02108nas a2200241   4500008004100000022001400041245007600055210006900131260008100200300001200281490000700293520126000300653002801560653002601588653002401614653001401638653001401652100001701666700002201683700002401705700002501729856011201754       2015                        eng d  a0959-665800aInsect trehalase: physiological significance and potential applications0 aInsect trehalase physiological significance and potential applic  aJOURNALS DEPT, 2001 EVANS RD, CARY, NC 27513 USAbOXFORD UNIV PRESS INCcAPR  a357-3670 v253 a<p>Trehalose, a non-reducing disaccharide, is widespread throughout the biological world. It is the major blood sugar in insects playing a crucial role as an instant source of energy and in dealing with abiotic stresses. The hydrolysis of trehalose is under the enzymatic control of trehalase. The enzyme trehalase is gaining interest in insect physiology as it regulates energy metabolism and glucose generation via trehalose catabolism. The two forms of insect trehalase namely, Tre-1 and Tre-2, are important in energy supply, growth, metamorphosis, stress recovery, chitin synthesis and insect flight. Insect trehalase has not been reviewed in depth and the information available is quite scattered. The present mini review discusses our recent understanding of the regulation, mechanism and biochemical characterization of insect trehalase with respect to its physiological role in vital life functions. We also highlight the molecular and biochemical properties of insect trehalase that makes it amenable to competitive inhibition by most glycosidase inhibitors. Due to its crucial role in carbon metabolism in insects, application of inhibitors against trehalose can form a promising area towards formulating strategies for insect pest control.</p>10acarbohydrate metabolism10aglycosidase inhibitor10aglycoside hydrolase10atrehalase10atrehalose1 aShukla, Ekta1 aThorat, Leena, J.1 aNath, Bimalendu, B.1 aGaikwad, Sushama, M.  uhttps://library.ncl.res.in/content/insect-trehalase-physiological-significance-and-potential-applications-002644nas a2200277   4500008004100000022001400041245011100055210006900166260000800235300000800243490000600251520174300257653002102000653002302021653001102044653002402055653001402079100001702093700001802110700002202128700002002150700002102170700002402191700002502215856012602240       2018                        eng d  a2190-572X00aCloning and characterization of trehalase: a conserved glycosidase from oriental midge, Chironomus ramosus0 aCloning and characterization of trehalase a conserved glycosidas  cAUG  a3520 v83 a<p>Insect trehalase is a multiferous enzyme, crucial for normal physiological functions as well as under stress conditions. In this report, we present a fundamental study of the trehalase gene segment (1587 bp) from Chironomus ramosus (CrTre) encoding for 529 amino acids, using appropriate bioinformatics tools. C. ramosus, a tropical midge is an emerging animal model to investigate the consequences of environmental stresses. We observed that CrTre belongs to GH family 37 in the CAZy database and possess 57-92% identity to dipteran trehalases. In silico characterization provided information regarding the structural, functional and evolutionary aspects of midge trehalase. In the phylogenetic tree, CrTre clustered with the soluble dipteran trehalases. Moreover, domain functional characterization of the deduced protein sequence by InterProScan (IPR001661), ProSite (PS00927 and PS00928) and Pfam (PF01204) indicated presence of highly conserved signature motifs which are important for the identification of trehalase superfamily. Furthermore, the instability index of CrTre was predicted to be &lt; 40 suggesting its in vivo stability while, the high aliphatic index indicated towards its thermal stability (index value 71-81). The modelled 3D tertiary structure of CrTre depicts a (alpha/alpha)(6) barrel toroidal core. The catalytic domain of the enzyme comprised Glu424 and Asp226 as the putative active site residues. Interestingly, the conserved motifs were observed to be formed by the flexible loopy regions in the tertiary structure. This study revealed essential sequence features of the midge trehalase and offers better insights into the structural aspects of this enzyme which can be correlated with its function.</p>10aConserved motifs10aHomology modelling10aMidges10aSecondary structure10atrehalose1 aShukla, Ekta1 aThorat, Leena1 aBendre, Ameya, D.1 aJadhav, Santosh1 aPal, Jayanta, K.1 aNath, Bimalendu, B.1 aGaikwad, Sushama, M.  uhttps://library.ncl.res.in/content/cloning-and-characterization-trehalase-conserved-glycosidase-oriental-midge-chironomus