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The Dpcarboxypeptidase of Bacillus coagulans was exclusively associated with the proto- plast membrane. The enzyme had a pH optimum of 4.9 and was sensitive to thiol reagents. The D,D-carboxypeptidase was stimulated by most divalent cations, Pb2+ and Cd2+ pro- viding the greatest degree of activation, but it was inhibited by Hg2+ and Fe2+. A particu- late L,D-carboxypeptidase was demonstrated in membrane preparations which were also able to catalyse a simple transpeptidation reaction employing D-alanine as the carboxyl acceptor. An endopeptidase activity capable of liberating D-alanyl-D-alanine from UDP-N- acetylmuramyl-~-alanyl-y-~-glutamy~-meso-2,6-diaminopime~y~-~-alanyl-~-a~anine (UDP- MurNAc-pentapeptide) was present in the cytoplasm. This appeared to be the reverse reaction of the D-alanyl-D-alanine-adding enzyme responsible for the generation of the peptidoglycan precursor UDP-MurNAc-pentapeptide.

Peptidoglycan Carboxypeptidase and Endopeptidase Activities of Bacillus coagulans NCIB 9365