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A new dimethylsulfoniopropionate lyase of the cupin superfamily in marine bacteria |
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| Authors: | Shu-Yan Wang Nan Zhang Zhao-Jie Teng Xiao-Di Wang Jonathan D. Todd Yu-Zhong Zhang Hai-Yan Cao Chun-Yang Li |
| Affiliation: | 1. Frontiers Science Center for Deep Ocean Multispheres and Earth System & College of Marine Life Sciences, Ocean University of China, Qingdao, China State Key Laboratory of Microbial Technology, Marine Biotechnology Research Center, Shandong University, Qingdao, China Laboratory for Marine Biology and Biotechnology, Pilot National Laboratory for Marine Science and Technology, Qingdao, China Contribution: Formal analysis (lead), Investigation (lead), Writing - original draft (lead);2. School of Bioengineering, Qilu University of Technology (Shandong Academy of Sciences), Jinan, China Contribution: Formal analysis (equal), Investigation (equal);3. State Key Laboratory of Microbial Technology, Marine Biotechnology Research Center, Shandong University, Qingdao, China Contribution: Data curation (lead), Formal analysis (equal);4. Frontiers Science Center for Deep Ocean Multispheres and Earth System & College of Marine Life Sciences, Ocean University of China, Qingdao, China Contribution: Data curation (equal), Formal analysis (equal);5. School of Biological Sciences, University of East Anglia, Norwich, UK Contribution: Writing - review & editing (equal);6. Frontiers Science Center for Deep Ocean Multispheres and Earth System & College of Marine Life Sciences, Ocean University of China, Qingdao, China;7. Frontiers Science Center for Deep Ocean Multispheres and Earth System & College of Marine Life Sciences, Ocean University of China, Qingdao, China State Key Laboratory of Microbial Technology, Marine Biotechnology Research Center, Shandong University, Qingdao, China Contribution: Formal analysis (equal), Writing - original draft (supporting), Writing - review & editing (supporting) |
| Abstract: | Dimethylsulfoniopropionate (DMSP) is a marine organosulfur compound with important roles in stress protection, marine biogeochemical cycling, chemical signalling and atmospheric chemistry. Diverse marine microorganisms catabolize DMSP via DMSP lyases to generate the climate-cooling gas and info-chemical dimethyl sulphide. Abundant marine heterotrophs of the Roseobacter group (MRG) are well known for their ability to catabolize DMSP via diverse DMSP lyases. Here, a new DMSP lyase DddU within the MRG strain Amylibacter cionae H-12 and other related bacteria was identified. DddU is a cupin superfamily DMSP lyase like DddL, DddQ, DddW, DddK and DddY, but shares <15% amino acid sequence identity with these enzymes. Moreover, DddU proteins forms a distinct clade from these other cupin-containing DMSP lyases. Structural prediction and mutational analyses suggested that a conserved tyrosine residue is the key catalytic amino acid residue in DddU. Bioinformatic analysis indicated that the dddU gene, mainly from Alphaproteobacteria, is widely distributed in the Atlantic, Pacific, Indian and polar oceans. For reference, dddU is less abundant than dddP, dddQ and dddK, but much more frequent than dddW, dddY and dddL in marine environments. This study broadens our knowledge on the diversity of DMSP lyases, and enhances our understanding of marine DMSP biotransformation. |
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