Pyruvyltransferase

Pyruvyltransferase is an enzyme that catalyzes the transfer of a pyruvyl group from an activated donor to an acceptor molecule, forming a pyruvylated product. These enzymes participate in the post-synthetic modification of glycans and lipid carriers in bacteria and archaea, and in some cases in eukaryotes. Pyruvylation can alter charge, hydrogen-bonding potential, and recognition properties, influencing cell surface antigens, biofilm formation, and interactions with host tissues.

Donor and acceptor substrates vary among pyruvyltransferases. Some rely on pyruvylated donors or on carrier cofactors, whereas others use pyruvate linked to an activated carrier. Acceptors are often hydroxyl groups on sugars within capsular polysaccharides or teichoic acid units, or on lipid-linked oligosaccharide intermediates. The reaction generally proceeds by direct transfer from donor to acceptor, with the exact stereochemical outcome depending on the enzyme family.

Distribution and function: Pyruvyltransferases have been identified predominantly in bacteria and, less commonly, in archaea. They are involved in modifications of cell surface polysaccharides such as teichoic acids, capsule polysaccharides, and other antigenic glycans, which can affect virulence, immune recognition, and biofilm formation.

Genetics and research: Genes encoding pyruvyltransferases are often located in operons related to cell envelope biosynthesis. Biochemical studies and, in some cases, structural analyses have begun to reveal substrate specificities and active-site features, aiding interpretation of their roles in physiology and their potential as targets for antimicrobial strategies.