ArticleEnvironmental microbiology2023
A new dimethylsulfoniopropionate lyase of the cupin superfamily in marine bacteria.
Article in Environmental microbiology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 22 citations in OpenAlex.
- Identification of a functional DddX-like enzyme that catalyzes dimethylsulfoniopropionate cleavage in marine bacteria.Engineering microbiology · 2026Article
- Dimethylsulfoniopropionate metabolism shapes microbial ecology and physiological adaptation during the austral winter in Southern Ocean sea ice and seawater.Nature communications · 2026Article
- Metabolic Regulation of Dimethylsulfoniopropionate Cleavage and Dimethyl Sulfide Production in Halomonas sp. D47.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Regulation of DMSP organosulfur cycling in ubiquitous Roseobacter marine bacteria.The EMBO journal · 2026Article
- Predicted shifts in bacterial and algal contributions to DMSP and DMS dynamics during a coastal spring-summer bloom.The ISME journal · 2026Article
- Genome-resolved adaptation strategies ofApplied and environmental microbiology · 2025Article
- Cloning and expression of the dimethylsulfoniopropionate lyase geneCurrent research in microbial sciences · 2025Article
- Dimethylsulfoniopropionate (DMSP) Increases Longevity and Mitochondrial Function inEnvironment & health (Washington, D.C.) · 2024Article
- DMSOP-cleaving enzymes are diverse and widely distributed in marine microorganisms.Nature microbiology · 2023Article
- A new dimethylsulfoniopropionate lyase of the cupin superfamily in marine bacteria.Environmental microbiology · 2023Article
Corrections and comments
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Authors and funding
8 authors at 5 institutions in 2 countries.
Funding
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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