title: New chelator-sensitive proteases in matrix of yeast mitochondria.
abstract: Proteases in yeast mitochondria were studied using fluorogenic synthetic substrates containing methylcoumaryl amide (MCA). Among the eleven substrates which are commonly employed for several types of proteases, Leu-MCA, Arg-MCA, Boc-Gln-Arg-Arg-MCA and Boc-Phe-Ser-Arg-MCA were found to be highly susceptible to proteases in mitochondria. All these proteases were localized in the matrix and sensitive to o-phenanthroline but not to phenylmethylsulfonyl fluoride or iodoacetate. The analysis of hydrolyzed products of Boc-Gln-Arg-Arg-MCA indicated that the peptide was cleaved at the site between Gln and Arg. These results demonstrate that there exist chelator-sensitive aminopeptidase(s) and endopeptidases in the matrix of yeast mitochondria.
mesh_terms: D000626:Aminopeptidases / Q000378:metabolism; D002614:Chelating Agents / Q000494:pharmacology; D010450:Endopeptidases / Q000378:metabolism; D008928:Mitochondria / Q000201:enzymology; D009842:Oligopeptides; D010447:Peptide Hydrolases / Q000378:metabolism*; D010618:Phenanthrolines / Q000494:pharmacology; D011480:Protease Inhibitors; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D013379:Substrate Specificity
chemical_list: D002614:Chelating Agents; D009842:Oligopeptides; D010618:Phenanthrolines; D011480:Protease Inhibitors; D010450:Endopeptidases; D010447:Peptide Hydrolases; D000626:Aminopeptidases; C025205:1,10-phenanthroline