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DOI:10.1126/SCIENCE.1135370 - Corpus ID: 22472634
@article{Todd2007StructuralAR, title={Structural and Regulatory Genes Required to Make the Gas Dimethyl Sulfide in Bacteria}, author={Jonathan D. Todd and Rachel Rogers and You Guo Li and Margaret Wexler and Philip L. Bond and Lei Sun and Andrew R. J. Curson and Gillian Malin and Michael Steinke and Andrew W. B. Johnston}, journal={Science}, year={2007}, volume={315}, pages={666 - 669}, url={https://api.semanticscholar.org/CorpusID:22472634}}
- J. Todd, Rachel Rogers, A. Johnston
- Published in Science 2 February 2007
- Environmental Science, Biology, Chemistry
It is demonstrated that the bacterial gene dddD is required for this process and that its transcription is induced by the DMSP substrate, and the inferred enzymatic mechanism for DMS liberation involves an initial step in which DMSP is modified by addition of acyl coenzyme A, rather than the immediate release of DMS by a DMSP lyase, the previously suggested mechanism.
260 Citations
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260 Citations
- Xiaohua ZhangJi Liu J. Todd
- 2019
Environmental Science, Biology
Science China Life Sciences
The global distribution pattern of DMSP and DMS, the known genes for biosynthesis and cleavage ofDMSP, and the physiological and ecological functions of these important organosulfur molecules are described, which will improve understanding of the mechanisms of DM SP and D MS production and their roles in the environment.
- 73
- PDF
- Chunyang LiXiu-Juan Wang Yu‐Zhong Zhang
- 2020
Environmental Science, Biology
bioRxiv
AcoD, an ATP-dependent DMSP lyase that belongs to the acyl-CoA synthetase superfamily, is widely distributed in many bacterial lineages, revealing this new pathway plays important roles in global DMSP/DMS cycles.
- 1
- PDF
- Chunyang LiTian‐Di Wei Yu‐Zhong Zhang
- 2014
Biology, Chemistry
Proceedings of the National Academy of Sciences
The crystal structure of DddQ, a DMSP lyase, was solved, and detailed biochemical and structural analyses were performed, providing important insight into the mechanism involved in the conversion of DMSP into DMS, which should lead to a better understanding of this globally important biogeochemical reaction.
- 52
- PDF
- M. MoranC. ReischR. KieneW. Whitman
- 2012
Environmental Science, Biology
Annual review of marine science
Genomic and functional genomic methods applied to both model organisms and natural communities have rapidly advanced understanding of bacterial dimethylsulfoniopropionate (DMSP) degradation in the ocean, but gene transcription analyses of natural bacterioplankton communities are making headway in unraveling the intricacies of bacterial DMSP processing in the Ocean.
- 154
- Jingli LiuJi Liu Xiaohua Zhang
- 2018
Environmental Science, Biology
Front. Microbiol.
Gene probes to the DMSP demethylation gene dmdA and theDMSP lyase gene dddP demonstrated that these DMSP-degrading genes are abundant and widely distributed in ECS seawaters, further confirming the link between this abundant bacterial class and the environmental DMSP cycling.
- 35
- Highly Influenced
- PDF
- H. BullockHaiwei LuoW. Whitman
- 2017
Environmental Science, Biology
Front. Microbiol.
Experimental evidence is covered supporting the hypothesis that, as DMSP became more readily available in the marine environment, marine bacteria adapted enzymes already encoded in their genomes to utilize this new compound.
- 95
- Highly Influenced
- PDF
- I. BurkhardtLukas LauterbachNelson L. BrockJeroen S. Dickschat
- 2017
Chemistry, Environmental Science
Comparative kinetic assays revealed differences in the conversion of DMSP and its analogues in terms of selectivity and overall velocity, giving additional insights into the molecular mechanisms ofDMSP lyases and into their putatively different biological functions.
- 20
- Uria AlcolombriP. LaurinoPedro Lara-AstiasoA. VardiDan S. Tawfik
- 2014
Environmental Science, Chemistry
Biochemistry
This work has identified DMSP and acetyl-coenzyme A to be DddD's native substrates and Asp602 as the active site residue mediating the CoA-transferase prior to lyase activity and shed light on the biochemical utilization of DMSP in the marine environment.
- 47
- Chunyang LiXiu-Juan Wang Yu‐Zhong Zhang
- 2021
Environmental Science, Chemistry
eLife
DddX is a novel ATP-dependent DMSP lyase that belongs to the acyl-CoA synthetase superfamily and is distinct from the eight other knownDMSP lyases, and may play an overlooked role in DMSP/DMS cycles.
- 29
- Highly Influenced
- PDF
- L. LeiUria AlcolombriDan S. Tawfik
- 2018
Environmental Science, Biology
Methods in enzymology
- 1
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18 References
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Environmental Science, Biology
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- E. C. HowardJames R. Henriksen M. Moran
- 2006
Environmental Science, Biology
Science
Through the discovery of a glycine cleavage T-family protein with DMSP methyltransferase activity, marine bacterioplankton in the Roseobacter and SAR11 taxa were identified as primary mediators of DMSP demethylation to methylmercaptopropate.
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- J. AnsedeR. FriedmanD. C. Yoch
- 2001
Environmental Science, Biology
Applied and Environmental Microbiology
Bacterial population analysis based on culturability has its limitations, bacteria from the α and γ subclasses of the Proteobacteria were the dominant DMS producers isolated from salt marsh sediments and estuaries, with the γ subclass representing 80% of the isolates.
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- PDF
- D. C. Yoch
- 2002
Environmental Science, Biology
Applied and Environmental Microbiology
This article is more comprehensive, as it includes some of the earlier literature in describing the sources of DMSP, its release and linkage to the marine (primarily microbial) food web and subsequent degradation via cleavage to DMS and acrylic acid or demethylation and demethiolation to methanethiol.
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- J. Stefels
- 2000
Environmental Science, Biology
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- R. Kiene
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Environmental Science
Applied and environmental microbiology
The results illustrate the significant potential for microbial conversion of dissolved DMSP to DMS in coastal seawater and the sensitivity to inhibitors with respect to growth and DMSP-lyase activity varied from strain to strain.
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- PDF
- Todd R. MillerR. Belas
- 2004
Biology, Environmental Science
Applied and Environmental Microbiology
The diverse metabolism of DMSP by the dinoflagellate-associated Roseobacter spp.
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- PDF
- M. MoranA. Buchan N. Ward
- 2004
Environmental Science, Biology
Nature
The genome sequence of Silicibacter pomeroyi, a member of the marine Roseobacter clade, is described, indicating that this organism relies upon a lithoheterotrophic strategy that uses inorganic compounds to supplement heterotrophy.
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- J. AnsedeP. PellechiaD. C. Yoch
- 2001
Environmental Science, Chemistry
Applied and Environmental Microbiology
A putative model is presented that best fits the experimental data regarding the pathway of DMSP and acrylate metabolism in the α-proteobacterium, strain LFR.
- 26
- PDF
- M. SteinkeJ. StefelsE. Stamhuis
- 2006
Biology, Environmental Science
It is demonstrated that copepods can detect and react to plumes of DMS and suggest that this biogenic trace gas can influence the structure and function of pelagic foodwebs.
- 112
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