Comparative bioinformatic and structural analyses of pepsin and renin

Identification of Di/Tripeptide(s) With Osteoblasts Proliferation Stimulation Abilities of Yak Bone Collagen by in silico Screening and Molecular Docking

“…Three common proteases in food laboratories, namely, trypsin, proteinase K, and pepsin, were selected to predict their yak bone collagen-I hydrolysis capacities. Pepsin, a kind of aspartic protease rich in polar and aspartic acid residues ( 40 ), has different enzyme cutting sites at different pH values. Therefore, the hydrolysis capacity of pepsin was considered, respectively, at pH > 2 and pH 1.3.…”

Comprehensive bioinformatics-based annotation and functional characterization of bovine chymosin protein revealed novel biological insights

“…Notably, Vallejo et al demonstrated that recombinant goat chymosin displayed superior catalytic efficiency compared to buffalo, bovine, or camel versions ( Vallejo et al, 2012 ). In another study, Grahame et al used bioinformatic tools to compare the structure and sequence of renin and pepsin ( Grahame et al, 2020 ). By analyzing key residues, motifs, solvent exposure, and flexibility, they attempted to understand why aspartic proteases are stable at different pH levels.…”

Bioinformatic analysis of subfamily-specific regions in 3D-structures of homologs to study functional diversity and conformational plasticity in protein superfamilies

“…Interest in the analysis of functionally important specific positions is a long-standing trend in computational biology: the concept was introduced in late 1990s [9] , [10] , the first systematic approach to identify such positions/residues in protein sequences was published in 2002 [11] , followed by a variety of improvements to increase the accuracy of predictions and facilitate the ease-of-use in the daily routine [3] , [5] , [7] , [12] , [13] . In particular, the original Zebra/Zebra2 approach [14] to identify SSPs/SDPs in multiple sequence alignments was recognized as a tool [15] , [16] to help studying structure–function relationship in protein superfamilies [17] , [18] , [19] , and used to assist experimental design of improved enzymes [20] and ligand binding specificity [21] .…”