Wolff Murielle, Seemann Myriam, Tse Sum Bui Bernadette, Frapart Yves, Tritsch Denis, Garcia Estrabot Ana, Rodríguez-Concepción Manuel, Boronat Albert, Marquet Andrée, Rohmer Michel
Université Louis Pasteur, UMR CNRS 7123, Institut Le Bel, Strasbourg, France.
FEBS Lett. 2003 Apr 24;541(1-3):115-20. doi: 10.1016/s0014-5793(03)00317-x.
The last enzyme (LytB) of the methylerythritol phosphate pathway for isoprenoid biosynthesis catalyzes the reduction of (E)-4-hydroxy-3-methylbut-2-enyl diphosphate into isopentenyl diphosphate and dimethylallyl diphosphate. This enzyme possesses a dioxygen-sensitive [4Fe-4S] cluster. This prosthetic group was characterized in the Escherichia coli enzyme by UV/visible and electron paramagnetic resonance spectroscopy after reconstitution of the purified protein. Enzymatic activity required the presence of a reducing system such as flavodoxin/flavodoxin reductase/reduced nicotinamide adenine dinucleotide phosphate or the photoreduced deazaflavin radical.
用于类异戊二烯生物合成的甲基赤藓糖醇磷酸途径的最后一种酶（LytB）催化（E）-4-羟基-3-甲基丁-2-烯基二磷酸还原为异戊烯基二磷酸和二甲基烯丙基二磷酸。这种酶具有对双加氧敏感的[4Fe-4S]簇。在纯化的蛋白质重构后，通过紫外/可见光谱和电子顺磁共振光谱对大肠杆菌中的这种辅基进行了表征。酶活性需要存在诸如黄素氧还蛋白/黄素氧还蛋白还原酶/还原型烟酰胺腺嘌呤二核苷酸磷酸或光还原脱氮黄素自由基等还原系统。
