1WC2

Beta-1,4-D-endoglucanase Cel45A from blue mussel Mytilus edulis at 1.2A

1WC2 の概要

• エントリーDOI: 10.2210/pdb1wc2/pdb
• 分子名称: ENDOGLUCANASE, ACETATE ION, DI(HYDROXYETHYL)ETHER, ... (4 entities in total)
• 機能のキーワード: hydrolase, cellulase, cellulose, double-psi fold, glycoside hydrolase
• 由来する生物種: MYTILUS EDULIS (BLUE MUSSEL)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 20003.78

構造登録者

Jakobsson, E.,Mahdi, S.,Kleywegt, G.J.,Stahlberg, J. (登録日: 2004-11-08, 公開日: 2006-05-24, 最終更新日: 2024-10-23)

主引用文献

Okmane, L.,Nestor, G.,Jakobsson, E.,Xu, B.,Igarashi, K.,Sandgren, M.,Kleywegt, G.J.,Stahlberg, J.
Glucomannan and beta-glucan degradation by Mytilus edulis Cel45A: Crystal structure and activity comparison with GH45 subfamily A, B and C.
Carbohydr Polym, 277:118771-118771, 2022

PubMed Abstract: The enzymatic hydrolysis of barley beta-glucan, konjac glucomannan and carboxymethyl cellulose by a β-1,4-D-endoglucanase MeCel45A from blue mussel, Mytilus edulis, which belongs to subfamily B of glycoside hydrolase family 45 (GH45), was compared with GH45 members of subfamilies A (Humicola insolens HiCel45A), B (Trichoderma reesei TrCel45A) and C (Phanerochaete chrysosporium PcCel45A). Furthermore, the crystal structure of MeCel45A is reported. Initial rates and hydrolysis yields were determined by reducing sugar assays and product formation was characterized using NMR spectroscopy. The subfamily B and C enzymes exhibited mannanase activity, whereas the subfamily A member was uniquely able to produce monomeric glucose. All enzymes were confirmed to be inverting glycoside hydrolases. MeCel45A appears to be cold adapted by evolution, as it maintained 70% activity on cellohexaose at 4 °C relative to 30 °C, compared to 35% for TrCel45A. Both enzymes produced cellobiose and cellotetraose from cellohexaose, but TrCel45A additionally produced cellotriose.

PubMed: 34893216
DOI: 10.1016/j.carbpol.2021.118771

実験手法

X-RAY DIFFRACTION (1.2 Å)