Physiological roles of pneumococcal peptidases.
A methionyl-specific dipeptidase from Streptococcus pneumoniae has been described. This enzyme and the pneumococcal tripeptidase have been shown to be intracellular, soluble, and constitutive. In addition to their function in cleavage of peptide nutrients, these peptidases may play a role in protein synthesis and turnover.
D000596:Amino Acids / Q000378:metabolism; D002118:Calcium / Q000494:pharmacology; D002474:Cell-Free System; D002499:Centrifugation, Density Gradient; D002850:Chromatography, Gel; D003035:Cobalt / Q000494:pharmacology; D004150:Dipeptidases / Q000302:isolation & purification / Q000378:metabolism*; D004492:Edetic Acid / Q000494:pharmacology; D005947:Glucose / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D008274:Magnesium / Q000494:pharmacology; D008345:Manganese / Q000494:pharmacology; D008628:Mercury / Q000494:pharmacology; D010447:Peptide Hydrolases / Q000378:metabolism; D010455:Peptides / Q000378:metabolism; D013291:Streptococcus / Q000201:enzymology*
D000596:Amino Acids; D010455:Peptides; D003035:Cobalt; D008345:Manganese; D004492:Edetic Acid; D010447:Peptide Hydrolases; D004150:Dipeptidases; D008628:Mercury; D008274:Magnesium; D005947:Glucose; D002118:Calcium