Activation of pro-caspase-7 by serine proteases includes a non-canonical specificity
Q Zhou, GS Salvesen - Biochemical Journal, 1997 - portlandpress.com
Q Zhou, GS Salvesen
Biochemical Journal, 1997•portlandpress.comAs 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.
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.
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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