Substitution of one calcium-binding amino acid strengthens substrate binding in a thermophilic alginate lyase
文献类型：期刊论文
| 作者 | Wang, Bing1,2; Ji, Shi-Qi1; Ma, Xiao-Qing1 ; Lu, Ming1; Wang, Lu-Shan3; Li, Fu-Li1
|
| 刊名 | FEBS LETTERS
 |
| 出版日期 | 2018-02-01 |
| 卷号 | 592期号:3页码:369-379 |
| 关键词 | Alginate Calcium-binding Sites Defluviitalea Phaphyphila Polysaccharide Lyase Thermophile |
| ISSN号 | 1873-3468 |
| DOI | 10.1002/1873-3468.12965 |
| 文献子类 | Article |
| 英文摘要 | Ligand binding is sensitive to temperatures since noncovalent bonds between the binding site and ligand could be broken by heat. How metal ion-binding amino acids in alginate lyase evolve to achieve tight substrate binding in a hostile environment remains unknown. An endolytic alginate lyase AlgAT0 specifically cleaved the M-G glycosidic bond and released disaccharides as the main end product. Four conserved calcium-binding sites were predicted and the supplement of Ca2+ led to enhanced substrate binding and protein stability. Among the four conserved calcium-binding sites, one substitution of aspartate for glutamate in AlgAT0 was proved to stimulate Ca2+ affinity. This study suggested that substrate affinity of polysaccharide lyases could be improved by tight binding to Ca(2+)via one amino acid substitution. |
| WOS关键词 | OLIGOSACCHARIDES ; RESIDUES ; ADAPTATION ; MECHANISM ; PROTEINS ; SEQUENCE ; ENZYMES ; ROLES |
| WOS研究方向 | Biochemistry & Molecular Biology ; Biophysics ; Cell Biology |
| 语种 | 英语 |
| WOS记录号 | WOS:000424875300008 |
| 出版者 | WILEY |
| 资助机构 | National Natural Science Funds of China(41506155 ; Shandong Province Natural Science Funds for Distinguished Young Scholars(JQ201507) ; Basic Research Program of Qingdao(15-9-1-104-jch) ; 31700112) |
| 源URL | [http://ir.qibebt.ac.cn/handle/337004/10635]  |
| 专题 | 青岛生物能源与过程研究所_微生物资源团队 |
| 通讯作者 | Ma, Xiao-Qing; Li, Fu-Li |
| 作者单位 | 1.Chinese Acad Sci, Shandong Prov Key Lab Synthet Biol, Key Lab Biofuels, Qingdao Inst Bioenergy & Bioproc Technol, Qingdao 266101, Peoples R China 2.Univ Chinese Acad Sci, Beijing, Peoples R China 3.Shandong Univ, State Key Lab Microbial Technol, Jinan, Shandong, Peoples R China |
| 推荐引用方式 GB/T 7714 | Wang, Bing,Ji, Shi-Qi,Ma, Xiao-Qing,et al. Substitution of one calcium-binding amino acid strengthens substrate binding in a thermophilic alginate lyase[J]. FEBS LETTERS,2018,592(3):369-379. |
| APA | Wang, Bing,Ji, Shi-Qi,Ma, Xiao-Qing,Lu, Ming,Wang, Lu-Shan,&Li, Fu-Li.(2018).Substitution of one calcium-binding amino acid strengthens substrate binding in a thermophilic alginate lyase.FEBS LETTERS,592(3),369-379. |
| MLA | Wang, Bing,et al."Substitution of one calcium-binding amino acid strengthens substrate binding in a thermophilic alginate lyase".FEBS LETTERS 592.3(2018):369-379. |
入库方式： OAI收割
来源：青岛生物能源与过程研究所
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