6JXG

Crystasl Structure of Beta-glucosidase D2-BGL from Chaetomella Raphigera

6JXG の概要

• エントリーDOI: 10.2210/pdb6jxg/pdb
• 分子名称: Beta-glucosidase, 2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-mannopyranose, ... (4 entities in total)
• 機能のキーワード: glucosidase, glycoside hydrolase, hydrolase
• 由来する生物種: Chaetomella raphigera
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 76621.23

構造登録者

Wang, A.H.-J.,Lee, C.C.,Kao, M.R.,Ho, T.H.D. (登録日: 2019-04-23, 公開日: 2019-11-20, 最終更新日: 2023-11-22)

主引用文献

Kao, M.R.,Kuo, H.W.,Lee, C.C.,Huang, K.Y.,Huang, T.Y.,Li, C.W.,Chen, C.W.,Wang, A.H.J.,Yu, S.M.,Ho, T.H.D.
Chaetomella raphigerabeta-glucosidase D2-BGL has intriguing structural features and a high substrate affinity that renders it an efficient cellulase supplement for lignocellulosic biomass hydrolysis.
Biotechnol Biofuels, 12:258-258, 2019

PubMed Abstract: To produce second-generation biofuels, enzymatic catalysis is required to convert cellulose from lignocellulosic biomass into fermentable sugars. β-Glucosidases finalize the process by hydrolyzing cellobiose into glucose, so the efficiency of cellulose hydrolysis largely depends on the quantity and quality of these enzymes used during saccharification. Accordingly, to reduce biofuel production costs, new microbial strains are needed that can produce highly efficient enzymes on a large scale.

PubMed: 31700541
DOI: 10.1186/s13068-019-1599-0

実験手法

X-RAY DIFFRACTION (1.9 Å)