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首页> 外文期刊>FEBS Open Bio >MutT from the fish pathogen Aliivibrio salmonicida is a cold-active nucleotide-pool sanitization enzyme with unexpectedly high thermostability
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MutT from the fish pathogen Aliivibrio salmonicida is a cold-active nucleotide-pool sanitization enzyme with unexpectedly high thermostability

机译：来自鱼类病原体Aliivibrio salicida的MutT是一种冷活性核苷酸池消毒酶，具有极高的热稳定性

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Upon infection by pathogenic bacteria, production of reactive oxygen species (ROS) is part of the host organism's first line of defence. ROS damage a number of macromolecules, and in order to withstand such a harsh environment, the bacteria need to have well-functioning ROS scavenging and repair systems. Herein, MutT is an important nucleotide-pool sanitization enzyme, which degrades 8-oxo-dGTP and thus prevents it from being incorporated into DNA. In this context, we have performed a comparative biochemical and structural analysis of MutT from the fish pathogen Aliivibrio salmonicida (AsMutT) and the human pathogen Vibrio cholerae (VcMutT), in order to analyse their function as nucleotide sanitization enzymes and also determine possible cold-adapted properties of AsMutT. The biochemical characterisation revealed that both enzymes possess activity towards the 8-oxo-dGTP substrate, and that AsMutT has a higher catalytic efficiency than VcMutT at all temperatures studied. Calculations based on the biochemical data also revealed a lower activation energy (E"a) for AsMutT compared to VcMutT, and differential scanning calorimetry experiments showed that AsMutT displayed an unexpected higher melting temperature (T"m) value than VcMutT. A comparative analysis of the crystal structure of VcMutT, determined to 2.42A resolution, and homology models of AsMutT indicate that three unique Gly residues in loops of VcMutT, and additional long range ion-pairs in AsMutT could explain the difference in temperature stability of the two enzymes. We conclude that AsMutT is a stable, cold-active enzyme with high catalytic efficiency and reduced E"a, compared to the mesophilic VcMutT.
机译：一旦被病原菌感染，活性氧（ROS）的产生是宿主生物防御的第一道防线的一部分。 ROS破坏了许多大分子，为了承受这种恶劣的环境，细菌需要具有功能良好的ROS清除和修复系统。在本文中，MutT是重要的核苷酸池消毒酶，它降解8-氧代-dGTP，从而防止其掺入DNA。在这种情况下，我们已经对鱼类病原体鲑鱼Aliivibrio salicida（AsMutT）和人类病原体霍乱弧菌（VcMutT）的MutT进行了比较生化和结构分析，以分析其作为核苷酸消毒酶的功能并确定可能的感冒-调整后的AsMutT属性。生化特征表明，两种酶都对8-oxo-dGTP底物具有活性，并且在所有研究温度下，AsMutT的催化效率均高于VcMutT。基于生化数据的计算还显示，与VcMutT相比，AsMutT的活化能（E“ a）低，差示扫描量热法实验表明，AsMutT的熔化温度（T” m）值比VcMutT高。对VcMutT的晶体结构进行比较分析（确定为2.42A分辨率）和AsMutT的同源性模型表明，VcMutT环中的三个独特的Gly残基以及AsMutT中的其他长距离离子对可以解释其温度稳定性的差异。两种酶。我们得出结论，与嗜温VcMutT相比，AsMutT是一种稳定的冷活性酶，具有高催化效率和降低的E“ a。

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