Pptidase activities in group N streptococci.
Several peptidase activites in the 3 species of Group N streptococci were partly separated by gel filtration on Sephadex G-200. The peptidases identified were a general aminopeptidase of wide specificity, a tripeptidase, a proline iminopeptidase (prolyl-beta-napthylamidase), a proline iminodipeptidase and an aminopeptidase-P. The effects of temperature and pH on the stability of the enzyme activities, and the influence of the type of N source used in the growth medium on the elution pattern of the enzymes were examined.
D000626:Aminopeptidases / Q000378:metabolism; D002474:Cell-Free System; D004150:Dipeptidases / Q000378:metabolism; D004355:Drug Stability; D006863:Hydrogen-Ion Concentration; D010447:Peptide Hydrolases / Q000302:isolation & purification / Q000378:metabolism*; D011392:Proline; D013045:Species Specificity; D013291:Streptococcus / Q000201:enzymology*; D013696:Temperature
D011392:Proline; D010447:Peptide Hydrolases; D000626:Aminopeptidases; D004150:Dipeptidases