...
  • 主题
高级搜索  >
历史搜索 清空历史
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
【24h】

Crystal structure and enzymatic properties of a broad substrate-specificity psychrophilic aminotransferase from the Antarctic soil bacterium Psychrobacter sp B6

机译：南极土壤细菌Psychrobacter sp B6的广泛底物特异性嗜热氨基转移酶的晶体结构和酶学性质。

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

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 aminoacid aminotransferase have been determined at resolutions of 2.19 angstrom for the native enzyme (PsyArAT) and 2.76 angstrom for its complex with aspartic acid (PsyArAT/D). Both types of crystals grew in the monoclinic space group P2(1) 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：氨基转移酶（ATs）是化学和制药行业中通常用于通过氨基转移反应合成天然和非天然氨基酸的酶。当前，最常用的是嗜温生物容易获得的酶。然而，出于经济和生态方面的原因，利用嗜冷菌的氨基转移酶将更为有利，因为它们的最佳反应温度通常明显低于嗜温ATs。在这里，报道了来自Psychrobacter sp。的冷活性芳香族氨基酸氨基转移酶（PsyArAT）的基因分离，蛋白质表达，纯化，酶学性质和结构研究。 B6，来自南极土壤的一种精神营养性革兰氏阴性菌株。初步的计算分析表明，该酶具有利用芳香族氨基酸和天冬氨酸作为底物的双重功能。酶活性测试证实了这种假设，表明它属于EC 2.6.1.57类。嗜冷芳香族氨基酸氨基转移酶的第一个晶体结构已确定为天然酶（PsyArAT）的分辨率为2.19埃，与天冬氨酸的复合物（PsyArAT / D）的分辨率为2.76埃。在稍微不同的结晶条件下，两种类型的晶体都生长在单斜晶空间群P2（1）中。 PsyArAT晶体在不对称单元中包含一个二聚体（90 kDa），与该酶的活性形式相对应，而PsyArAT / D复合物的晶体包含四个显示转氨反应不同阶段的二聚体。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号