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首页> 外文期刊>Applied Microbiology >X-Ray Structure of the Amidase Domain of AtzF, the Allophanate Hydrolase from the Cyanuric Acid-Mineralizing Multienzyme Complex
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X-Ray Structure of the Amidase Domain of AtzF, the Allophanate Hydrolase from the Cyanuric Acid-Mineralizing Multienzyme Complex

机译：氰尿酸矿化多酶复合物脲基甲酸酯水解酶AtzF酰胺酶结构域的X射线结构

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摘要

The activity of the allophanate hydrolase from Pseudomonas sp. strain ADP, AtzF, provides the final hydrolytic step for the mineralization of s -triazines, such as atrazine and cyanuric acid. Indeed, the action of AtzF provides metabolic access to two of the three nitrogens in each triazine ring. The X-ray structure of the N-terminal amidase domain of AtzF reveals that it is highly homologous to allophanate hydrolases involved in a different catabolic process in other organisms (i.e., the mineralization of urea). The smaller C-terminal domain does not appear to have a physiologically relevant catalytic function, as reported for the allophanate hydrolase of Kluyveromyces lactis , when purified enzyme was tested in vitro . However, the C-terminal domain does have a function in coordinating the quaternary structure of AtzF. Interestingly, we also show that AtzF forms a large, ca. 660-kDa, multienzyme complex with AtzD and AtzE that is capable of mineralizing cyanuric acid. The function of this complex may be to channel substrates from one active site to the next, effectively protecting unstable metabolites, such as allophanate, from solvent-mediated decarboxylation to a dead-end metabolic product.
机译：假单胞菌属的脲基甲酸酯水解酶的活性。 ADP菌株AtzF为s-三嗪（如阿特拉津和氰尿酸）的矿化提供了最后的水解步骤。实际上，AtzF的作用提供了对每个三嗪环中三个氮中的两个氮的代谢通道。 AtzF的N末端酰胺酶结构域的X射线结构表明，它与参与其他生物体不同分解代谢过程（即尿素矿化）的脲基甲酸酯水解酶高度同源。如对乳酸克鲁维酵母的脲基甲酸酯水解酶报道的那样，当体外测试纯化的酶时，较小的C末端域似乎没有生理相关的催化功能。但是，C末端域确实具有协调AtzF的四级结构的功能。有趣的是，我们还显示AtzF形成一个大的ca。具有AtzD和AtzE的660 kDa多酶复合物，能够使氰尿酸矿化。该复合物的功能可能是将底物从一个活性位点引导至另一个活性位点，从而有效地保护不稳定的代谢产物（如脲基甲酸酯）免受溶剂介导的脱羧作用直至最终代谢产物。

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