Identification of the algal dimethyl sulfide–releasing enzyme: A missing link in the marine sulfur cycle

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Science  26 Jun 2015:
Vol. 348, Issue 6242, pp. 1466-1469
DOI: 10.1126/science.aab1586

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Sourcing the smell of the seaside

Marine phytoplankton plays a critical role in the global sulfur cycle. Algae, for instance, are the main source of the aromatic compound dimethylsulfide (DMS) released from the oceans into the atmosphere. Alcolombri et al. identified the lyase enzyme responsible for DMS production in the bloom-forming marine phytoplankton Emiliania huxleyi (see the Perspective by Johnston). The presence of this gene in other globally distributed phytoplankton and corals suggests that it may serve as a reliable indicator of DMS production across diverse phyla. Because DMS gets oxidized to sulfur aerosols, which act as cloud condensation nuclei, this enzyme is a key global biogeochemical catalyst.

Science, this issue p. 1466; see also p. 1430


Algal blooms produce large amounts of dimethyl sulfide (DMS), a volatile with a diverse signaling role in marine food webs that is emitted to the atmosphere, where it can affect cloud formation. The algal enzymes responsible for forming DMS from dimethylsulfoniopropionate (DMSP) remain unidentified despite their critical role in the global sulfur cycle. We identified and characterized Alma1, a DMSP lyase from the bloom-forming algae Emiliania huxleyi. Alma1 is a tetrameric, redox-sensitive enzyme of the aspartate racemase superfamily. Recombinant Alma1 exhibits biochemical features identical to the DMSP lyase in E. huxleyi, and DMS released by various E. huxleyi isolates correlates with their Alma1 levels. Sequence homology searches suggest that Alma1 represents a gene family present in major, globally distributed phytoplankton taxa and in other marine organisms.

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