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KMID : 0545120150250010044
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Journal of Microbiology and Biotechnology
2015 Volume.25 No. 1 p.44 ~ p.49
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Determination of Substrate Specificities Against β-Glucosidase A (BglA) from Thermotoga maritime: A Molecular Docking Approach
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Muhammad Ibrahim Rajoka
Sobia Idrees
Usman Ali Ashfaq
Beenish Ehsan
Asma Haq
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Abstract
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Thermostable enzymes derived from Thermotoga maritima have attracted worldwide interest for their potential industrial applications. Structural analysis and docking studies were preformed on T. maritima β-glucosidase enzyme with cellobiose and pNP-linked substrates. The 3D structure of the thermostable β-glucosidase was downloaded from the Protein Data Bank database. Substrates were downloaded from the PubCehm database and were minimized using MOE software. Docking of BglA and substrates was carried out using MOE software. After analyzing docked enzyme/substrate complexes, it was found that Glu residues were mainly involved in the reaction, and other important residues such as Asn, Ser, Tyr, Trp, and His were involved in hydrogen bonding with pNP-linked substrates. By determining the substrate recognition pattern, a more suitable β-glucosidase enzyme could be developed, enhancing its industrial potential.
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KEYWORD
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Active site residues, β-glucosidase, Thermotoga maritima, interactions, molecular docking
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