Enzymatic Synthesis of N-Acetylglucosaminylribitol Linkages in Teichoic Acid from Staphylococcus aureus, Strain Copenhagen

SUMMARY A particulate enzyme preparation from Staphylococcus aureus, strain Copenhagen, catalyzed the transfer of acetylglucosamine residues from uridine diphosphoacetylglucosamine to an accep- tor, termed, a-acetylglucosaminylpolyribitol phosphate, with simultaneous formation of uridine diphosphate. The acceptor was obtained by treating the teichoic acid isolated from this strain with /I-N-acetylglucosaminidase. Teichoic acid itself was inactive as acceptor. The enzyme preparation catalyzed the synthesis of both (Y- and &acetylglucosaminylribitol units in about the same proportion as these are found in the teichoic acid isolated from the cell walls of this organism. Some properties of this enzyme preparation have been described. REFERENCES 1. BADDILEY, J., PYOC. Che,)r. Sot., 177 (1959). 2. KINDERSON, A.R., J~ERGENs,~.~., ANLI QTROMINGER, J.L., Biochem. and Bioph ys. Research C’onw~uns., 6. 472 (1961).