来自棒状杆菌属U-96的异源四聚体肌氨酸氧化酶的晶体结构
Crystal structure of heterotetrameric sarcosine oxidase from Corynebacterium sp. U-96.
作者信息
Ida Koh, Moriguchi Tomotaka, Suzuki Haruo
机构信息
Department of Biosciences, School of Science, Kitasato University, 1-15-1 Kitasato, Sagamihara, Kanagawa 228-8555, Japan.
出版信息
Biochem Biophys Res Commun. 2005 Jul 29;333(2):359-66. doi: 10.1016/j.bbrc.2005.05.116.
Sarcosine oxidase from Corynebacterium sp. U-96 is a heterotetrameric enzyme. Here we report the crystal structures of the enzyme in complex with dimethylglycine and folinic acid. The alpha subunit is composed of two domains, contains NAD(+), and binds folinic acid. The beta subunit contains dimethylglycine, FAD, and FMN, and these flavins are approximately 10A apart. The gamma subunit is in contact with two domains of alpha subunit and has possibly a folate-binding structure. The delta subunit contains a single atom of zinc and has a Cys(3)His zinc finger structure. Based on the structures determined and on the previous works, the structure-function relationship on the heterotetrameric sarcosine oxidase is discussed.
来自棒状杆菌属U-96的肌氨酸氧化酶是一种异源四聚体酶。在此我们报告该酶与二甲基甘氨酸和亚叶酸复合物的晶体结构。α亚基由两个结构域组成，含有NAD(+)，并结合亚叶酸。β亚基含有二甲基甘氨酸、FAD和FMN，这些黄素相距约10埃。γ亚基与α亚基的两个结构域接触，可能具有叶酸结合结构。δ亚基含有单个锌原子，具有Cys(3)His锌指结构。基于所确定的结构以及先前的研究工作，对异源四聚体肌氨酸氧化酶的结构-功能关系进行了讨论。
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