title: Cleavage efficiency by adenovirus protease is site-dependent.
abstract: The adenovirus protease cleaves consensus sequences (M/I/L)XGX-G and (M/I/L)XGG-X. Using purified recombinant protease, we showed that a peptide bearing the GX-G site was hydrolyzed more rapidly than a peptide bearing the GG-X site. The GX-G site was also preferentially cleaved on viral protein pVI which bears both sites of cleavage. Evidence is presented that suggests a biological role for this differential cleavage efficiency.
authors.affiliation: Department of Microbiology, Faculty of Medicine, University of Sherbrooke, Quebec, Canada J1H 5N4. j.weber@courrier.usherb.ca
authors.forename: M
authors.initials: M
authors.lastname: Diouri
authors.forename: H
authors.initials: H
authors.lastname: Keyvani-Amineh
authors.forename: K F
authors.initials: KF
authors.lastname: Geoghegan
authors.forename: J M
authors.initials: JM
authors.lastname: Weber
mesh_terms: D000260:Adenoviruses, Human / Q000201:enzymology*; D000595:Amino Acid Sequence; D002213:Capsid / Q000378:metabolism; D016384:Consensus Sequence; D003546:Cysteine Endopeptidases / Q000378:metabolism*; D010450:Endopeptidases / Q000378:metabolism*; D011498:Protein Precursors / Q000378:metabolism; D013379:Substrate Specificity
chemical_list: D011498:Protein Precursors; D010450:Endopeptidases; D003546:Cysteine Endopeptidases