[Action of leucine aminopeptidase 1 and 2 (Aspergillus oryzae 410) on various synthetic peptides (author's transl)].
By use of di- or tripeptides as substrates, LAP 1 and LAP 2, 2 fractions from Aspergillus oryzae hydrolyze oligopeptides that possess leucine as N-terminal amino acid. LAP 1 fraction also hydrolyzes the histidyl bond. Both fractions have no activity towards peptides as glutathion, gly-pro-ala; they have low or no activity towards tyrosyl and tryptophanyl bond.
D001230:Aspergillus / Q000201:enzymology*; D001236:Aspergillus oryzae / Q000201:enzymology*; D004151:Dipeptides / Q000378:metabolism; D006868:Hydrolysis; D007931:Leucyl Aminopeptidase / Q000378:metabolism*; D009842:Oligopeptides / Q000378:metabolism; D013329:Structure-Activity Relationship
D004151:Dipeptides; D009842:Oligopeptides; D007931:Leucyl Aminopeptidase
Action de leucine aminopeptidase I et II extracellulaires d'Aspergillus oryzae (I.P.410) sur des peptides synthétiques