[Isolation and properties of leucine aminopeptidase from Aspergillus oryzae].
Homogenious leucine aminopeptidase is purified from "oryzine"--mixture of enzymes produced by surface culture of Asperigillus oryzae using treatment with activated characoal, followed by DEAE-cellulose and hydroxylapatite chromatographies, Biogel P-100 gel-filtration and polyacrylamide-gel electrophoresis. The enzyme has pH optimum 9.0 and the molecular weight 37500 as estimated by gil-filtration through Sephadex G-100 (superfine) and SDS-polyacrylamide gel electrophoresis. Leucine aminopeptidase from Asp. oryzae has a broad substrate specificity, therefore, cleaving with the highest rate the peptides carrying N-terminal leucine. The enzyme is completely inhibited with EDTA and beta-mercaptoethanol, and it is a metalloenzyme.
D001230:Aspergillus / Q000201:enzymology*; D001236:Aspergillus oryzae / Q000201:enzymology*; D004492:Edetic Acid / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D007931:Leucyl Aminopeptidase / Q000037:antagonists & inhibitors / Q000302:isolation & purification* / Q000378:metabolism; D008623:Mercaptoethanol / Q000494:pharmacology; D008667:Metalloproteins / Q000302:isolation & purification; D008970:Molecular Weight; D013329:Structure-Activity Relationship
D008667:Metalloproteins; D008623:Mercaptoethanol; D004492:Edetic Acid; D007931:Leucyl Aminopeptidase
Vydelenie i svoistva leitsinaminopeptidazy iz Aspergillus oryzae.