Peptide-Modulated Activity Enhancement of Acidic Protease Cathepsin E at Neutral pH
Table 2
Amino acid sequences of selected peptides.
Name
Paired blocks1
Amino acid sequence (N→C)2
Size (a.a.)
Activity (%)3
Frequency4
T1
S2-(s1)-α
GCPCIDFMVEVQVEVAEALLTALSLSPGL GMTATKGEFQHTGGRY
45
—
6
T2
S2-(s1)-α
SCPCIDFMVEVQVEVAEALLTALSLSPGL GMTATKGEFQHTGGRY
45
—
1
T3
S2-(s1)-α
SCPCIDFMVEVQVEVAEALLTALSLSPGL GMTAT
34
—
6
T4
S2-(s1)-α
IEGRGCPCIDFMVEVQVEVAEALLTALSL SPGS
33
175 (122)
1
T5
S2-(s1)-α
SCPCIDFMVEVQVEVAEALLTALSLSPGL GM
32
—
1
T6
S10-(s1)-α
SDDKSTTLVEVQVEVAEELWRHYHYLLHG
29
118
2
T7
β-(s2)-γ
SYKDSCIGGRGSGGGPGGIPGRIGYIG
25
111
1
T8
β-(s2)-γ
NYKDSCIGGRGSGGGPGGIPGRIGYIG
25
—
1
T9
δ
VFVVGRSCLRLARGRVHFVSG
21
—
1
T10
ε-(s1)-S2
AVDAVLGGDPNLGGHSIGSCG
21
—
1
T11
ζ
-(s1)-S1
IEGRLLSGGAGACSVRTVDDSFDCG
26
186 (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.