体外重建参与 futalosine 衍生menaquinone 生物合成的自由基 S-腺苷甲硫氨酸酶 MqnC。
In vitro reconstitution of the radical S-adenosylmethionine enzyme MqnC involved in the biosynthesis of futalosine-derived menaquinone.
机构信息
Department of Chemistry, Texas A&M University , College Station, Texas 77842, United States.
出版信息
Biochemistry. 2013 Jul 9;52(27):4592-4. doi: 10.1021/bi400498d. Epub 2013 Jun 27.
Abstract
The radical S-adenosylmethionine enzyme MqnC catalyzes conversion of dehypoxanthine futalosine (DHFL) to the unique spiro compound cyclic DHFL in the futalosine pathway for menaquinone biosynthesis. This study describes the in vitro reconstitution of [4Fe-4S] cluster-dependent MqnC activity and identifies the site of abstraction of a hydrogen atom from DHFL by the adenosyl radical.
摘要
激进的 S-腺苷甲硫氨酸酶 MqnC 催化 dehypoxanthine futalosine (DHFL) 向 futalosine 途径中独特的螺环化合物环状 DHFL 的转化，用于menaquinone 生物合成。本研究描述了 [4Fe-4S] 簇依赖的 MqnC 活性的体外重建，并确定了腺苷自由基从 DHFL 中提取氢原子的位置。
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