Substitution of one calcium-binding amino acid strengthens substrate binding in a thermophilic alginate lyase
Wang, Bing1,2; Ji, Shi-Qi1; Ma, Xiao-Qing1; Lu, Ming1; Wang, Lu-Shan3; Li, Fu-Li1
刊名FEBS LETTERS
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
DOI10.1002/1873-3468.12965
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
出版者WILEY
WOS记录号WOS:000424875300008
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)
内容类型期刊论文
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.
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