Authors Affiliation(s)
- 1Department of Chemistry, CV Raman College of Engineering, Bidyanagra Mahura, Janla, Bhubaneswar, Odisha 752054, INDIA
- 2Department of Chemistry, Gangadhar Meher University, Sambalpur, Odisha, INDIA
- 3School of Life Sciencese, Sambalpur University, Jyoti Vihar, Burla, Sambalpur, Odisha, INDIA
Can J Biotech, Volume 1, Special Issue-Supplement, Page 217, DOI: https://doi.org/10.24870/cjb.2017-a202
Presenting author: pranab.mohapatra@cvrgi.edu.in
Abstract
β-Glucosidase, a family 1 glycosyl hydrolase (GH1), encoded by din2 in Arabidopsis is reported to be expressed during late phase of senescence [1, 2]. In absence of 3D structure of Din2 (BGLU30), an attempt has been made to build 3D structure of the enzyme by homology modeling and to analyze the active site based upon the template structure from other β -glucosidases to decipher the function of the enzyme. The structural insight, energetics and docking of ligands reveal that Arg380 residue may play a role in the catalysis. The residue is conserved in Arabidopsis BGLU28 and BGLU29 β -glucosidases of GH1 also. Participation of Arg380 in the hydrolysis of β -glucoside is discussed.
References
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- Patro, L., Mohapatra, P.K., Biswal, U.C. and Biswal, B. (2014) Dehydration induced loss of photosynthesis in Arabidopsis leaves during senescence is accompanied by the reversible enhancement in the activity of cell wall β-glucosidase. J Photochem Photobiol B 137: 49-54. Crossref