to epithelia (in pathogenic bacteria); glycosylation is important for the stability and function of the adhesins.