title: Characterization of the proteolytic activity firmly attached to yeast phoshoenolpyruvate carboxykinase.
abstract: Incubation of partially purified yeast phosphoenolpyruvate carboxykinase (ATP:oxaloacetate carboxy-lyase (transphosphorylating), EC 4.1.1.49) with 5% mercaptoethanol and 0.01% sodium dodecyl sulfate at 37 degrees C results in degradation of the enzyme. The degradation can be partially prevented by addition of proteinase B inhibitor 2 or phenylmethylsulfonyl fluoride, an inhibitor of proteinase B and carboxypeptidase Y. The degradation can be completely inhibited by addition of proteinase B inhibitor 2 together with pepstatin, and inhibitor of proteinase A. Thus it appears that proteolytic activities are firmly attached to phosphoenolpyruvate carboxykinase and are identical with the yeast proteinases A and B. The latter conclusion was supported by experiments using the pure yeast proteinases.
mesh_terms: D016282:Aspartic Acid Endopeptidases; D002268:Carboxypeptidases / Q000494:pharmacology; D043402:Cathepsin A; D010450:Endopeptidases / Q000378:metabolism*; D006023:Glycoproteins / Q000494:pharmacology; D010436:Pepstatins / Q000494:pharmacology; D010664:Phenylmethylsulfonyl Fluoride / Q000494:pharmacology; D010729:Phosphoenolpyruvate Carboxykinase (GTP) / Q000378:metabolism*; D011480:Protease Inhibitors / Q000494:pharmacology; D011489:Protein Denaturation; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D029701:Saccharomyces cerevisiae Proteins; D012697:Serine Endopeptidases
chemical_list: D006023:Glycoproteins; D010436:Pepstatins; D011480:Protease Inhibitors; D029701:Saccharomyces cerevisiae Proteins; C018169:yeast proteinase B inhibitor; D010664:Phenylmethylsulfonyl Fluoride; D002268:Carboxypeptidases; D010450:Endopeptidases; D043402:Cathepsin A; C499283:PRC1 protein, S cerevisiae; C022633:serine carboxypeptidase; D012697:Serine Endopeptidases; C023302:yeast proteinase B; C022325:aspartic proteinase A; D016282:Aspartic Acid Endopeptidases; D010729:Phosphoenolpyruvate Carboxykinase (GTP)