| Literature DB >> 9182691 |
Abstract
As a model to investigate the mechanism of caspase activation we have analysed the processing of pro-caspase-7 by serine proteases with varied specificities. The caspase-7 zymogen was rapidly activated by granzyme B and more slowly by subtilisin and cathepsin G, generating active enzymes with similar kinetic properties. Significantly, cathepsin G activated the zymogen by cleaving at a Gln-Ala bond, indicating that the canonical cleavage specificity at aspartic acid is not required for activation.Entities:
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Year: 1997 PMID: 9182691 PMCID: PMC1218439 DOI: 10.1042/bj3240361
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857