Conformational changes on ligand binding in wild-type and mutants from Spodoptera frugiperda midgut trehalase.

ABSTRACT: Trehalase specifically hydrolyses trehalose into two glucose units and is most important in insects and fungi. Previous evidence suggested that Spodoptera frugiperda midgut trehalase (wild type, WT) has substantial conformational changes on binding different substances. Our goal is to understand this mobility. For this, two deletion mutants were produced, lacking regions supposed to be the cause of mobility [(102 residues from the N-terminus (NT) and this portion plus 31 residues from the C-terminus (NCT)]. Circular dichroism spectra before and after denaturation of the enzymes support the assertion that they are appropriately folded. The overall results show that the removal of 102 or 133 amino acids does not greatly change the interaction with the substrate and competitive inhibit

SUBMITTER: Silva W 

PROVIDER: S-EPMC5668925 | biostudies-literature | 2015 Dec

REPOSITORIES: biostudies-literature