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

• DOI: 10.7554/elife.64045
• Publication Date: 2021-05-10T12:00:30Z
• Authors: 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
• Keywords: Dimethylsulfoniopropionate; Dimethyl sulfide; Lyase; Alphaproteobacteria; Organosulfur compounds; Marine bacteriophage

Dimethylsulfoniopropionate (DMSP) is an abundant and ubiquitous organosulfur molecule in marine environments with important roles global sulfur nutrient cycling. Diverse DMSP lyases some algae, bacteria, fungi cleave to yield gaseous dimethyl sulfide (DMS), infochemical atmospheric chemistry. Here, we identified a novel ATP-dependent lyase, DddX. DddX belongs the acyl-CoA synthetase superfamily distinct from eight other known lyases. catalyses conversion of DMS via two-step reaction: ligation CoA form intermediate DMSP-CoA, which then cleaved acryloyl-CoA. The catalytic mechanism was elucidated by structural biochemical analyses. found several Alphaproteobacteria, Gammaproteobacteria, Firmicutes, suggesting that this new lyase may play overlooked role DMSP/DMS cycles.