Cleavage efficiency by adenovirus protease is site-dependent.
J Biol Chem
; 271(51): 32511-4, 1996 Dec 20.
Article
in En
| MEDLINE
| ID: mdl-8955073
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.
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Collection:
01-internacional
Database:
MEDLINE
Main subject:
Endopeptidases
/
Cysteine Endopeptidases
/
Adenoviruses, Human
Language:
En
Journal:
J Biol Chem
Year:
1996
Document type:
Article