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Backbone and side-chain assignments for a novel CBM69 starch binding domain AmyP-SBD
Li, Xinxin1; Yu, Jigang1; Zhang, Jiahai2; Sun, Hongbin3; Zhang, Xuecheng1
2017-10-01
Source PublicationBIOMOLECULAR NMR ASSIGNMENTS
Volume11Issue:2Pages:235-237
AbstractStarch binding domains (SBDs) are important for the functions of glycoside hydrolysis enzymes such as alpha-amylases, they have great application potential in biotechnology and industries. AmyP is a newly identified alpha-amylase belonging to a new subfamily 37 of glycoside hydrolysis enzyme family 13. AmyP shows preferential degradation to soluble starch, in which its C-terminal starch binding domain, AmyP-SBD, plays an important role. AmyP-SBD shares very low sequence similarity with other biochemically characterized SBDs and was assigned to a new carbohydrate binding module family CBM69. Intriguingly, AmyP-SBD is unfolded in free form, and substrate analogue beta-cyclodextrin may induce it to fold into a relatively rigid state. Structure determination for AmyP-SBD will be helpful for understanding its unique properties. Here, we report the backbone and side-chain H-1, C-13 and N-15 resonance assignments of folded AmyP-SBD, as a basis for structure determination and further studies.
SubtypeArticle
KeywordStarch Binding Domain Cbm69 Amyp Nmr
WOS HeadingsScience & Technology ; Life Sciences & Biomedicine ; Technology
Funding OrganizationNational Natural Science Foundation of China(31470775) ; National Natural Science Foundation of China(31470775) ; International Science and Technology Cooperation Plan of Anhui Province(1503062010) ; International Science and Technology Cooperation Plan of Anhui Province(1503062010) ; National Natural Science Foundation of China(31470775) ; National Natural Science Foundation of China(31470775) ; International Science and Technology Cooperation Plan of Anhui Province(1503062010) ; International Science and Technology Cooperation Plan of Anhui Province(1503062010)
DOI10.1007/s12104-017-9755-6
WOS KeywordALPHA-AMYLASE ENZYMES ; ASPERGILLUS-NIGER ; GLUCOAMYLASE ; FAMILY
Indexed BySCI
Language英语
Funding OrganizationNational Natural Science Foundation of China(31470775) ; National Natural Science Foundation of China(31470775) ; International Science and Technology Cooperation Plan of Anhui Province(1503062010) ; International Science and Technology Cooperation Plan of Anhui Province(1503062010) ; National Natural Science Foundation of China(31470775) ; National Natural Science Foundation of China(31470775) ; International Science and Technology Cooperation Plan of Anhui Province(1503062010) ; International Science and Technology Cooperation Plan of Anhui Province(1503062010)
WOS Research AreaBiophysics ; Spectroscopy
WOS SubjectBiophysics ; Spectroscopy
WOS IDWOS:000410473300023
Citation statistics
Document Type期刊论文
Identifierhttp://ir.hfcas.ac.cn:8080/handle/334002/33669
Collection中科院强磁场科学中心
Affiliation1.Anhui Univ, Sch Life Sci, Anhui Prov Engn Technol Res Ctr Microorganisms &, 111 Jiulong Rd, Hefei 230601, Anhui, Peoples R China
2.Univ Sci & Technol China, Sch Life Sci, Hefei Natl Lab Phys Sci Microscale, Hefei 230026, Anhui, Peoples R China
3.Chinese Acad Sci, Hefei Inst Phys Sci, High Magnet Field Lab, Hefei 230031, Anhui, Peoples R China
Recommended Citation
GB/T 7714
Li, Xinxin,Yu, Jigang,Zhang, Jiahai,et al. Backbone and side-chain assignments for a novel CBM69 starch binding domain AmyP-SBD[J]. BIOMOLECULAR NMR ASSIGNMENTS,2017,11(2):235-237.
APA Li, Xinxin,Yu, Jigang,Zhang, Jiahai,Sun, Hongbin,&Zhang, Xuecheng.(2017).Backbone and side-chain assignments for a novel CBM69 starch binding domain AmyP-SBD.BIOMOLECULAR NMR ASSIGNMENTS,11(2),235-237.
MLA Li, Xinxin,et al."Backbone and side-chain assignments for a novel CBM69 starch binding domain AmyP-SBD".BIOMOLECULAR NMR ASSIGNMENTS 11.2(2017):235-237.
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