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. 2004 Apr;16(4):857–873. doi: 10.1105/tpc.017947

Table 4.

Hydrolytic Activity of SAS-1 and SAS-2 toward Caspase and Granzyme B Substrates

Percentage of Z-VAD-AFC
Substrate Protease with Optimal Specificity SAS-1 SAS-2
Z-VAD-AFCa Pan-caspase 100% ± 1.2% 100% ± 1.9%
Z-YVAD-AFCa Caspase-1 19% ± 2.1% 28% ± 2.5%
Z-VDVAD-AFCa Caspase-2 0% ± 0% 0% ± 0%
Z-DEVD-AFCa Caspase-3 0% ± 0% 0% ± 0%
Ac-LEVD-AFCa Caspase-4 39% ± 4.4% 51% ± 2.6%
Z-WEHD-AFCa Caspase-5 0% ± 0% 0% ± 0%
Ac-VEHD-AFCa Caspase-6 311% ± 21.5% 366% ± 15.6%
Ac-VEID-AFCa Caspase-6 0% ± 0% 0% ± 0%
Ac-VKMD-AFCa Caspase-6 623% ± 32.5% 654% ± 28.8%
Ac-VNLD-AFCa Caspase-6 384% ± 18.2% 521% ± 21.8%
Ac-IETD-AFCa Caspase-8 130% ± 10.1% 172% ± 14.7%
Ac-LEHD-AFCa Caspase-9 105% ± 9.6% 140% ± 10.2%
Z-AAD-AFCa Granzyme B 144% ± 13.9% 183% ± 20.1%

Z-VAD-AFC was used as the 100% control.

Z, benzyloxycarbonyl; Ac, acetyl; AFC, 7-amido-4-(trifluoromethyl)coumarin.

a

Recognition sequence in single-letter amino acid code.