Conformational and activity changes on subtilisin cleavage of carboxypeptidase A.
D001224:Aspartic Acid; D001407:Bacillus / Q000201:enzymology; D001419:Bacteria / Q000201:enzymology; D001593:Benzyl Compounds; D001665:Binding Sites; D002268:Carboxypeptidases; D002384:Catalysis; D002942:Circular Dichroism; D010450:Endopeptidases; D005561:Formates; D005998:Glycine; D006626:Hippurates; D006868:Hydrolysis; D007531:Isoflurophate; D007700:Kinetics; D007773:Lactates; D009578:Nitrobenzenes; D010196:Pancreatic Elastase; D010649:Phenylalanine; D011402:Pronase; D011422:Propionates; D011487:Protein Conformation; D012694:Serine
D001593:Benzyl Compounds; D005561:Formates; D006626:Hippurates; D007773:Lactates; D009578:Nitrobenzenes; D011422:Propionates; D007531:Isoflurophate; D001224:Aspartic Acid; D012694:Serine; D010649:Phenylalanine; D002268:Carboxypeptidases; D010450:Endopeptidases; D010196:Pancreatic Elastase; D011402:Pronase; D005998:Glycine