{'fraction_non_alphanumeric': 0.01859799713876967, 'fraction_numerical': 0.002861230329041488, 'mean_word_length': 5.537383177570093, 'pattern_counts': {'":': 0, '<': 0, '<?xml version=': 0, '>': 0, 'https://': 0, 'lorem ipsum': 0, 'www.': 0, 'xml': 0}, 'pii_count': 0, 'substrings_counts': 0, 'word_list_counts': {'cursed_substrings.json': 0, 'profanity_word_list.json': 0, 'sexual_word_list.json': 0, 'zh_pornsignals.json': 0}}
Structural ensemble-based computational analysis of trypsin enzyme genes discovered highly conserved peptide motifs in insects

Abstract Trypsin is the major protease enzyme existing in the midgut of most insect species. Despite the importance of trypsin enzymes in insects, there is no comprehensive evidence available on the structure and function of this enzyme. Therefore, in the present study, trypsin enzymes from different species including insect and other organisms were analyzed using bioinformatics approaches. Ten motifs were found by MEME and MAST tools, which similarly existed in all various insect species. Moreover, the phylogenetic study revealed a high similarity among the insect trypsins, suggesting that they might have derived from a common ancestor. To understand the characteristics of insect trypsins, including active binding site structure, a reliable structural model of trypsin for the studied species was predicted using I-TASSER program. Furthermore, relying on the results of Predotar server, the studied trypsins contained R targeting sequences representing 99% probability. In protein– protein interactions analysis obtained by STRING 11 tool, ten enriched pathways were known in D. melanogaster trypsin. This study shed more lights on the unique features of insect trypsin enzymes and can be a basis for designing specific inhibitors to insects’ trypsin enzymes.