title: A consensus sequence for substrate hydrolysis by rhinovirus 3C proteinase.
abstract: Kinetic constants were determined for the hydrolysis of a series of synthetic peptide substrates by recombinant rhinovirus (HRV 14) 3C proteinase. Systematic removal or replacement of individual residues indicated that the minimum sequence required for effective cleavage by the viral cysteine proteinase was P5-Val/Thr-P3-P2-Gln-Gly-Pro.
authors.affiliation: Dept. of Biochemistry, University of Wales College of Cardiff.
authors.forename: A C
authors.initials: AC
authors.lastname: Long
authors.forename: D C
authors.initials: DC
authors.lastname: Orr
authors.forename: J M
authors.initials: JM
authors.lastname: Cameron
authors.forename: B M
authors.initials: BM
authors.lastname: Dunn
authors.forename: J
authors.initials: J
authors.lastname: Kay
mesh_terms: D000086042:3C Viral Proteases; D000595:Amino Acid Sequence; D001665:Binding Sites; D003001:Cloning, Molecular; D003546:Cysteine Endopeptidases / Q000235:genetics / Q000378:metabolism*; D006868:Hydrolysis; D007700:Kinetics; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000378:metabolism; D011994:Recombinant Proteins / Q000378:metabolism; D012229:Rhinovirus / Q000201:enzymology* / Q000235:genetics; D013379:Substrate Specificity; D014764:Viral Proteins
chemical_list: D010446:Peptide Fragments; D011994:Recombinant Proteins; D014764:Viral Proteins; D003546:Cysteine Endopeptidases; D000086042:3C Viral Proteases