来自嗜冷细菌丁香假单胞菌的冷活性热不稳定 tRNA 修饰 GTPase（Lz4W）。
A cold-active heat-labile t-RNA modification GTPase from a psychrophilic bacterium Pseudomonas syringae (Lz4W).
机构信息
Centre for Cellular and Molecular Biology, Uppal Road, Hyderabad 500 007, India.
出版信息
Res Microbiol. 2010 Jan-Feb;161(1):46-50. doi: 10.1016/j.resmic.2009.11.002. Epub 2009 Nov 24.
A cold-active heat-labile t-RNA modification GTPase (TrmE) from psychrophilic bacterium Pseudomonas syringae (Lz4W) has been purified and characterized. The purified TrmE is a 53 kDa protein, has GTPase activity and hydrolyses only the oxy and deoxy forms of GTP but not the other nucleotide triphosphates. The enzyme exhibits optimal activity at 12-18 degrees C and retains 65% of its optimal activity at 4 degrees C, indicating that it is a cold-active enzyme. The enzyme is also heat-labile and loses 60% of its activity at 30 degrees C. This is the first report on the purification and characterization of a TrmE from a psychrophilic bacterium.
已从嗜冷菌丁香假单胞菌（Lz4W）中纯化并鉴定了一种冷活性热不稳定 tRNA 修饰 GTP 酶（TrmE）。纯化的 TrmE 是一种 53kDa 的蛋白质，具有 GTPase 活性，仅水解氧和脱氧 GTP，但不水解其他核苷酸三磷酸。该酶在 12-18°C 时表现出最佳活性，在 4°C 时保留其最佳活性的 65%，表明其是一种冷活性酶。该酶也不稳定，在 30°C 时失活 60%。这是首次从嗜冷菌中纯化和鉴定 TrmE。
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