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Curson, Andrew R. J., Sullivan, Matthew J. 
ORCID: https://orcid.org/0000-0003-2276-3132, Todd, Jonathan D. and Johnston, Andrew W. B.
(2011)
DddY, a periplasmic dimethylsulfoniopropionate lyase found in taxonomically diverse species of Proteobacteria.
The ISME Journal, 5 (7).
pp. 1191-1200.
ISSN 1751-7362
Abstract
The abundant compatible solute dimethylsulfoniopropionate (DMSP) is made by many marine algae. Different marine bacteria catabolise DMSP by various mechanisms, some of which liberate the environmentally important gas dimethyl sulfide (DMS). We describe an enzyme, DddY, which cleaves DMSP into DMS plus acrylate and is located in the bacterial periplasm, unlike other DMSP lyases that catalyse this reaction. There are dddY-like genes in strains of Alcaligenes, Arcobacter and Shewanella, in the ß-, e- and ?-proteobacteria, respectively. In Alcaligenes, dddY is in a cluster of ddd and acu genes that resemble, but also have significant differences to, those in other bacteria that catabolise both DMSP and acrylate. Although production of DMS and transcription of Alcaligenes dddY are both apparently inducible by pre-growth of cells with DMSP, this substrate must be catabolised to form acrylate, the bona fide coinducer.
| 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 |
| UEA Research Groups: | Faculty of Science > Research Groups > Environmental Biology Faculty of Science > Research Groups > Resources, Sustainability and Governance (former - to 2018) Faculty of Science > Research Groups > Molecular Microbiology |
| Depositing User: | Users 2731 not found. |
| Date Deposited: | 09 Jan 2012 13:18 |
| Last Modified: | 21 Nov 2022 16:30 |
| URI: | https://ueaeprints.uea.ac.uk/id/eprint/35963 |
| DOI: | 10.1038/ismej.2010.203 |
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