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. Author manuscript; available in PMC: 2011 Jun 21.
Published in final edited form as: Biochemistry. 2006 Nov 7;45(44):13249–13263. doi: 10.1021/bi0611964

Table 2.

Summary of V8 and Trypsin Proteolysis

V8 Protease
protein cleavage site
comments loops affected by mutation
E248/D253 E25 E98/E106 E173/E190
procaspase-3 + + + + bands 2 and 3, 16–18 and 38 kDa bands −
D3A/E167Aa − + − − removal of prodomain at E25 is the only cleavage L2′ and L4
D169A + + + very little very slow kinetics of cleavage L2′ and L4
D3A/E173A − + − − cleavage of prodomain at E25;
8 kDa band arises from alternate processing		 L2′ and L4
D3A/Y203F + + + + cleavage kinetics similar to those of the control none
caspase-3 + − − + cleavage at E173; no cleavage at E190 –
E167A + − − + cleavage kinetics similar to those of the control none
E173A + − − + cleavage kinetics similar to those of the control none
Y203F + − − + cleavage kinetics similar to those of the control none
Trypsin Protease
cleavage site
loops affected
protein K57/R64 R207 comments by mutation
procaspase-3 + + cleavage in L1 and L3 –
D3A/E167A + + cleavage kinetics similar to those of the procaspase control none
D3A/D169A + + cleavage kinetics similar to those of the procaspase control none
D3A/Y203F + + cleavage kinetics similar to those of the procaspase control none
caspase-3 + (large subunit) + (small subunit) cleavage is ~10 times faster than for the procaspase –
E167A + + cleavage kinetics similar to those of the caspase control none
E173A + + cleavages at K57/R64 and R207 much slower than for the control L1 and L3
Y203F + + cleavage at K57/R64 slower than for the control;
cleavage at R207 much slower than for the control		 L1 and L3
a

D3A refers to procaspase-3(D9A/D28A/D175A).