A novel ATP dependent dimethylsulfoniopropionate lyase in bacteria that releases dimethyl sulfide and acryloyl-CoA

Li, 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 and Zhang, Yu-Zhong (2021) A novel ATP dependent dimethylsulfoniopropionate lyase in bacteria that releases dimethyl sulfide and acryloyl-CoA. eLife, 10. ISSN 2050-084X

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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.

Item Type:	Article
Uncontrolled Keywords:	sdg 14 - life below water ,/dk/atira/pure/sustainabledevelopmentgoals/life_below_water
Faculty \ School:	Faculty of Science > School of Biological Sciences
Related URLs:	https://elifesciences.org/articles/64045
Depositing User:	LivePure Connector
Date Deposited:	28 May 2021 00:33
Last Modified:	24 Oct 2022 06:45
URI:	https://ueaeprints.uea.ac.uk/id/eprint/80145
DOI:	10.7554/eLife.64045

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