title: Purification and characterization of an aminopeptidase from the edible basidiomycete Grifola frondosa.
abstract: An aminopeptidase was purified 178-fold from an extract of Grifola frondosa by ammonium sulfate precipitation and a series of column chromatographies on phenyl-Toyopearl, Sephadex G-25, and Mono-Q. The molecular mass of the enzyme was estimated to be 27 kDa and 30 kDa by gel filtration and SDS-PAGE, respectively. The enzyme had an optimum pH of 8.5 and was stable between pH 6.0 and pH 10.5, and it also had a high level of heat stability. The enzyme was inactivated by EDTA and o-phenanthroline, and it was also strongly inhibited by bestatin, but no inhibitory effect of DFP was observed. The enzyme preferentially hydrolyzed peptides containing hydrophobic residues in the N-terminal position.
authors: National Food Research Institute, Ministry of Agriculture, Forestry, and Fisheries, Tsukuba, Ibaraki, Japan. nisiwaki@ari.pref.niigata.jp
authors: T
authors: T
authors: Nishiwaki
authors: K
authors: K
authors: Hayashi
mesh_terms: D000363:Agaricales / Q000201:enzymology*; D000595:Amino Acid Sequence; D000626:Aminopeptidases / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D002413:Cations, Divalent / Q000494:pharmacology; D004492:Edetic Acid / Q000494:pharmacology; D004795:Enzyme Stability; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D007930:Leucine / Q000031:analogs & derivatives / Q000494:pharmacology; D008970:Molecular Weight; D010618:Phenanthrolines / Q000494:pharmacology; D013379:Substrate Specificity
chemical_list: D002413:Cations, Divalent; D010618:Phenanthrolines; D004492:Edetic Acid; D000626:Aminopeptidases; D007930:Leucine; C012211:ubenimex; C025205:1,10-phenanthroline