Structural and functional diversities in lepidopteran serine proteases |
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Authors: | Ajay Srinivasan Ashok P Giri Vidya S Gupta |
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Institution: | (1) Plant Molecular Biology Group, Division of Biochemical Sciences, National Chemical Laboratory, Pune, 411008, India |
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Abstract: | Primary protein-digestion in Lepidopteran larvae relies on serine proteases like trypsin and chymotrypsin. Efforts toward
the classification and characterization of digestive proteases have unraveled a considerable diversity in the specificity
and mechanistic classes of gut proteases. Though the evolutionary significance of mutations that lead to structural diversity
in serine proteases has been well characterized, detailing the resultant functional diversity has continually posed a challenge
to researchers. Functional diversity can be correlated to the adaptation of insects to various host-plants as well as to exposure
of insects to naturally occurring antagonistic biomolecules such as plant-derived protease inhibitors (PIs) and lectins. Current
research is focused on deciphering the changes in protease specificities and activities arising from altered amino acids at
the active site, specificity-determining pockets and other regions, which influence activity. Some insight has been gained
through in silico modeling and simulation experiments, aided by the limited availability of characterized proteases. We examine the structurally
and functionally diverse Lepidopteran serine proteases, and assess their influence on larval digestive processes and on overall
insect physiology.
Invited paper |
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Keywords: | Functional diversity Lepidoptera Serine protease Structural diversity |
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