发现嗜热古菌（Sulfolobus solfataricus）中存在一种假定的乙酰丙酮脱氢酶复合物。
Discovery of a putative acetoin dehydrogenase complex in the hyperthermophilic archaeon Sulfolobus solfataricus.
机构信息
Centre for Extremophile Research, Department of Biology and Biochemistry, University of Bath, Bath, UK.
出版信息
FEBS Lett. 2010 Mar 19;584(6):1231-4. doi: 10.1016/j.febslet.2010.02.037. Epub 2010 Feb 18.
Like many other aerobic archaea, the hyperthermophile Sulfolobus solfataricus possesses a gene cluster encoding components of a putative 2-oxoacid dehydrogenase complex. In the current paper, we have cloned and expressed the first two genes of this cluster and demonstrate that the protein products form an alpha(2)beta(2) hetero-tetramer possessing the catalytic activity characteristic of the first component enzyme of an acetoin dehydrogenase multienzyme complex. This represents the first report of an acetoin multienzyme complex in archaea, and contrasts with the branched-chain 2-oxoacid dehydrogenase complex activities characterised in two other archaea, Thermoplasma acidophilum and Haloferax volcanii.
与许多其他需氧古菌一样，高温喜热菌（Sulfolobus solfataricus）拥有一个基因簇，编码一个假定的 2-氧代酸脱氢酶复合物的组成部分。在本论文中，我们克隆并表达了这个基因簇的前两个基因，并证明其蛋白质产物形成一个具有丙酮醛脱氢酶多酶复合物第一组成酶特征的催化活性的 α(2)β(2)异源四聚体。这是古菌中首次报道的丙酮醛多酶复合物，与在另外两种古菌——嗜酸热原体（Thermoplasma acidophilum）和沃氏嗜盐菌（Haloferax volcanii）中鉴定的支链 2-氧代酸脱氢酶复合物活性形成对比。
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