Fig. 3
From: Engineering mouse chymotrypsin B1 for improved trypsinogen degradation
Amino-acid sequence and evolutionary conservation of the peptide segment in mouse anionic (T8) and cationic (T7) trypsinogen cleaved by mouse CTRB1. Note that the amino-acid numbering is shifted by 1 between the two trypsinogen isoforms. (A) Chymotrypsin cleavage sites in mouse trypsinogens. The peptide bonds cleaved by mouse CTRB1 are indicated by arrows and the P1 residues are highlighted in red. The conserved Cys residues are shown in yellow, and Asp156 is in green. (B) Evolutionary conservation profiling of the chymotryptic cleavage-site regions in mouse anionic (T8) and cationic (T7) trypsinogens. Amino acids are indicated with their one-letter code. The logo was created with the WebLogo application (https://weblogo.berkeley.edu/logo.cgi). The input sequence set was generated by multiple sequence alignment of natural trypsinogen homologs, as described in “Materials & methods”. The incidence of Phe150 and Asp156 among the anionic (T8) trypsinogen homologues were 3.2% and 47.2%, respectively. The height of each column indicates the level of evolutionary conservation (frequency) at the given position. Chemical characteristics of the amino-acid residues are color-coded as follows: aliphatic is green, aromatic is orange, acidic is red, basic is blue, polar without charge is pink, and Cys, Gly, Pro are black. The corresponding amino-acid sequences of mouse T8 and T7 trypsinogens are also shown.
