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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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| Published in: | Current opinion in chemical biology 2016-04, Vol.31, p.58-65 |
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| Language: | English |
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| container_title | Current opinion in chemical biology |
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| creator | Johnston, Andrew WB Green, Robert T Todd, Jonathan D |
| description | •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. |
| doi_str_mv | 10.1016/j.cbpa.2016.01.011 |
| format | article |
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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.</description><identifier>ISSN: 1367-5931</identifier><identifier>EISSN: 1879-0402</identifier><identifier>DOI: 10.1016/j.cbpa.2016.01.011</identifier><identifier>PMID: 26851513</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>Amino Acid Sequence ; Bacteria - enzymology ; Bacteria - genetics ; Enzymes - chemistry ; Enzymes - metabolism ; Genes, Bacterial ; Marine Biology ; Seawater ; Sequence Homology, Amino Acid ; Sulfonium Compounds - metabolism</subject><ispartof>Current opinion in chemical biology, 2016-04, Vol.31, p.58-65</ispartof><rights>2016</rights><rights>Copyright © 2016. Published by Elsevier Ltd.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c466t-a5718c3b895177f305150be6b83a3ed992242c4ef08f01a319fc5b10fdea6e6f3</citedby><cites>FETCH-LOGICAL-c466t-a5718c3b895177f305150be6b83a3ed992242c4ef08f01a319fc5b10fdea6e6f3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,786,790,27957,27958</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/26851513$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Johnston, Andrew WB</creatorcontrib><creatorcontrib>Green, Robert T</creatorcontrib><creatorcontrib>Todd, Jonathan D</creatorcontrib><title>Enzymatic breakage of dimethylsulfoniopropionate—a signature molecule for life at sea</title><title>Current opinion in chemical biology</title><addtitle>Curr Opin Chem Biol</addtitle><description>•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.
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| ispartof | Current opinion in chemical biology, 2016-04, Vol.31, p.58-65 |
| issn | 1367-5931 1879-0402 |
| language | eng |
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| source | ScienceDirect Freedom Collection |
| subjects | Amino Acid Sequence Bacteria - enzymology Bacteria - genetics Enzymes - chemistry Enzymes - metabolism Genes, Bacterial Marine Biology Seawater Sequence Homology, Amino Acid Sulfonium Compounds - metabolism |
| title | Enzymatic breakage of dimethylsulfoniopropionate—a signature molecule for life at sea |
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