Proteomics comparison of aspartic protease enzyme in insects

Abstract

IntroductionProteases (peptidases or proteinases) are a large category of enzymes that catalyze the hydrolysis of peptide bonds. Proteases that cleave peptide bonds within the polypeptide chain are classified as endopeptidases, and those that cleave peptide bonds at the N or C termini of polypeptide chains are known as exopeptidases (López-Otín and Bond, 2008). Thus, the term "protease" includes both "endopeptidases" and "exopeptidases", while the term "proteinase" is used to describe only "endopeptidases" (Ryan, 1990). Proteases are present in all organisms and are involved in various physiological processes, including the production of nutrients for cell growth and proliferation (Lin et al., 2011), for protein degradation (Ciechanover, 2005), and as regulatory components for diverse physiological functions (Ehrmann and Clausen, 2004;Oikonomopoulou et al., 2006). Proteases include aspartic, cysteine, glutamic, serine, and threonine proteases, depending on the amino acids present in the active site, or the metalloproteases, if a metal ion is required for catalytic activity (Alagarsamy et al., 2006). Microbial-sourced proteases are invaluable commercial enzymes and account for approximately 60% of the total worldwide sales of industrial enzymes

De Novo characterization of transcriptomes from two North American Papaipema stem-borers (Lepidoptera: Noctuidae)

“…Aspartic peptidases, which break down the peptide bonds in dietary proteins, are essential to the survival of plant feeding insects [ 51 ]. Lineage-specific evolution of aspartic peptidases appears to be common in insects with different feeding habits [ 52 ]. Within Papaipema , the presence of species-specific genes in these two categories suggests they may contribute to sensory and digestive adaptations to endophagous feeding.…”