Expression and characterization of the terminal heme synthetic enzymes from the hyperthermophile Aquifex aeolicus.
Expression and characterization of the terminal heme synthetic enzymes from the hyperthermophile Aquifex aeolicus.
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超嗜热菌 Aquifex aeolicus 末端血红素合成酶的表达和表征。
DOI：
10.1111/j.1574-6968.2001.tb10789.x
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发表时间：
2001
影响因子：
2.1
通讯作者：
Dailey,HA
中科院分区：
文献类型：
--
作者：
Wang,KF;Dailey,TA;Dailey,HA
超嗜热菌Aquifex aeolicus血红素生物合成途径的两个末端酶原卟啉原氧化酶和亚铁螯合酶在大肠杆菌中得到表达、纯化并进行了生化表征。该菌的铁螯合酶和原卟啉原氧化酶都是单体，与枯草芽孢杆菌的相应酶一样。但与B。subtilisproteins，博塔.酵母酶是膜相关的。两种蛋白质的最适温度均超过60°C。这是在极端嗜热细菌中功能性血红素生物合成酶的第一个证明。
The terminal two heme biosynthetic pathway enzymes, protoporphyrinogen oxidase and ferrochelatase, of the hyperthermophilic bacteriumAquifex aeolicushave been expressed inEscherichia coli, purified to homogeneity, and biochemically characterized. Ferrochelatase and protoporphyrinogen oxidase of this organism are both monomeric, as was found for the corresponding enzymes ofBacillus subtilis. However, unlike theB. subtilisproteins, bothA. aeolicusenzymes are membrane-associated. Both proteins have temperature optima over 60°C. This is the first demonstration of functional heme biosynthetic enzymes in an extreme thermophilic bacterium.