Literature DB >> 25575592

Biochemical characterization and structural analysis of a bifunctional cellulase/xylanase from Clostridium thermocellum.

Shuo-Fu Yuan1, Tzu-Hui Wu2, Hsiao-Lin Lee3, Han-Yu Hsieh1, Wen-Ling Lin3, Barbara Yang1, Chih-Kang Chang3, Qian Li4, Jian Gao4, Chun-Hsiang Huang4, Meng-Chiao Ho5, Rey-Ting Guo6, Po-Huang Liang7.   

Abstract

We expressed an active form of CtCel5E (a bifunctional cellulase/xylanase from Clostridium thermocellum), performed biochemical characterization, and determined its apo- and ligand-bound crystal structures. From the structures, Asn-93, His-168, His-169, Asn-208, Trp-347, and Asn-349 were shown to provide hydrogen-bonding/hydrophobic interactions with both ligands. Compared with the structures of TmCel5A, a bifunctional cellulase/mannanase homolog from Thermotoga maritima, a flexible loop region in CtCel5E is the key for discriminating substrates. Moreover, site-directed mutagenesis data confirmed that His-168 is essential for xylanase activity, and His-169 is more important for xylanase activity, whereas Asn-93, Asn-208, Tyr-270, Trp-347, and Asn-349 are critical for both activities. In contrast, F267A improves enzyme activities.
© 2015 by The American Society for Biochemistry and Molecular Biology, Inc.

Entities:  

Keywords:  Biodegradation; Biofuel; Site-directed Mutagenesis; Substrate Specificity; X-ray Crystallography

Mesh：

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Year:  2015        PMID： 25575592      PMCID： PMC4342484          DOI： 10.1074/jbc.M114.604454

Source DB:  PubMed          Journal:  J Biol Chem        ISSN： 0021-9258            Impact factor:   5.157


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