A consensus sequence for substrate hydrolysis by rhinovirus 3C proteinase.
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.
Long
A C
AC
Dept. of Biochemistry, University of Wales College of Cardiff.
Orr
D C
DC
Cameron
J M
JM
Dunn
B M
BM
Kay
J
J
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
D010446:Peptide Fragments; D011994:Recombinant Proteins; D014764:Viral Proteins; D003546:Cysteine Endopeptidases; D000086042:3C Viral Proteases