cytotoxic chymotrypsin-like serine protease with preference for bulky and aromatic residues at the P1 position and acidic residues at the P3' and P4' sites
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cytotoxic chymotrypsin-like serine protease with preference for bulky and aromatic residues at the P1 position and acidic residues at the P3' and P4' sites
the enzyme induces cell death primarily via a Bcl-2-sensitive mitochondrial cell death pathway that does not require direct Bid activation, overview. Neither the apoptosome nor caspase-3 is essential to the induction of GrH-mediated cell death. The enzyme might have pro-apoptotic activity that might be distinct from that of granzyme B and FasL, which can be relevant when Fas/FasL or granzyme B activity or death pathways are impaired. Direct processing of DFF45 by the enzyme may be leading to DNA damage. The enzyme inhibits caspase-3 activation
granzyme H is a serine protease, initially produced as a zymogen that requires the activity of granule-resident cathepsin C to become active. Cell death in cytotoxic potential of the enzyme with replication-deficient adenovirus 5 in target cells, i.e. K562 cells, Jurkat cells, and EBV-transformed B cell line RPMI-8866,the enzyme is less effective against tumor cells. Enzyme GrH induces cytochrome C loss from the mitochondrial intermembrane space. Similar to cytochrome C, SMAC/DIABLO is also observed to undergo translocation from the mitochondria to the cytosol after treatment with the enzyme
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