Substrate-Binding Site of Family 11 Xylanase from Bacillus firmus K-1 by Molecular Docking

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概要

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• The three-dimensional structure (3D structure) of Xyn11A, a family 11 xylanase from Bacillus firmus K-1, was obtained through homology modeling. To study the substrate-binding site of Xyn11A, six xylooligosaccharides, xylobiose to xyloheptaose (X2–X7), were docked into the active site of Xyn11A by molecular docking. Based on the docked energy and estimated free energy of binding combined with modeled enzyme-substrate complexes, the substrate-binding site of Xyn11A probably contained six subsites, defined as −3, −2, −1, +1, +2, and +3. Focus on possible stacking interaction presented seven aromatic residues, that played an important role in six subsites of Xyn11A such as Tyr165 (−3), Trp9 and Tyr69 (−2), Tyr80 (−1), Tyr65 (+1), Tyr88 (+2) and Tyr173 (+3). The bond-cleavage positions showed that X2 and X3 did not bind at the cleft (subsites −1 and +1) of Xyn11A. Related to the experiment, the end products of larchwood xylan hydrolysis by purified Xyn11A were X2 and X3. X2 and X3 acted as the end product inhibitors of Xyn11A.

• 社団法人 日本農芸化学会の論文
• 2009-04-23

著者

• Ratanakhanokchai Khanok

  School Of Bioresources And Technology King Mongkut's University Of Technology Thonburi

• Kyu Khin

  School Of Bioresources And Technology King Mongkut's University Of Technology Thonburi

• JOMMUENGBOUT Pattraporn

  School of Bioresources and Technology, King Mongkut's University of Technology Thonburi

• PINITGLANG Surapong

  Faculty of Science, University of the Thai Chamber of Commerce

• Pinitglang Surapong

  Faculty Of Science University Of The Thai Chamber Of Commerce

• Jommuengbout Pattraporn

  School Of Bioresources And Technology King Mongkut's University Of Technology Thonburi

関連論文

• Characterization of Paenibacillus curdlanolyticus Intracellular Xylanase Xyn10B Encoded by the xyn10B Gene
• Substrate-Binding Site of Family 11 Xylanase from Bacillus firmus K-1 by Molecular Docking
• Isolation and characterization of a multienzyme complex (cellulosome) of the Paenibacillus curdlanolyticus B-6 grown on Avicel under aerobic conditions(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)
• Effect of Carbon Sources on the Induction of Xylanolytic-Cellulolytic Multienzyme Complexes in Paenibacillus curdlanolyticus Strain B-6
• Purification and Partial Characterization of an Acidic α-Glucan-Protein Complex from the Fruiting Body of Pleurotus sajor-caju and Its Effect on Macrophage Activation

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