{"refrec":{"BRefID":248084,"RR":"<b>Alcolombri, U.; Ben-Dor, S.; Feldmesser, E.; Levin, Y.; Tawfik, D.S.; Vardi, A.</b> (2015). Identification of the algal dimethyl sulfide–releasing enzyme: A missing link in the marine sulfur cycle. <i>Science (Wash.) 348(6242 )</i>: 1466-1469. <a href=\"http://dx.doi.org/10.1126/science.aab1586\" target=\"_blank\">http://dx.doi.org/10.1126/science.aab1586</a>","BEntID":239788,"PublicFlag":1,"CheckedFlag":1,"wosflag":1,"vabbflag":1,"RefStringPartII":". <i>Science (Wash.) 348(6242 )</i>: 1466-1469. <a href=\"http://dx.doi.org/10.1126/science.aab1586\" target=\"_blank\">http://dx.doi.org/10.1126/science.aab1586</a>","DocTypID":8,"DocType":"Journal article","MarineFlag":1,"FreshFlag":0,"BrackishFlag":0,"TerrestrialFlag":0,"Authorstring":"Alcolombri, U.; Ben-Dor, S.; Feldmesser, E.; Levin, Y.; Tawfik, D.S.; Vardi, A.","OrigTitleTranslFlag":0,"Authorstringtrunc":"Alcolombri, U. <i>et al.</i>","Englishabstract":"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 <i>Emiliania huxleyi</i>. 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 <i>E. huxleyi</i> 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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