@article { ISI:000353901700002,
	title = {Insect trehalase: physiological significance and potential applications},
	journal = {Glycobiology},
	volume = {25},
	number = {4},
	year = {2015},
	month = {APR},
	pages = {357-367},
	publisher = {OXFORD UNIV PRESS INC},
	address = {JOURNALS DEPT, 2001 EVANS RD, CARY, NC 27513 USA},
	abstract = {<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>},
	keywords = {carbohydrate metabolism, glycosidase inhibitor, glycoside hydrolase, trehalase, trehalose},
	issn = {0959-6658},
	doi = {10.1093/glycob/cwu125},
	author = {Shukla, Ekta and Thorat, Leena J. and Nath, Bimalendu B. and Gaikwad, Sushama M.}
}
@article {46119,
	title = {Mechanistic insights into enzymatic catalysis by trehalase from the insect gut endosymbiont Enterobacter cloacae},
	journal = {FEBS Journal},
	volume = {286},
	year = {2019},
	month = {MAY},
	pages = {1700-1716},
	type = {Article},
	abstract = {<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>
},
	keywords = {Enterobacter cloacae, Plutella xylostella, structural analysis, trehalase, validoxylamine A},
	issn = {1742-464X},
	doi = {10.1111/febs.14760},
	author = {Adhav, Anmol and Harne, Shrikant and Bhide, Amey and Giri, Ashok and Gayathri, Pananghat and Joshi, Rakesh}
}
@article {49242,
	title = {Trehalase inhibition in Helicoverpa armigera activates machinery for alternate energy acquisition},
	journal = {JOURNAL OF BIOSCIENCES},
	volume = {49},
	year = {2024},
	month = {JUL },
	pages = {74},
	type = {Journal Article},
	keywords = {Energy metabolism, glucose, Metabolomics, Transcriptomics, trehalase, validamycin A},
	issn = {0250-5991},
	doi = {10.1007/s12038-024-00453-8},
	author = {Tellis, Meenakshi and Mohite, Sharada and Joshi, Rakesh}
}
