| 论文题目: | Crystal structure and substrate-binding mode of a novel pectate lyase from alkaliphilic Bacillus sp N16-5 |
|---|---|
| 作者: | Zheng, YY; Huang, CH; Liu, WT; Ko, TP; Xue, YF; Zhou, C; Guo, RT; Ma, YH |
| 联系作者: | Ma, YH |
| 刊物名称: | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS |
| 期: | 2 |
| 卷: | 420 |
| 页: | 269-274 |
| 年份: | 2012 |
| 影响因子: | 2.484 |
| 论文下载: | 下载地址 |
| 摘要: | The pectate lyase (Bsp165PelA) from Bacillus sp. N16-5 has great potential in industrial applications because it shows high specific activity under extremely alkaline conditions. Besides, activity measurement of Bsp165PelA does not require addition of calcium, in a way different from the other pectate lyases. Here we report crystal structures of Bsp165PelA in apo-form and in complex with trigalacturonate. The parallel beta-helix, active site residues and substrate binding cleft are similar to those in the other pectate lyases from Polysaccharide Lyase family 1. However, some of the highly conserved Ca2+ binding residues and secondary structures are altered in Bsp165PelA, making it difficult to coordinate with Ca2+ as in the other pectate lyases. We found Bsp165PelA forms some direct enzyme-substrate interactions instead of using Ca2+ ions bridging in the extremely alkaline environment. (C) 2012 Elsevier Inc. All rights reserved. |
京公网安备 11010502044263号