Enzymatic activity of the blue light‐regulated phosphodiesterase BlrP1 from Klebsiella pneumoniae shows a nonlinear dependence on light intensity
Enzymatic activity of the blue light‐regulated phosphodiesterase BlrP1 from Klebsiella pneumoniae shows a nonlinear dependence on light intensity
复制标题
肺炎克雷伯菌蓝光调节磷酸二酯酶 BlrP1 的酶活性显示出对光强度的非线性依赖性
DOI：
10.1002/1873-3468.14073
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发表时间：
2021
期刊：
影响因子：
3.5
通讯作者：
Terazima Masahide
中科院分区：
文献类型：
--
作者：
Shibata Kosei;Nakasone Yusuke;Terazima Masahide
来自肺炎克雷伯菌的蓝光调节磷酸二酯酶 BlrP1 以蓝光依赖性方式水解环状二聚单磷酸鸟苷 (GMP)。它包含一个光传感 BLUF 结构域和一个功能性 EAL 结构域。此前，据报道，只有当二聚体的两个原聚体都被激发时，二聚体在光照射下才会发生构象变化。基于这一观察，有人提出 BlrP1 可能是一种非线性光强度传感器。为了测试这一点，这里通过同时监测反应速率和fred来测量水解反应的周转数（kcat）和激发蛋白的分数（fred）之间的相关性。我们的结果表明 kcat 与 Fred2 成正比。因此，BlrP1 作为非线性光强度传感器来感知强光环境。
The blue light‐regulated phosphodiesterase BlrP1 fromKlebsiella pneumoniaehydrolyzes cyclic dimeric guanosine monophosphate (GMP) in a blue light‐dependent manner. It contains a photosensing BLUF domain and a functional EAL domain. Previously, it was reported that conformational changes in the dimer upon light illumination occurred only when both protomers of the dimer were excited. Based on this observation, it was proposed that BlrP1 might be a nonlinear light intensity sensor. To test this, here, the correlation between the turnover number of the hydrolysis reaction (kcat) and the fraction of the excited protein (fred) was measured by simultaneously monitoring the reaction rate andfred. Our results show thatkcatis proportional tofred2. Thus, BlrP1 works as a nonlinear light intensity sensor to sense a strong light environment.