Constant pH Accelerated Molecular Dynamics Investigation of the pH Regulation Mechanism of Dinoflagellate Luciferase
Constant pH Accelerated Molecular Dynamics Investigation of the pH Regulation Mechanism of Dinoflagellate Luciferase
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DOI：
10.1021/acs.biochem.7b00873
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发表时间：
2018-01-23
期刊：
影响因子：
2.9
通讯作者：
Mansoorabadi, Steven O.
中科院分区：
文献类型：
--
作者：
Donnan, Patrick H.;Ngo, Phong D.;Mansoorabadi, Steven O.
甲藻中的生物发光反应涉及甲藻荧光素酶（LCF）对开链四吡咯的氧化。LCF的活性受pH值（约8）的严格调节，其中该酶在pH值（约6）时基本上无活性，在pH值（约8）时最佳活性LCF的机制或活性形式的结构知之甚少，尽管有人提出N-末端区域的几个分子内保守的组氨酸残基对pH值调节机制很重要。在这里，恒定pH加速的分子动力学被用来深入了解酸化诱导的LCF的构象激活。
The bioluminescence reaction in dinoflagellates involves the oxidation of an open-chain tetrapyrrole by the enzyme dinoflagellate luciferase (LCF). The activity of LCF is tightly regulated by pH similar to 8, where the enzyme is essentially inactive at pH similar to 6 and optimally active at pH Little is known about the mechanism of LCF or the structure of :the active form of the enzyme although it has been proposed that several intramolecularly conserved histidine residues in the N-terminal region are important for the pH regulation mechanism. Here, constant pH accelerated molecular dynamics was employed to gain insight into the conformational activation of LCF induced by acidification.