Comparative peptide specificity of cell wall, membrane and intracellular peptidases of group N streptococci.
Solubilized cell walls of group N streptococci contain two electrophoretically distinct peptidases, one of which hydrolysed trileucine only, while the second hydrolysed a wide range of di- and tripeptides. Neither enzyme possessed leucine aminopeptidase or endopeptidase activity. Four and three peptidases, respectively, were separated in intracellular extracts of Streptococcus lactis subsp. lactis and Strep. lactis subsp. cremoris produced by osmotic lysis of spheroplasts. In contrast with the cell-wall extracts, two of the peptidases had broad specificites, though only one of these hydrolysed trileucine. Purified membranes of Strep. lactis subsp. lactis contained only one electrophoretically distinct peptidase of very narrow specificity. There were small differences between the numbers of peptides hydrolysed by cell wall preparations from milk-grown or broth-grown cells.
D002462:Cell Membrane / Q000201:enzymology; D002473:Cell Wall / Q000201:enzymology; D004150:Dipeptidases / Q000378:metabolism; D004151:Dipeptides / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D013294:Lactococcus lactis / Q000201:enzymology*; D009842:Oligopeptides / Q000378:metabolism; D010447:Peptide Hydrolases / Q000378:metabolism*; D013104:Spheroplasts / Q000201:enzymology; D013291:Streptococcus / Q000201:enzymology*; D013379:Substrate Specificity
D004151:Dipeptides; D009842:Oligopeptides; D010447:Peptide Hydrolases; D004150:Dipeptidases; C036671:leucyl-leucyl-leucine