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Elife

Title:		A novel ATP dependent dimethylsulfoniopropionate lyase in bacteria that releases dimethyl sulfide and acryloyl-CoA
Author(s):		Li CY; Wang XJ; Chen XL; Sheng Q; Zhang S; Wang P; Quareshy M; Rihtman B; Shao X; Gao C; Li F; Li S; Zhang W; Zhang XH; Yang GP; Todd JD; Chen Y; Zhang YZ;
Address:		"State Key Lab of Microbial Technology, Marine Biotechnology Research Center, Shandong University, Qingdao, China. College of Marine Life Sciences, Ocean University of China, Qingdao, China. Laboratory for Marine Biology and Biotechnology, Pilot National Laboratory for Marine Science and Technology, Qingdao, China. School of Life Sciences, University of Warwick, Coventry, United Kingdom. National Glycoengineering Research Center and Shandong Key Laboratory of Carbohydrate Chemistry and Glycobiology, Shandong University, Qingdao, China. Frontiers Science Center for Deep Ocean Multispheres and Earth System, Key Laboratory of Marine Chemistry Theory and Technology, Ministry of Education, Ocean University of China, Qingdao, China. School of Biological Sciences, University of East Anglia, Norwich Research Park, Norwich, United Kingdom. Marine Biotechnology Research Center, State Key Laboratory of Microbial Technology, Shandong University, Qingdao, China"
Journal Title:		Elife
Year:		2021
Volume:		20210510
Issue:
Page Number:		-
DOI:		10.7554/eLife.64045
ISSN/ISBN:		2050-084X (Electronic) 2050-084X (Linking)
Abstract:		"Dimethylsulfoniopropionate (DMSP) is an abundant and ubiquitous organosulfur molecule in marine environments with important roles in global sulfur and nutrient cycling. Diverse DMSP lyases in some algae, bacteria, and fungi cleave DMSP to yield gaseous dimethyl sulfide (DMS), an infochemical with important roles in atmospheric chemistry. Here, we identified a novel ATP-dependent DMSP lyase, DddX. DddX belongs to the acyl-CoA synthetase superfamily and is distinct from the eight other known DMSP lyases. DddX catalyses the conversion of DMSP to DMS via a two-step reaction: the ligation of DMSP with CoA to form the intermediate DMSP-CoA, which is then cleaved to DMS and acryloyl-CoA. The novel catalytic mechanism was elucidated by structural and biochemical analyses. DddX is found in several Alphaproteobacteria, Gammaproteobacteria, and Firmicutes, suggesting that this new DMSP lyase may play an overlooked role in DMSP/DMS cycles. The global sulfur cycle is a collection of geological and biological processes that circulate sulfur-containing compounds through the oceans, rocks and atmosphere. Sulfur itself is essential for life and important for plant growth, hence its widespread use in fertilizers. Marine organisms such as bacteria, algae and phytoplankton produce one particular sulfur compound, called dimethylsulfoniopropionate, or DMSP, in massive amounts. DMSP made in the oceans gets readily converted into a gas called dimethyl sulfide (DMS), which is the largest natural source of sulfur entering the atmosphere. In the air, DMS is converted to sulfate and other by-products that can act as cloud condensation nuclei, which, as the name suggests, are involved in cloud formation. In this way, DMS can influence weather and climate, so it is often referred to as 'climate-active' gas. At least eight enzymes are known to cleave DMSP into DMS gas with a few by-products. These enzymes are found in algae, bacteria and fungi, and are referred to as lyases, for the way they breakdown their target compounds (DMSP, in this case). Recently, researchers have identified some bacteria that produce DMS from DMSP without using known DMSP lyases. This suggests there are other, unidentified enzymes that act on DMSP in nature, and likely contribute to global sulfur cycling. Li, Wang et al. set out to uncover new enzymes responsible for converting the DMSP that marine bacteria produce into gaseous DMS. One new enzyme called DddX was identified and found to belong to a superfamily of enzymes quite separate to other known DMSP lyases. Li, Wang et al. also showed how DddX drives the conversion of DMSP to DMS in a two-step reaction, and that the enzyme is found across several classes of bacteria. Further experiments to characterise the protein structure of DddX also revealed the molecular mechanism for its catalytic action. This study offers important insights into how marine bacteria generate the climatically important gas DMS from DMSP, leading to a better understanding of the global sulfur cycle. It gives microbial ecologists a more comprehensive perspective of these environmental processes, and provides biochemists with data on a family of enzymes not previously known to act on sulfur-containing compounds. eng"
Keywords:		Acyl Coenzyme A/metabolism Adenosine Triphosphate Bacteria/growth & development/isolation & purification Bacterial Proteins/chemistry Carbon-Sulfur Lyases/*chemistry/genetics Psychrobacter/*enzymology/genetics/growth & development Sulfides/metabolism Sulf;
Notes:		"MedlineLi, Chun-Yang Wang, Xiu-Juan Chen, Xiu-Lan Sheng, Qi Zhang, Shan Wang, Peng Quareshy, Mussa Rihtman, Branko Shao, Xuan Gao, Chao Li, Fuchuan Li, Shengying Zhang, Weipeng Zhang, Xiao-Hua Yang, Gui-Peng Todd, Jonathan D Chen, Yin Zhang, Yu-Zhong eng Research Support, Non-U.S. Gov't England 2021/05/11 Elife. 2021 May 10; 10:e64045. doi: 10.7554/eLife.64045"