Loop 3 of Fungal Endoglucanases of Glycoside Hydrolase Family 12 Modulates Catalytic Efficiency

文献类型： 外文期刊

第一作者： Yang, Hong

作者： Yang, Hong;Shi, Pengjun;Liu, Yun;Xia, Wei;Wang, Xiaoyu;Cao, Huifang;Ma, Rui;Luo, Huiying;Bai, Yingguo;Yao, Bin;Liu, Yun;Wang, Xiaoyu

作者机构：

关键词： Neosartorya fischeri;GH12 beta-endoglucanase;loop;catalytic efficiency;hydrogen bond

期刊名称：APPLIED AND ENVIRONMENTAL MICROBIOLOGY （ 影响因子：4.792； 五年影响因子：5.26 ）

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收录情况： SCI

摘要： Glycoside hydrolase (GH) family 12 comprises enzymes with a wide range of activities critical for the degradation of lignocellulose. However, the important roles of the loop regions of GH12 enzymes in substrate specificity and catalytic efficiency remain poorly understood. This study examined how the loop 3 region affects the enzymatic properties of GH12 glucanases using NfEG12A from Neosartorya fischeri P1 and EG (PDB 1KS4) from Aspergillus niger. Acidophilic and thermophilic NfEG12A had the highest catalytic efficiency (k(cat)/K-m, 3,001 and 263 ml/mg/s toward lichenin and carboxymethyl cellulose sodium [CMC-Na], respectively) known so far. Based on the multiple-sequence alignment and homology modeling, two specific sequences (FN and STTQA) were identified in the loop 3 region of GH12 endoglucanases from fungi. To determine their functions, these sequences were introduced into NfEG12A, or the counterpart sequence STTQA was removed from EG. These modifications had no effects on the optimal pH and temperature or substrate specificity but changed the catalytic efficiency (k(cat)/K-m) of these enzymes (in descending order, NfEG12A [100%], NfEG12A-FN [140%], and NfEG12A-STTQA [190%]; EG [100%] and EG.STTQA [41%]). Molecular docking and dynamic simulation analyses revealed that the longer loop 3 in GH12 may strengthen the hydrogen-bond interactions between the substrate and protein, thereby increasing the turnover rate (k(cat)). This study provides a new insight to understand the vital roles of loop 3 for GH12 endoglucanases in catalysis.

分类号： Q939.9`X1

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