Enzymatic breakage of dimethylsulfoniopropionate—a signature molecule for life at sea

•Dimethylsulfoniopropionate (DMSP) is made in large amounts by marine eukaryotes.•Various marine microorganisms can catabolise this zwitterion in a range of different ways.•Recent studies reveal novel enzymatic mechanisms for DMSP cleavage or demethylation.•We review these findings, in relation to e...

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Bibliographic Details
Published in:Current opinion in chemical biology 2016-04, Vol.31, p.58-65
Main Authors: Johnston, Andrew WB, Green, Robert T, Todd, Jonathan D
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Bacteria - enzymology
Bacteria - genetics
Enzymes - chemistry
Enzymes - metabolism
Genes, Bacterial
Marine Biology
Seawater
Sequence Homology, Amino Acid
Sulfonium Compounds - metabolism
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Summary:•Dimethylsulfoniopropionate (DMSP) is made in large amounts by marine eukaryotes.•Various marine microorganisms can catabolise this zwitterion in a range of different ways.•Recent studies reveal novel enzymatic mechanisms for DMSP cleavage or demethylation.•We review these findings, in relation to earlier genetic studies on this process. Largely using gene-based evidence, the last few years have seen real insights on the diverse ways in which different microbes break down dimethylsulfoniopropionate, an abundant anti-stress molecule that is made by marine algae, some corals and a few angiosperms. Here, we review more recent advances in which in vitro biochemical tools—including structural determinations—have shed new light on how the corresponding enzymes act on DMSP. These have revealed how enzymes in very different polypeptide families can act on this substrate, often by novel ways, and with broader implications that extend from enzymatic mechanisms to microbial ecology.
ISSN:1367-5931
1879-0402
DOI:10.1016/j.cbpa.2016.01.011