Presence of X-prolyl-dipeptidyl-peptidase in lactic acid bacteria.
Prolyl-dipeptidyl-peptidase activity was detected in cell extracts of 21 lactic acid bacteria tested. Using disc electrophoresis and various substrates it was possible to distinguish it from proline iminopeptidase and proline endopeptidase. Generally the activity was high and was greater than that of proline iminopeptidase of proline endopeptidase at neutral pH and at 25 degrees C.
D000626:Aminopeptidases / Q000378:metabolism; D004150:Dipeptidases / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000378:metabolism; D007778:Lactobacillus / Q000201:enzymology*; D000085822:Prolyl Oligopeptidases; D012697:Serine Endopeptidases; D013291:Streptococcus / Q000201:enzymology*
D010450:Endopeptidases; D000626:Aminopeptidases; C022450:prolyl aminopeptidase; D004150:Dipeptidases; C022454:prolyl dipeptidase; D012697:Serine Endopeptidases; D000085822:Prolyl Oligopeptidases