Nanjing Institute of Soils

Nanjing, China

Nanjing Institute of Soils

Nanjing, China
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Wu W.-M.,China Pharmaceutical University | Lao X.-Z.,China Pharmaceutical University | Zheng H.,China Pharmaceutical University | Zheng H.,Nanjing Institute of Soils
Chinese Journal of Pharmaceutical Biotechnology | Year: 2013

Arabinosidase can catalyze the hydrolysis of the glycoside bond between L-Arabinose and xylose, and release arabinose from hemicellulose, therefore it plays important role in the degradation of hemicellulose and the preparation of arabinose. The arabinosidase from the anaerobic thermophile Thermoanaerobacter ethanolicus poses the double functional activity of xylosidase and arabinosidase, and is a thermostable enzyme. In order to further study the catalytic mechanism, the 3D structure of the arabinosidase was predicted. It also figured out the important residues in the predicted structure. The homology modeling method was used to predict its structure, using the structure of the β-glucosidase from Thermotoga neapolitana as template. The substrate of p-nitrophenyl α-L-arabi-nopyranoside (pNPAP) and p-nitrophenyl β-D-xylopyranoside (pNPX) were docked into the active site of the predicted structure of the arabinosidase, respectively. The results showed that the residue of Asn90, Argl64, Lys201 and Asp281 on the active site may play important role in substrate binding and hydrolyzing process.

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