Structural and functional analysis of the truncated Fibrobacter succinogenes 1,3-1,4-β-D-glucanase mutant Y42L and inhibitor complex
Autor: | Wen-Chin Chang, 張文進 |
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Rok vydání: | 2012 |
Druh dokumentu: | 學位論文 ; thesis |
Popis: | 100 Fibrobacter succinogenes 1,3-1,4-β-D-glucanase (Fsβ-glucanase, E.C.3.2.1.73) specifically hydrolyze the β-1,4 bonds when β-1,3 linkages are located prior to the β-1,4 bonds in β-D-glucan or lichenan. The final hydrolyzed products are tri- and penta- saccharides. Three calcium ions and two tris molecules are found in the truncated Fsβ-glucanase mutant Y42L structure. The first calcium ion is located at the same position as that of wild type. The second Ca2+ ion was found near the residues Phe152 and Glu154 on the protein’s surface, and the third one near the active site residue Asp202. Moreover, a tris molecule interacts with the catalytic residues Glu56 and Glu60 at subunit -1 of substrate. Based on the kinetic data, it is shown that the third Ca2+ ion and tris molecule are non-competitive and competitive inhibitors for the enzyme, respectively. |
Databáze: | Networked Digital Library of Theses & Dissertations |
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