title: Distribution of chymoelastases and trypsin-like enzymes in five species of entomopathogenic deuteromycetes.
abstract: Nine isolates of the entomopathogenic deuteromycetes Metarhizium anisopliae, Beauveria bassiana, Verticillium lecanii, Nomuraea rileyi, and Aschersonia aleyrodis produced basic (pI greater than 7.0) chymoelastases that possessed extended binding sites, comprising at least four or five subsites, with preference for hydrophobic residues at the primary binding site. Most isolates also produced additional acidic enzymes with similar specificities against ester and amide substrates but which lacked activity against elastin. Both acidic and basic enzymes degraded high protein azure or locust cuticle and, as shown by inhibition studies, possessed essential serine and histidine residues in the active site. In spite of similarities in catalytic properties antibodies generated against a Metarhizium chymoelastase cross-reacted only with enzymes from two (out of four) Metarhizium isolates; enzymes from all other isolates did not cross-react. Two isolates of Metarhizium produced a third class of protease which degraded Bz-AA-AA-Arg-NA substrates (AA, various amino acids) and hide protein azure. Analogous peptidases were produced by other isolates but they were specific for Bz-Phe-Val-Arg-NA and showed less sensitivity to trypsin inhibitors. The possible significance to pathology of the presence of diverse yet similar protease forms in five genera of entomopathogens is discussed.
authors.affiliation: University of Bath, Avon, United Kingdom.
authors.forename: R J
authors.initials: RJ
authors.lastname: St Leger
authors.forename: R M
authors.initials: RM
authors.lastname: Cooper
authors.forename: A K
authors.initials: AK
authors.lastname: Charnley
mesh_terms: D000577:Amides / Q000378:metabolism; D001665:Binding Sites; D004549:Elastin / Q000378:metabolism; D004817:Epidermis / Q000378:metabolism; D004952:Esters / Q000378:metabolism; D007525:Isoelectric Focusing; D007700:Kinetics; D003904:Mitosporic Fungi / Q000201:enzymology*; D010447:Peptide Hydrolases / Q000378:metabolism; D011480:Protease Inhibitors / Q000494:pharmacology; D012697:Serine Endopeptidases / Q000378:metabolism*; D015842:Serine Proteinase Inhibitors; D013379:Substrate Specificity; D014357:Trypsin / Q000378:metabolism*; D014361:Trypsin Inhibitors / Q000494:pharmacology
chemical_list: D000577:Amides; D004952:Esters; D011480:Protease Inhibitors; D015842:Serine Proteinase Inhibitors; D014361:Trypsin Inhibitors; D004549:Elastin; D010447:Peptide Hydrolases; D012697:Serine Endopeptidases; C053722:chymoelastase; D014357:Trypsin