The novel amylase function of the carboxyl terminal domain of Amy63

doi:10.1016/j.bbrc.2023.05.071

CORC > 海洋研究所 > 中国科学院海洋研究所 > 实验海洋生物学重点实验室

	The novel amylase function of the carboxyl terminal domain of Amy63
	Sun, Yufan 1,2,3; Liu, Ge 6,7,8; Liu, Guangfeng 4; Tang, Haixu 5; Sun, Chaomin 6,7,8; Zhang, Wen 2,3; Chen, Li 1
刊名	BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
	2023-09-03
卷号	671 页码:10-17
关键词	Amy63 Amylase CTD The smallest amylase Oligomeric assembly Nanozyme X-ray crystallography
ISSN号	0006-291X
DOI	10.1016/j.bbrc.2023.05.071
通讯作者	Sun, Chaomin(sunchaomin2020@126.com) ; Zhang, Wen(wenz@fudan.edu.cn) ; Chen, Li(lichen_bk@fudan.edu.cn)
英文摘要	a-amylase plays a crucial role in regulating metabolism and health by hydrolyzing of starch and glycogen. Despite comprehensive studies of this classic enzyme spanning over a century, the function of its carboxyl terminal domain (CTD) with a conserved eight b-strands is still not fully understood. Amy63, identified from a marine bacterium, was reported as a novel multifunctional enzyme with amylase, agarase and carrageenase activities. In this study, the crystal structure of Amy63 was determined at 1.8 & ANGS; resolution, revealing high conservation with some other amylases. Interestingly, the independent amylase activity of the carboxyl terminal domain of Amy63 (Amy63_CTD) was newly discovered by the plate-based assay and mass spectrometry. To date, the Amy63_CTD alone could be regarded as the smallest amylase subunit. Moreover, the significant amylase activity of Amy63_CTD was measured over a wide range of temperature and pH, with optimal activity at 60 & DEG;C and pH 7.5. The Small-angle X-ray scattering (SAXS) data showed that the high-order oligomeric assembly gradually formed with increasing concentration of Amy63_CTD, implying the novel catalytic mechanism as revealed by the assembly structure. Therefore, the discovery of the novel independent amylase activity of Amy63_CTD suggests a possible missing step or a new perspective in the complex catalytic process of Amy63 and other related a-amylases. This work may shed light on the design of nanozymes to process marine polysaccharides efficiently.
资助项目	National Science and Technology Major Project[2014ZX09101046-004] ; National Natural Science Foundation of China[11179012] ; National Key Basic Research and Development Plan[2011CB710800] ; the Medical Research Data Center in Shanghai Medical College of Fudan University
WOS关键词	X-RAY-SCATTERING ; LICHENIFORMIS ALPHA-AMYLASE ; CRYSTAL-STRUCTURE ; DATA REDUCTION ; BINDING ; EVOLUTION
WOS研究方向	Biochemistry & Molecular Biology ; Biophysics
语种	英语
出版者	ACADEMIC PRESS INC ELSEVIER SCIENCE
WOS记录号	WOS:001018431500001
内容类型	期刊论文
源URL	[http://ir.qdio.ac.cn/handle/337002/182379]
专题	海洋研究所_实验海洋生物学重点实验室
通讯作者	Sun, Chaomin; Zhang, Wen; Chen, Li
作者单位	1.Fudan Univ, Sch Basic Med Sci, Dept Med Microbiol, Key Lab Med Mol Virol,Minist Educ & Hlth, Shanghai 200032, Peoples R China 2.Fudan Univ, Pudong Med Ctr, Inst Biomed Sci, Shanghai 200032, Peoples R China 3.Fudan Univ, Sch Basic Med Sci, Dept Syst Biol Med, Shanghai 200032, Peoples R China 4.Chinese Acad Sci, Shanghai Adv Res Inst, Natl Ctr Prot Sci Shanghai, Shanghai 201204, Peoples R China 5.Indiana Univ, Luddy Sch Informat Comp & Engn, Bloomington, IN 47408 USA 6.Chinese Acad Sci, Ctr Ocean Mega Sci, Qingdao 266071, Peoples R China 7.Qingdao Natl Lab Marine Sci & Technol, Lab Marine Biol & Biotechnol, Qingdao 266071, Peoples R China 8.Chinese Acad Sci, Inst Oceanol, CAS Key Lab Expt Marine Biol, Qingdao 266071, Peoples R China
推荐引用方式 GB/T 7714	Sun, Yufan,Liu, Ge,Liu, Guangfeng,et al. The novel amylase function of the carboxyl terminal domain of Amy63[J]. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS,2023,671:10-17.
APA	Sun, Yufan.,Liu, Ge.,Liu, Guangfeng.,Tang, Haixu.,Sun, Chaomin.,...&Chen, Li.(2023).The novel amylase function of the carboxyl terminal domain of Amy63.BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS,671,10-17.
MLA	Sun, Yufan,et al."The novel amylase function of the carboxyl terminal domain of Amy63".BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS 671(2023):10-17.