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LPXTGase of S. pyogenes contains 7 lysine residues. However, trypsin digestion of the enzyme yields only two tryptic fragments. Exhaustive dinitrophenylation of the enzyme and subsequent hydrolysis of the dinitrophenylated enzyme by 6N HCl revealed that, of the 7 lysine residues present in the enzyme, only two lysine residue are dinitrophenylated, while five are not, indicating that both α-amino group and Ɛ-aminogroups of five lysine residues are linked internally to uncharacterized amino acids in the enzyme. When S. pyogenes was grown in a sub-lethal dose of penicillin, LPXTGase synthesis in the organism is greatly reduced, suggesting that the cross-linking in the LPXTGase molecule is mediated by penicillin binding proteins. A knockout of the transpeptidase domains of penicillin binding proteins 1a and 1b produced less LPXTGase, but a transpeptidase knockout mutant of a single penicillin binding protein did not completely abolish LPXTGase production, indicating that more than one penicillin binding protein cooperatively participate in the internal cross-linking of LPXTGase. DOI: 10.29011/JMGE-114. 000114

journal of microbiology and genetics

LPXTGase of S. pyogenes is Internally Cross-Linked Through the ε-Amino Groups of Lysines and the Cross-Linking is Catalyzed by Penicillin-Binding Proteins