Structure of a bifunctional alcohol dehydrogenase involved in bioethanol generation in Geobacillus thermoglucosidasius
Structure of a bifunctional alcohol dehydrogenase involved in bioethanol generation in Geobacillus thermoglucosidasius
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DOI：
10.1107/s0907444913020349
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发表时间：
2013-10-01
影响因子：
2.2
通讯作者：
Danson, Michael J.
中科院分区：
文献类型：
--
作者：
Extance, Jonathan;Crennell, Susan J.;Danson, Michael J.
双功能醇/乙醛脱氢酶 (ADHE) 存在于许多发酵微生物中。它们通过醛中间体催化酰基辅酶 A 转化为醇；这与两个 NADH 分子的氧化相结合，以在发酵代谢过程中维持 NAD(+) 库。来自产乙醇的嗜热地芽孢杆菌热葡萄糖苷酶的 ADHE 蛋白的乙醇脱氢酶 (ADH) 结构域的结构已确定为 2.5 埃分辨率。这是针对此类域报告的第一个结构。已进行计算机建模以生成乙醛脱氢酶结构域的同源模型，随后将其与 ADH 结构域结构对接以模拟完整 ADHE 蛋白的结构。该模型首次提出了形成大型多聚体组装体或“螺体”的结构机制，这种机制是在这种 ADHE 蛋白中观察到的，并且之前已报道过来自其他生物体的 ADHE。
Bifunctional alcohol/aldehyde dehydrogenase (ADHE) enzymes are found within many fermentative microorganisms. They catalyse the conversion of an acyl-coenzyme A to an alcohol via an aldehyde intermediate; this is coupled to the oxidation of two NADH molecules to maintain the NAD(+) pool during fermentative metabolism. The structure of the alcohol dehydrogenase (ADH) domain of an ADHE protein from the ethanol-producing thermophile Geobacillus thermoglucosidasius has been determined to 2.5 angstrom resolution. This is the first structure to be reported for such a domain. In silico modelling has been carried out to generate a homology model of the aldehyde dehydrogenase domain, and this was subsequently docked with the ADH-domain structure to model the structure of the complete ADHE protein. This model suggests, for the first time, a structural mechanism for the formation of the large multimeric assemblies or 'spirosomes' that are observed for this ADHE protein and which have previously been reported for ADHEs from other organisms.