@article{mbs:/content/journal/micro/10.1099/00221287-111-2-327, author = "Mcarthur, Hamish A. I. and Reynolds, Peter E.", title = "Peptidoglycan Carboxypeptidase and Endopeptidase Activities of Bacillus coagulans NCIB 9365", journal= "Microbiology", year = "1979", volume = "111", number = "2", pages = "327-335", doi = "https://doi.org/10.1099/00221287-111-2-327", url = "https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-111-2-327", publisher = "Microbiology Society", issn = "1465-2080", type = "Journal Article", abstract = "The D,D-carboxypeptidase 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+ providing the greatest degree of activation, but it was inhibited by Hg2+ and Fe2+. A particulate 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-L-Alanyl-y-γ-D-glutamy-meso-2,6-diaminopimelyl-D-alanyl-D-alanine (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.", }