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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Structure of an archaeal alanine:glyoxylate aminotransferase.
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Structure of an archaeal alanine:glyoxylate aminotransferase.

机译:古细菌丙氨酸的结构:乙醛酸转氨酶。

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摘要

The crystal structure of a novel alanine:glyoxylate aminotransferase from the hyperthermophilic archaeon Thermococcus litoralis was determined at 2.3 A resolution. The asymmetric unit contains four homologous subunits and the functional tetramer is generated by noncrystallographic 222 symmetry. Although the main-chain coordinates of the monomer of the Thermococcus litoralis enzyme showed a high degree of similarity to those of aspartate aminotransferase from Thermus thermophilus HB8, the amino-acid residues involved in substrate binding in the aspartate aminotransferase are only partially conserved in the Thermococcus litoralis enzyme. This may account for the difference in the substrate specificities of the two enzymes.
机译:一种新型的晶体结构丙氨酸:乙醛酸的转氨酶hyperthermophilic archaeon Thermococcus litoralis确定在2.3一项决议。不对称单元包含四个同源的子单元和功能四聚物生成222年noncrystallographic对称。主链的单体的坐标Thermococcus litoralis酶显示高相似度的天冬氨酸转氨酶从栖热菌属酸奶HB8,氨基酸残基参与底物绑定在天冬氨酸转氨酶只是部分Thermococcus守恒litoralis酶。不同的底物特异性两种酶。

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