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. 1997 Jun 1;324(Pt 2):361–364. doi: 10.1042/bj3240361

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

Q Zhou 1, G S Salvesen 1
PMCID: PMC1218439  PMID: 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.

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Selected References

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