title: Enzymatic breakage of dimethylsulfoniopropionate-a signature molecule for life at sea.
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.
authors: School of Biological Sciences, University of East Anglia, Norwich Research Park, Norwich NR4 7TJ, UK. Electronic address: a.johnston@uea.ac.uk.
authors: Andrew Wb
authors: AW
authors: Johnston
authors: School of Biological Sciences, University of East Anglia, Norwich Research Park, Norwich NR4 7TJ, UK.
authors: Robert T
authors: RT
authors: Green
authors: School of Biological Sciences, University of East Anglia, Norwich Research Park, Norwich NR4 7TJ, UK. Electronic address: jonathan.todd@uea.ac.uk.
authors: Jonathan D
authors: JD
authors: Todd
mesh_terms: D000595:Amino Acid Sequence; D001419:Bacteria / Q000201:enzymology / Q000235:genetics; D004798:Enzymes / Q000737:chemistry / Q000378:metabolism*; D005798:Genes, Bacterial; D008386:Marine Biology; D012623:Seawater; D017386:Sequence Homology, Amino Acid; D013452:Sulfonium Compounds / Q000378:metabolism*
chemical_list: D004798:Enzymes; D013452:Sulfonium Compounds; C068078:dimethylpropiothetin