Structural insights into a novel Ca2+-independent PL-6 alginate lyase from Vibrio OU02 identify the possible subsites responsible for product distribution
文献类型：期刊论文
| 作者 | Lyu, Qianqian1,2; Zhang, Keke1; Shi, Yanhong3 ; Li, Weihua4; Diao, Xiaotong5; Liu, Weizhi1,2
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| 刊名 | BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS
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| 出版日期 | 2019-07-01 |
| 卷号 | 1863期号:7页码:1167-1176 |
| 关键词 | Alginate lyase PL-6 Catalytic mechanism X-ray crystallography Product distribution |
| ISSN号 | 0304-4165 |
| DOI | 10.1016/j.bbagen.2019.04.013 |
| 通讯作者 | Liu, Weizhi(liuweizhi@ouc.edu.cn) |
| 英文摘要 | Alginate lyases have a wide range of industrial applications, such as oligosaccharide preparation, medical treatment, and bioconversion. Therefore, the discovery and characterization of novel alginate lyases are extremely important. PL-6 alginate lyases are classified into two groups: those with a single domain or two domains. However, only one structure of a two-domain alginate lyase has been determined to date. In this study, we characterized a novel single-domain PL-6 alginate lyase (named AlyF). According to the biochemical analysis, AlyF possesses unique features compared with other PL-6 enzymes, including (1) a Ca2+-independent catalytic mechanism and (2) a PolyG-specific cleavage specificity that predominantly produces trisaccharides. The structures of AlyF and its complexes described here reveal the structural basis for these unique features and substrate binding mechanisms, which were further confirmed using mutagenesis. More importantly, we determined the possible subsites specifying the predominantly trisaccharide products of AlyF, which may facilitate the rational design of AlyF for potential applications in preparing a single alginate oligomer. |
| WOS关键词 | MECHANISM |
| 资助项目 | National Natural Science Foundation of China[41706151] ; National Key R&D Program of China[2018YFC0311105] |
| WOS研究方向 | Biochemistry & Molecular Biology ; Biophysics |
| 语种 | 英语 |
| WOS记录号 | WOS:000470339000001 |
| 出版者 | ELSEVIER SCIENCE BV |
| 源URL | [http://119.78.100.183/handle/2S10ELR8/289635]  |
| 专题 | 中国科学院上海药物研究所 |
| 通讯作者 | Liu, Weizhi |
| 作者单位 | 1.Ocean Univ China, Coll Marine Life Sci, MOE Key Lab Marine Genet & Breeding, Qingdao 266003, Shandong, Peoples R China 2.Qingdao Natl Lab Marine Sci & Technol, Lab Marine Biol & Biotechnol, Qingdao 266235, Shandong, Peoples R China 3.Chinese Acad Sci, Shanghai Inst Mat Med, Shanghai 201203, Peoples R China 4.East China Univ Sci & Technol, Sch Pharm, Shanghai Key Lab New Drug Design, Shanghai 200237, Peoples R China 5.Shandong Univ, State Key Lab Microbial Technol, Qingdao 266237, Shandong, Peoples R China |
| 推荐引用方式 GB/T 7714 | Lyu, Qianqian,Zhang, Keke,Shi, Yanhong,et al. Structural insights into a novel Ca2+-independent PL-6 alginate lyase from Vibrio OU02 identify the possible subsites responsible for product distribution[J]. BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS,2019,1863(7):1167-1176. |
| APA | Lyu, Qianqian,Zhang, Keke,Shi, Yanhong,Li, Weihua,Diao, Xiaotong,&Liu, Weizhi.(2019).Structural insights into a novel Ca2+-independent PL-6 alginate lyase from Vibrio OU02 identify the possible subsites responsible for product distribution.BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS,1863(7),1167-1176. |
| MLA | Lyu, Qianqian,et al."Structural insights into a novel Ca2+-independent PL-6 alginate lyase from Vibrio OU02 identify the possible subsites responsible for product distribution".BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS 1863.7(2019):1167-1176. |
入库方式： OAI收割
来源：上海药物研究所
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