Structural insights into the catalytic mechanism of aldehyde-deformylating oxygenases.
Structural insights into the catalytic mechanism of aldehyde-deformylating oxygenases.
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醛脱甲酰加氧酶催化机制的结构见解
DOI：
10.1007/s13238-014-0108-2
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发表时间：
2015-01
期刊：
影响因子：
21.1
通讯作者：
Chang, Wenrui
中科院分区：
文献类型：
--
作者：
Jia, Chenjun;Li, Mei;Li, Jianjun;Zhang, Jingjing;Zhang, Hongmei;Cao, Peng;Pan, Xiaowei;Lu, Xuefeng;Chang, Wenrui
关键词：
近年来，蓝藻中的脂肪烷（a/e）ne生物合成途径作为一种有前途的生物燃料生产途径受到了广泛关注。蓝藻脱羧脱甲酰加氧酶（cADO）是该途径中的关键酶，催化Cn脂肪醛转化为相应的Cn-1alk（a/e）ne。由于其低活性，通过cADO生产烷（a/e）ne是低效的方法。以前的生化和结构的cADO的调查提供了一些信息，其催化反应。然而，其催化过程的细节仍不清楚。在这里，我们报告五个晶体结构的cADO从聚球藻elongates菌株PCC 7942在其无铁和铁结合的形式，代表不同的状态，在其催化过程中。结构比较和功能酶分析表明，Glu 144，铁配位残基之一，在cADO的催化反应中起着至关重要的作用。此外，Glu 144所在的螺旋呈现出两种不同的构象，这与cADO结构中二铁中心的不同结合状态相关。因此，我们的研究结果提供了一个高度不稳定的功能cADO二铁中心，我们提出了与其低酶活性的结构解释。在我们的结构和生化数据的基础上，cADO的一个可能的催化过程，这可以帮助设计的cADO与提高活性。
The fatty alk(a/e)ne biosynthesis pathway found in cyanobacteria gained tremendous attention in recent years as a promising alternative approach for biofuel production. Cyanobacterial aldehyde-deformylating oxygenase (cADO), which catalyzes the conversion of Cnfatty aldehyde to its corresponding Cn-1alk(a/e)ne, is a key enzyme in that pathway. Due to its low activity, alk(a/e)ne production by cADO is an inefficient process. Previous biochemical and structural investigations of cADO have provided some information on its catalytic reaction. However, the details of its catalytic processes remain unclear. Here we report five crystal structures of cADO from theSynechococcus elongatesstrain PCC7942 in both its iron-free and iron-bound forms, representing different states during its catalytic process. Structural comparisons and functional enzyme assays indicate that Glu144, one of the iron-coordinating residues, plays a vital role in the catalytic reaction of cADO. Moreover, the helix where Glu144 resides exhibits two distinct conformations that correlates with the different binding states of the di-iron center in cADO structures. Therefore, our results provide a structural explanation for the highly labile feature of cADO di-iron center, which we proposed to be related to its low enzymatic activity. On the basis of our structural and biochemical data, a possible catalytic process of cADO was proposed, which could aid the design of cADO with improved activity.
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影响因子：
2.9
作者：
Li, Ning;Chang, Wei-chen;Bollinger, J. Martin, Jr.
通讯作者：
Bollinger, J. Martin, Jr.
DOI：
10.1107/s0907444909052925
发表时间：
2010-02
期刊：
Acta crystallographica. Section D, Biological crystallography
影响因子：
--
作者：
Adams PD;Afonine PV;Bunkóczi G;Chen VB;Davis IW;Echols N;Headd JJ;Hung LW;Kapral GJ;Grosse-Kunstleve RW;McCoy AJ;Moriarty NW;Oeffner R;Read RJ;Richardson DC;Richardson JS;Terwilliger TC;Zwart PH
通讯作者：
Zwart PH
通过非血红素铁依赖性蓝藻醛脱羰酶校正不依赖于氧的烷烃形成：动力学研究和外部电子供体的需求。
影响因子：
2.9
作者：
Eser BE;Das D;Han J;Jones PR;Marsh EN
通讯作者：
Marsh EN
影响因子：
7.8
作者：
Krebs, Carsten;Bollinger, J. Martin, Jr.;Booker, Squire J.
通讯作者：
Booker, Squire J.
影响因子：
6.8
作者：
Nordlund, P;Eklund, H
通讯作者：
Eklund, H