Attachment of pneumococcal autolysin to wall teichoic acids, an essential step in enzymatic wall degradation.
High concentrations of choline and phosphorylcholine blocked the adsorption of pneumococcal autolytic enzyme to homologous cell walls and inhibited enzymatic cell wall hydrolysis in a noncompetitive manner. Enzyme adsorption had an absolute requirement for the presence of choline residues in the wall teichoic acid. Other amino alcohols and derivatives such as ethanolamine, monomethylaminoethanolamine , and phosphorylethanolamine had no effect on enzyme adsorption or hydrolytic activity. It is proposed that enzymatic hydrolysis of cell walls requires prior adsorption of enzyme molecules to the insoluble wall substrate and that cholin residues of the wall teichoic acid have the role of adsorption ligands in this process.
D000327:Adsorption; D000581:Amidohydrolases / Q000378:metabolism*; D002473:Cell Wall / Q000502:physiology*; D002794:Choline / Q000494:pharmacology; D007700:Kinetics; D009238:N-Acetylmuramoyl-L-alanine Amidase / Q000378:metabolism*; D010767:Phosphorylcholine / Q000494:pharmacology; D013296:Streptococcus pneumoniae / Q000378:metabolism*; D013682:Teichoic Acids / Q000378:metabolism*
D013682:Teichoic Acids; D010767:Phosphorylcholine; D000581:Amidohydrolases; D009238:N-Acetylmuramoyl-L-alanine Amidase; D002794:Choline