title: Solubilization and isolation of the membrane-bound DD-carboxypeptidase of Streptococcus faecalis ATCC9790. Properties of the purified enzyme.
abstract: Streptococcus faecalis ATCC 9790 possesses six membrane-bound, penicillin-binding proteins. That numbered 6 (Mr 43000) is the most abundant one and is the DD-carboxypeptidase studied previously. The enzyme has been solubilized and purified to the stage where one single protein band can be detected by gel electrophoresis. The purification procedure does not alter the properties that the enzyme exhibits when it is membrane-bound. The DD-carboxypeptidase itself may be a killing target for penicillin in S. faecalis.
mesh_terms: D002268:Carboxypeptidases / Q000378:metabolism*; D002352:Carrier Proteins / Q000302:isolation & purification; D002462:Cell Membrane / Q000201:enzymology*; D003023:Cloxacillin / Q000378:metabolism; D013293:Enterococcus faecalis / Q000187:drug effects / Q000201:enzymology*; D002267:Muramoylpentapeptide Carboxypeptidase / Q000302:isolation & purification / Q000378:metabolism*; D009842:Oligopeptides / Q000378:metabolism; D010400:Penicillin G / Q000378:metabolism; D010406:Penicillins / Q000378:metabolism; D012995:Solubility
chemical_list: D002352:Carrier Proteins; D009842:Oligopeptides; D010406:Penicillins; D002268:Carboxypeptidases; D002267:Muramoylpentapeptide Carboxypeptidase; D003023:Cloxacillin; D010400:Penicillin G