Substitution of one calcium-binding amino acid strengthens substrate binding in a thermophilic alginate lyase

doi:10.1002/1873-3468.12965

QIBEBT-IR > 分子微生物工程研究组

	Substitution of one calcium-binding amino acid strengthens substrate binding in a thermophilic alginate lyase
	Wang, Bing 1,2; Ji, Shi-Qi 1; Ma, Xiao-Qing1 ; Lu, Ming 1; Wang, Lu-Shan 3; Li, Fu-Li 1
	2018-02-01
发表期刊	FEBS LETTERS
ISSN	1873-3468
卷号	592 期号:3 页码:369-379
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.
文章类型	Article
关键词	Alginate Calcium-binding Sites Defluviitalea Phaphyphila Polysaccharide Lyase Thermophile
WOS标题词	Science & Technology ; Life Sciences & Biomedicine
DOI	10.1002/1873-3468.12965
关键词[WOS]	OLIGOSACCHARIDES ; RESIDUES ; ADAPTATION ; MECHANISM ; PROTEINS ; SEQUENCE ; ENZYMES ; ROLES
收录类别	SCI
语种	英语
WOS研究方向	Biochemistry & Molecular Biology ; Biophysics ; Cell Biology
项目资助者	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)
WOS类目	Biochemistry & Molecular Biology ; Biophysics ; Cell Biology
WOS记录号	WOS:000424875300008
出版者	WILEY
引用统计	被引频次：12[WOS] [WOS记录] [WOS相关记录]
文献类型	期刊论文
条目标识符	http://ir.qibebt.ac.cn/handle/337004/10636
专题	分子微生物工程研究组
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.