| Literature DB >> 26113722 |
Uria Alcolombri1, Shifra Ben-Dor2, Ester Feldmesser3, Yishai Levin3, Dan S Tawfik4, Assaf Vardi5.
Abstract
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.Entities:
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Year: 2015 PMID: 26113722 DOI: 10.1126/science.aab1586
Source DB: PubMed Journal: Science ISSN: 0036-8075 Impact factor: 47.728