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Towards a systematic understanding of structure–function relationship of dimethylsulfoniopropionate‐catabolizing enzymes
Author(s) -
Chen Yin,
Schäfer Hendrik
Publication year - 2019
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/mmi.14230
Subject(s) - dimethylsulfoniopropionate , osmolyte , biogeochemical cycle , biology , demethylation , enzyme , biochemistry , phytoplankton , ecology , gene expression , nutrient , gene , dna methylation
Summary Each year, several million tons of dimethylsulfoniopropionate (DMSP) are produced by marine phytoplankton and bacteria as an important osmolyte to regulate their cellular osmosis. Microbial breakdown of DMSP to the volatile gas dimethylsulfide (DMS) plays an important role in global biogeochemical cycles of the sulphur element between land and the sea. Understanding the enzymes involved in the transformation of DMSP and DMS holds the key to a better understanding of oceanic DMSP cycles. Recent work by Shao et al. (2019) has resolved the crystal structure of two important enzymes, DmdB and DmdC, involved in DMSP transformation through the demethylation pathway. Their work represents an important step towards a systematic understanding of the structure–function relationships of DMSP‐catabolizing enzymes in marine microbes.