02107nas a2200241   4500008004100000022001400041245007600055210006900131260008100200300001200281490000700293520126000300653002801560653002601588653002401614653001401638653001401652100001701666700002201683700002401705700002501729856011101754       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.  uhttp://library.ncl.res.in/content/insect-trehalase-physiological-significance-and-potential-applications-002369nas a2200265   4500008004100000022001400041245011700055210006900172260000800241300001400249490000800263520148700271653002501758653002401783653002401807653001401831653002101845100001701866700002001883700001601903700001601919700002401935700001801959856012601977       2019                        eng d  a1742-464X00aMechanistic insights into enzymatic catalysis by trehalase from the insect gut endosymbiont Enterobacter cloacae0 aMechanistic insights into enzymatic catalysis by trehalase from   cMAY  a1700-17160 v2863 a<p>Energy metabolism in the diamondback moth Plutella xylostella is facilitated by trehalase, an enzyme which assists in trehalose hydrolysis, from the predominant gut bacterium Enterobacter cloacae. We report the biochemical and structural characterization of recombinant trehalase from E. cloacae (Px_EclTre). Px_EclTre showed K-M of 1.47 (+/- 0.05) mm, k(cat) of 6254.72 min(-1) and V-max 0.2 (+/- 0.002) mm center dot min(-1) at 55 degrees C and acidic pH. Crystal structures of Px_EclTre were determined in the ligand-free form and bound to the inhibitor Validoxylamine A. The crystal structure of the ligand-free form, unavailable until now for any other bacterial trehalases, enabled us to delineate the conformational changes accompanying ligand binding in trehalases. Multiple salt bridges were identified that potentially facilitated closure of a hood over the substrate-binding site. A cluster of five tryptophans lined the -1 substrate-binding subsite, interacted with crucial active site residues and contributed to both trehalase activity and stability. The importance of these residues in enzyme activity was further validated by mutagenesis studies. Many of these identified residues form part of signature motifs and other conserved sequences in trehalases. The structure analysis thus led to the assignment of the functional role to these conserved residues. This information can be further explored for the design of effective inhibitors against trehalases.</p>
10aEnterobacter cloacae10aPlutella xylostella10astructural analysis10atrehalase10avalidoxylamine A1 aAdhav, Anmol1 aHarne, Shrikant1 aBhide, Amey1 aGiri, Ashok1 aGayathri, Pananghat1 aJoshi, Rakesh  uhttp://library.ncl.res.in/content/mechanistic-insights-enzymatic-catalysis-trehalase-insect-gut-endosymbiont-enterobacter