Display Settings:

Format

Send to:

Choose Destination
We are sorry, but NCBI web applications do not support your browser and may not function properly. More information
    ISME J. 2011 Jul;5(7):1191-200. doi: 10.1038/ismej.2010.203. Epub 2011 Jan 20.

    DddY, a periplasmic dimethylsulfoniopropionate lyase found in taxonomically diverse species of Proteobacteria.

    Source

    School of Biological Sciences, University of East Anglia, Norwich, UK.

    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 β-, ɛ- and γ-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.

    PMID:
    21248856
    [PubMed - indexed for MEDLINE]
    PMCID:
    PMC3146280
    Free PMC Article

    Images from this publication.See all images (5)Free text

    Figure 1
    Figure 2
    Figure 3
    Figure 4
    Figure 5

      Supplemental Content

      Icon for Nature Publishing Group Icon for PubMed Central

      Save items

      Recent activity

      Your browsing activity is empty.

      Activity recording is turned off.

      Turn recording back on

      See more...
      Write to the Help Desk