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Figure 5 | BMC Evolutionary Biology

Figure 5

From: Molecular co-evolution of a protease and its substrate elucidated by analysis of the activity of predicted ancestral hatching enzyme

Figure 5

P2 site preference of rFLCE, rMLCE, FLCE_mu4, and MLCE_mu4. Cleavage activities of rFLCE (A), rMLCE (B), MLCE_mu4 (C), and FLCE_mu4 (D) towards wild-type, shown in FigureĀ 2C, peptide 2, and mutant medaka mid-ZPd peptides whose P2 sites were substituted with various amino acid residues. Letters under the horizontal axis show the amino acid residues at the P2 sites of the peptides. The P2 site residue of the wild-type peptide is P.

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