Digestive peptidase evolution in holometabolous insects led to a divergent group of enzymes in Lepidoptera

摘要: Abstract Trypsins and chymotrypsins are well-studied serine peptidases that cleave peptide bonds at the carboxyl side of basic hydrophobic l -amino acids, respectively. These enzymes largely responsible for digestion proteins. Three primary processes regulate activity these peptidases: secretion, precursor (zymogen) activation substrate-binding site recognition. Here, we present a detailed phylogenetic analysis trypsins in three orders holometabolous insects reveal divergent characteristics Lepidoptera comparison with those Coleoptera Diptera. In particular, trypsin subsite S1 was more hydrophilic than Diptera, whereas subsites S2–S4 were hydrophobic, suggesting different substrate preferences. Furthermore, displayed lineage-specific group belonging only to Noctuidae family. Evidence facilitated auto-activation events also observed all insect studied, characteristic zymogen motif complementary active site. contrast, did not seem have peculiar evolutionary history respect their mammal counterparts. Overall, our findings suggest need fast allowed evolve groups high rates, highlight evolution led most diverse Lepidoptera.