Bacterial SBP56 identified as a Cu-dependent methanethiol oxidase widely distributed in the biosphere.
Bacterial SBP56 identified as a Cu-dependent methanethiol oxidase widely distributed in the biosphere.
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DOI：
10.1038/ismej.2017.148
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发表时间：
2018-01
期刊：
影响因子：
--
通讯作者：
Schäfer H
中科院分区：
文献类型：
--
作者：
Eyice Ö;Myronova N;Pol A;Carrión O;Todd JD;Smith TJ;Gurman SJ;Cuthbertson A;Mazard S;Mennink-Kersten MA;Bugg TD;Andersson KK;Johnston AW;Op den Camp HJ;Schäfer H
甲烷乙烷氧化是硫循环中的重要步骤。MT是全球重要的有机硫化合物包括二甲基磺基丙酸酯（DMSP）和二甲基硫醚（DMS）的代谢中间体，在海洋碳和硫循环中起着关键作用。在需氧细菌中，MT被MT氧化酶（MTO）降解。MT氧化的酶和遗传基础仍然很差。在这里，我们首次确定的MTO酶和它的编码基因（mtoX）在DMS降解细菌Hyphomicrobium SP。VS。我们表明，MTO是一种同源四聚体金属酶，需要铜的酶活性。MTO被预测为可溶性周质酶，并且是硒结合蛋白（SBP 56）家族的不同进化枝的成员，其功能尚未被报道。与mtoX正交的基因存在于许多能够降解DMS、其他一碳化合物或DMSP的细菌中，特别是在海洋模式生物Ruegeria pomeroyi DSS-3中，该模式生物Ruegeria pomeroyi DSS-3是海洋环境中大量存在的杜鹃花科（Rhododocellaceae）的成员。mtoX的标记交换突变破坏了R. pomeroyi代谢MT，证实其在这种DMSP降解细菌中的功能。In R. pomeroyi，mtoX的转录被DMSP、甲基巯基丙酸酯和MT增强。MT降解率增加后，预孵育的野生型菌株与MT。在多种细菌、环境样品中检测到mtoX直系同源物及其在一系列宏基因组数据集中的丰度，表明这种酶广泛分布于环境中，并在全球硫循环中发挥关键作用。
Oxidation of methanethiol (MT) is a significant step in the sulfur cycle. MT is an intermediate of metabolism of globally significant organosulfur compounds including dimethylsulfoniopropionate (DMSP) and dimethylsulfide (DMS), which have key roles in marine carbon and sulfur cycling. In aerobic bacteria, MT is degraded by a MT oxidase (MTO). The enzymatic and genetic basis of MT oxidation have remained poorly characterized. Here, we identify for the first time the MTO enzyme and its encoding gene (mtoX) in the DMS-degrading bacterium Hyphomicrobium sp. VS. We show that MTO is a homotetrameric metalloenzyme that requires Cu for enzyme activity. MTO is predicted to be a soluble periplasmic enzyme and a member of a distinct clade of the Selenium-binding protein (SBP56) family for which no function has been reported. Genes orthologous to mtoX exist in many bacteria able to degrade DMS, other one-carbon compounds or DMSP, notably in the marine model organism Ruegeria pomeroyi DSS-3, a member of the Rhodobacteraceae family that is abundant in marine environments. Marker exchange mutagenesis of mtoX disrupted the ability of R. pomeroyi to metabolize MT confirming its function in this DMSP-degrading bacterium. In R. pomeroyi, transcription of mtoX was enhanced by DMSP, methylmercaptopropionate and MT. Rates of MT degradation increased after pre-incubation of the wild-type strain with MT. The detection of mtoX orthologs in diverse bacteria, environmental samples and its abundance in a range of metagenomic data sets point to this enzyme being widely distributed in the environment and having a key role in global sulfur cycling.
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影响因子：
3.5
作者：
Flemetakis, E;Agalou, A;Katinakis, P
通讯作者：
Katinakis, P
DOI：
10.1038/ismej.2015.37
发表时间：
2015-11
期刊：
The ISME journal
影响因子：
--
作者：
Eyice Ö;Namura M;Chen Y;Mead A;Samavedam S;Schäfer H
通讯作者：
Schäfer H
影响因子：
4.4
作者：
Kettle, AJ;Rhee, TS;Andreae, MO
通讯作者：
Andreae, MO
影响因子：
5.8
作者：
Hernandez, David;Tewhey, Ryan;Schrenzel, Jacques
通讯作者：
Schrenzel, Jacques
DOI：
10.1111/j.1432-1033.1992.tb17360.x
发表时间：
1992-11-01
期刊：
EUROPEAN JOURNAL OF BIOCHEMISTRY
影响因子：
--
作者：
ANTHOLINE, WE;KASTRAU, DHW;KRONECK, PMH
通讯作者：
KRONECK, PMH