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

Chun-Yang Li, Xiu-Juan Wang, Xiu-Lan Chen, Qi Sheng, Shan Zhang, Peng Wang, Mussa Quareshy, Branko Rihtman, Xuan Shao, Chao Gao, Fuchuan Li, Shengying Li, Weipeng Zhang, Xiao-Hua Zhang, Gui-Peng Yang, Jonathan D. Todd, Yin Chen, Yu-Zhong Zhang

Research output: Contribution to journalArticlepeer-review

40 Citations (Scopus)
20 Downloads (Pure)


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.
Original languageEnglish
Article numbere64045
Publication statusPublished - 10 May 2021

Cite this