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首页> 外文期刊>Acta crystallographica. Section D, Biological crystallography. >Crystal structure and enzymatic properties of a broad substrate-specificity psychrophilic aminotransferase from the Antarctic soil bacterium Psychrobacter sp. B6
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Crystal structure and enzymatic properties of a broad substrate-specificity psychrophilic aminotransferase from the Antarctic soil bacterium Psychrobacter sp. B6

机译：晶体结构和酶的性质广泛的底物特异性好寒性的转氨酶从南极土壤细菌Psychrobacter sp。B6

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摘要

Aminotransferases (ATs) are enzymes that are commonly used in the chemical and pharmaceutical industries for the synthesis of natural and non-natural amino acids by transamination reactions. Currently, the easily accessible enzymes from mesophilic organisms are most commonly used; however, for economical and ecological reasons the utilization of aminotransferases from psychrophiles would be more advantageous, as their optimum reaction temperature is usually significantly lower than for the mesophilic ATs. Here, gene isolation, protein expression, purification, enzymatic properties and structural studies are reported for the cold-active aromatic amino-acid aminotransferase (PsyArAT) from Psychrobacter sp. B6, a psychrotrophic, Gram-negative strain from Antarctic soil. Preliminary computational analysis indicated dual functionality of the enzyme through the ability to utilize both aromatic amino acids and aspartate as substrates. This postulation was confirmed by enzymatic activity tests, which showed that it belonged to the class EC 2.6.1.57. The first crystal structures of a psychrophilic aromatic amino-acid aminotransferase have been determined at resolutions of 2.19?? for the native enzyme (PsyArAT) and 2.76?? for its complex with aspartic acid (PsyArAT/D). Both types of crystals grew in the monoclinic space group P21 under slightly different crystallization conditions. The PsyArAT crystals contained a dimer (90?kDa) in the asymmetric unit, which corresponds to the active form of this enzyme, whereas the crystals of the PsyArAT/D complex included four dimers showing different stages of the transamination reaction.
机译：转氨酶(ATs)是酶常用的化学和制药合成的自然和工业非天然的氨基酸通过转氨作用反应。从嗜中温微生物酶常用的;利用生态原因从它们将转氨酶更有利,因为他们的最佳反应通常温度明显低于嗜中温at。蛋白质表达、纯化、酶性质和结构的研究报道cold-active芳香族氨基酸从Psychrobacter sp转氨酶(PsyArAT)。psychrotrophic B6,革兰氏阴性菌株南极土壤。分析表明,双重的功能利用两个酶的能力芳香族氨基酸和天冬氨酸为底物。证实了这一假定酶活动测试,这表明它属于EC 2.6.1.57的类。好寒性的芳香族氨基酸的结构转氨酶就下定决心分辨率为2.19 ? ?(PsyArAT)和2.76 ? ?天冬氨酸(PsyArAT / D)。下的单斜P21空间群稍微不同的结晶条件。PsyArAT晶体包含一个二聚体(90 kDa ?)在不对称单位,对应这种酶的活性形式,而晶体PsyArAT / D复杂的包括四个二聚体显示不同阶段的转氨作用的反应。

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