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

Curr Opin Chem Biol. 2016 Apr:31:58-65. doi: 10.1016/j.cbpa.2016.01.011. Epub 2016 Feb 4.

Abstract

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.

Publication types

  • Review
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacteria / enzymology
  • Bacteria / genetics
  • Enzymes / chemistry
  • Enzymes / metabolism*
  • Genes, Bacterial
  • Marine Biology*
  • Seawater*
  • Sequence Homology, Amino Acid
  • Sulfonium Compounds / metabolism*

Substances

  • Enzymes
  • Sulfonium Compounds
  • dimethylpropiothetin