Research Article

Peptide-Modulated Activity Enhancement of Acidic Protease Cathepsin E at Neutral pH

Table 2

Amino acid sequences of selected peptides.

NamePaired blocks1Amino acid sequence (N→C)2Size (a.a.)Activity (%)3Frequency4

T1S2-(s1)-αGCPCIDFMVEVQVEVAEALLTALSLSPGL
GMTATKGEFQHTGGRY
456
T2S2-(s1)-αSCPCIDFMVEVQVEVAEALLTALSLSPGL
GMTATKGEFQHTGGRY
451
T3S2-(s1)-αSCPCIDFMVEVQVEVAEALLTALSLSPGL
GMTAT
346
T4S2-(s1)-αIEGRGCPCIDFMVEVQVEVAEALLTALSL
SPGS
33175 (122)1
T5S2-(s1)-αSCPCIDFMVEVQVEVAEALLTALSLSPGL
GM
321
T6S10-(s1)-αSDDKSTTLVEVQVEVAEELWRHYHYLLHG29118 2
T7β-(s2)-γSYKDSCIGGRGSGGGPGGIPGRIGYIG25111 1
T8β-(s2)-γNYKDSCIGGRGSGGGPGGIPGRIGYIG251
T9δVFVVGRSCLRLARGRVHFVSG211
T10ε-(s1)-S2AVDAVLGGDPNLGGHSIGSCG211
T11ζ -(s1)-S1IEGRLLSGGAGACSVRTVDDSFDCG26186 (138)1

1See Table 1 for block names detail. Novel blocks were temporarily labeled as α, β, γ, δ, ε, and ζ.
2Bold regions were contained in the original blocks.
3Peptides for activity assay were obtained by in vitro translation (in italic) or chemical synthesis (in bold). In this study, the discrepancy is unexpectedly large and adverse to our previous experiences due to unknown reason [19].
4Copy numbers found in sequenced clones.