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首页> 外文期刊>Applied Microbiology >Malonic Semialdehyde Reductase from the Archaeon Nitrosopumilus maritimus Is Involved in the Autotrophic 3-Hydroxypropionate/4-Hydroxybutyrate Cycle
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Malonic Semialdehyde Reductase from the Archaeon Nitrosopumilus maritimus Is Involved in the Autotrophic 3-Hydroxypropionate/4-Hydroxybutyrate Cycle

机译：海古细菌Nitrosopumilus maritimus的丙二醛半醛还原酶参与了自养的3-羟基丙酸酯/ 4-羟基丁酸酯循环。

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The recently described ammonia-oxidizing archaea of the phylum Thaumarchaeota are highly abundant in marine, geothermal, and terrestrial environments. All characterized representatives of this phylum are aerobic chemolithoautotrophic ammonia oxidizers assimilating inorganic carbon via a recently described thaumarchaeal version of the 3-hydroxypropionate/4-hydroxybutyrate cycle. Although some genes coding for the enzymes of this cycle have been identified in the genomes of Thaumarchaeota , many other genes of the cycle are not homologous to the characterized enzymes from other species and can therefore not be identified bioinformatically. Here we report the identification and characterization of malonic semialdehyde reductase Nmar_1110 in the cultured marine thaumarchaeon Nitrosopumilus maritimus . This enzyme, which catalyzes the reduction of malonic semialdehyde with NAD(P)H to 3-hydroxypropionate, belongs to the family of iron-containing alcohol dehydrogenases and is not homologous to malonic semialdehyde reductases from Chloroflexus aurantiacus and Metallosphaera sedula . It is highly specific to malonic semialdehyde ( K_(m) , 0.11 mM; V _(max), 86.9 μmol min~(?1) mg~(?1) of protein) and exhibits only low activity with succinic semialdehyde ( K_(m) , 4.26 mM; V _(max), 18.5 μmol min~(?1) mg~(?1) of protein). Homologues of N. maritimus malonic semialdehyde reductase can be found in the genomes of all Thaumarchaeota sequenced so far and form a well-defined cluster in the phylogenetic tree of iron-containing alcohol dehydrogenases. We conclude that malonic semialdehyde reductase can be regarded as a characteristic enzyme for the thaumarchaeal version of the 3-hydroxypropionate/4-hydroxybutyrate cycle.
机译：最近描述的梭菌门的氨氧化古细菌在海洋，地热和陆地环境中高度丰富。该门的所有特征性代表都是需氧化自养自养性氨氧化剂，其通过最近描述的3-羟基丙酸酯/ 4-羟基丁酸酯循环的硫杂变形式吸收无机碳。尽管已经在Thaumarchaeota的基因组中确定了编码该循环酶的某些基因，但该循环的许多其他基因与其他物种的特征化酶并不同源，因此无法进行生物信息学鉴定。在这里，我们报告的鉴定和表征的丙二酸半醛还原酶Nmar_1110在养殖海洋拟南芥Nitrosopumilus maritimus。该酶催化NAD（P）H将丙二醛半醛还原为3-羟基丙酸酯，属于含铁的醇脱氢酶家族，与来自桔小球藻（Chloroflexus aurantiacus）和景天属（Metallosphaera sedula）的丙二醛半醛还原酶同源。它对丙二醛半醛（K_（m），0.11 mM; V _（max），86.9μmolmin〜（？1）mg〜（？1）蛋白质具有高度特异性，并且对琥珀酸半醛（K_（ m），4.26mM; V_（max），18.5μmolmin·（〜1）mg·（〜1）蛋白质）。到目前为止，已测序的所有丘缘古菌的基因组中都可以发现海马链霉菌丙二醛半醛还原酶的同系物，并在含铁醇脱氢酶的系统树中形成一个明确定义的簇。我们得出的结论是，丙二酸半醛还原酶可以被视为3-羟基丙酸酯/ 4-羟基丁酸酯循环的硫杂形式的特征酶。

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