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Activation of pro-caspase-7 by serine proteases includes a non-canonical specificity.


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.

SUBMITTER: Zhou Q 

PROVIDER: S-EPMC1218439 | biostudies-other | 1997 Jun

REPOSITORIES: biostudies-other

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