藻类二甲硫释放酶的鉴定：海洋硫循环中的一个缺失环节,Science

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藻类二甲硫释放酶的鉴定：海洋硫循环中的一个缺失环节
Science ( IF 44.7 ) Pub Date : 2015-06-25 , DOI: 10.1126/science.aab1586
Uria Alcolombri _{1,

2} , Shifra Ben-Dor ₃ , Ester Feldmesser ₄ , Yishai Levin ₄ , Dan S. Tawfik ₁ , Assaf Vardi ₂

Affiliation

寻找海边海洋浮游植物的气味在全球硫循环中起着至关重要的作用。例如，藻类是从海洋释放到大气中的芳香族化合物二甲基硫醚 (DMS) 的主要来源。阿尔科隆布里等人。鉴定了负责在形成水华的海洋浮游植物 Emiliania huxleyi 中产生 DMS 的裂解酶（参见约翰斯顿的观点）。该基因在其他全球分布的浮游植物和珊瑚中的存在表明它可以作为跨不同门的 DMS 生产的可靠指标。由于 DMS 被氧化成硫气溶胶，作为云凝结核，这种酶是一种关键的全球生物地球化学催化剂。科学，这个问题 p。第1466章另见第。1430 Emiliania huxleyi 的二甲基磺基丙酸裂解酶是参与海洋硫循环的大型酶家族的一部分。[另请参阅约翰斯顿的观点] 藻华会产生大量二甲基硫醚 (DMS)，这是一种在排放到大气中的海洋食物网中具有多种信号作用的挥发性物质，在那里它会影响云的形成。负责从二甲基磺基丙酸酯 (DMSP) 形成 DMS 的藻类酶仍然未知，尽管它们在全球硫循环中起着关键作用。我们鉴定并表征了 Alma1，这是一种来自形成水华的藻类 Emiliania huxleyi 的 DMSP 裂解酶。Alma1 是天冬氨酸消旋酶超家族的四聚体、氧化还原敏感酶。重组 Alma1 表现出与 E. huxleyi 中的 DMSP 裂解酶相同的生化特征，以及由各种 E. huxleyi 释放的 DMS。huxleyi 分离株与其 Alma1 水平相关。序列同源性搜索表明，Alma1 代表存在于主要、全球分布的浮游植物类群和其他海洋生物中的一个基因家族。

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

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 The dimethylsulfoniopropionate lyase of Emiliania huxleyi is part of a large enzyme family involved in the marine sulfur cycle. [Also see Perspective by Johnston] 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.

更新日期：2015-06-25

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