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Catalytic site flexibility facilitates the substrate and catalytic promiscuity of Vibrio dual lipase/transferase

文献类型：期刊论文

作者Wang, Chongyang2,3,4,5; Liu, Changshui3,4,5; Zhu, Xiaochuan4,5; Peng, Quancai1; Ma, Qingjun1,2,3,4,5
刊名NATURE COMMUNICATIONS
出版日期2023-08-09
卷号14期号:1页码:11
DOI10.1038/s41467-023-40455-y
通讯作者Ma, Qingjun(qma@qdio.ac.cn)
英文摘要Vibrio dual lipases/transferases are virulence-related enzymes, with both substrate and catalytic promiscuity. Wang et al reveal their prominent structural flexibility, proposing a catalytic site tuning mechanism underlying enzyme promiscuity. Although enzyme catalysis is typified by high specificity, enzymes can catalyze various substrates (substrate promiscuity) and/or different reaction types (catalytic promiscuity) using a single active site. This interesting phenomenon is widely distributed in enzyme catalysis, with both fundamental and applied importance. To date, the mechanistic understanding of enzyme promiscuity is very limited. Herein, we report the structural mechanism underlying the substrate and catalytic promiscuity of Vibrio dual lipase/transferase (VDLT). Crystal structures of the VDLT from Vibrio alginolyticus (ValDLT) and its fatty acid complexes were solved, revealing prominent structural flexibility. In particular, the "Ser-His-Asp" catalytic triad machinery of ValDLT contains an intrinsically flexible oxyanion hole. Analysis of ligand-bound structures and mutagenesis showed that the flexible oxyanion hole and other binding residues can undergo distinct conformational changes to facilitate substrate and catalytic promiscuity. Our study reveals a previously unknown flexible form of the famous catalytic triad machinery and proposes a "catalytic site tuning" mechanism to expand the mechanistic paradigm of enzyme promiscuity.
WOS关键词ENZYME PROMISCUITY ; STRUCTURAL BASIS ; PHOSPHOLIPASE ; PURIFICATION ; HEMOLYSIN ; PARAHAEMOLYTICUS ; IDENTIFICATION ; PATHOGENICITY ; ACTIVATION ; MECHANISM
资助项目Qingdao Innovation Leadership Program[2015ASTP] ; Pilot National Laboratory for Marine Science and Technology[18-1-2-12-zhc]
WOS研究方向Science & Technology - Other Topics
语种英语
出版者NATURE PORTFOLIO
WOS记录号WOS:001045317100017
源URL[http://ir.qdio.ac.cn/handle/337002/182774]  
专题海洋研究所_实验海洋生物学重点实验室
通讯作者Ma, Qingjun
作者单位1.Chinese Acad Sci, Inst Oceanol, Ctr Ocean Mega Sci, Qingdao, Peoples R China
2.Univ Chinese Acad Sci, Beijing, Peoples R China
3.Qingdao Natl Lab Marine Sci & Technol, Lab Marine Biol & Biotechnol, Qingdao, Peoples R China
4.Chinese Acad Sci, Inst Oceanol, Shandong Prov Key Lab Expt Marine Biol, Qingdao, Peoples R China
5.Chinese Acad Sci, Qingdao, Peoples R China
推荐引用方式
GB/T 7714		 Wang, Chongyang,Liu, Changshui,Zhu, Xiaochuan,et al. Catalytic site flexibility facilitates the substrate and catalytic promiscuity of Vibrio dual lipase/transferase[J]. NATURE COMMUNICATIONS,2023,14(1):11.
APA Wang, Chongyang,Liu, Changshui,Zhu, Xiaochuan,Peng, Quancai,&Ma, Qingjun.(2023).Catalytic site flexibility facilitates the substrate and catalytic promiscuity of Vibrio dual lipase/transferase.NATURE COMMUNICATIONS,14(1),11.
MLA Wang, Chongyang,et al."Catalytic site flexibility facilitates the substrate and catalytic promiscuity of Vibrio dual lipase/transferase".NATURE COMMUNICATIONS 14.1(2023):11.

入库方式： OAI收割

来源：海洋研究所

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