Structure of the Catalytic Domain of α-l-Arabinofuranosidase from Coprinopsis cinerea, CcAbf62A, Provides Insights into Structure–Function Relationships in Glycoside Hydrolase Family 62

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• 作者：Takashi Tonozuka ; Yutaro Tanaka ; Shunsaku Okuyama…
• 关键词：Coprinopsis cinerea ; α ; l ; arabinofuranosidase ; Arabinoxylan ; GH62 ; Hemicellulose
• 刊名：Applied Biochemistry and Biotechnology
• 出版年：2017
• 出版时间：February 2017
• 年：2017
• 卷：181
• 期：2
• 页码：511-525
• 全文大小：
• 刊物类别：Chemistry and Materials Science
• 刊物主题：Biotechnology; Biochemistry, general;
• 出版者：Springer US
• ISSN：1559-0291
• 卷排序：181

文摘

α-l-Arabinofuranosidases, belonging to the glycoside hydrolase family (GH) 62, hydrolyze the α-1,2- or α-1,3-bond to liberate l-arabinofuranose from the xylan backbone. Here, we determined the structure of the C-terminal catalytic domain of CcAbf62A, a GH62 α-l-arabinofuranosidase from Coprinopsis cinerea. CcAbf62A is composed of a five-bladed β-propeller, as observed in other GH62 enzymes. The structure near the active site of CcAbf62A is also highly homologous to those of other GH62 enzymes. However, a calcium atom in the catalytic center interacts with an asparagine residue, Asn279, which is not found in other GH62 enzymes. In addition, some residues in subsites +3R, +2NR, +3NR, and +4NR of CcAbf62A are not conserved in other GH62 enzymes. In particular, a histidine residue, His221, is uniquely observed in subsite +2NR of CcAbf62A, which is likely to influence the substrate specificity. The results obtained here suggest that the amino acid residues that interact with the xylan backbone vary among the GH62 enzymes, despite the high similarity of their overall structures.