Structural and functional analysis of the Eukaryotic Orpinomyces sp. glucanase Cel6

• Main Authors: Chih-Hung Huang, 黃致鈜
• Other Authors: 蔡麗珠
• Format: Others
• Language: zh-TW
• Published: 2013
• Online Access: http://ndltd.ncl.edu.tw/handle/52ez6a

碩士 === 國立臺北科技大學 === 有機高分子研究所 === 101 === Endoglucanases (EC 3.2.1.91) that belong to GH 6 glycosyl hydrolase, cleave the ?β-1,4-glucosidic linkage of cellulose and release cellooliogsaccharides as the major product. Endoglucanase from Orpinomyces sp. PC-2 contains two subunits of dockerin domain (residues 1-100) and catalytic domain (OsCel6, residues 105-449). The crystal structure of OsCel6 at a resolution of 1.8 A, reveals this enzyme contains an open cleft active site. The topology of OsCel6 open cleft active site is similar to those of Thermobifida fusca Cel6A and Humicola insolens Cel6B endoglucanase. The structural study suggests that two loops (loop1; residues 201-218, and loop2; residues 410-425) located around the active site is likely to move to form a tunnel active site for exo-activity. Enzymatic function data reveal that OsCel6 functions as a major endoglucanase activity.