...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>International Journal of Molecular Sciences >Crystal Structure of a Putative Cytochrome P450 Alkane Hydroxylase (CYP153D17) from Sphingomonas sp. PAMC 26605 and Its Conformational Substrate Binding
【24h】

Crystal Structure of a Putative Cytochrome P450 Alkane Hydroxylase (CYP153D17) from Sphingomonas sp. PAMC 26605 and Its Conformational Substrate Binding

机译：鞘氨醇单胞菌（Sphingomonas sp。）推测的细胞色素P450烷烃羟化酶（CYP153D17）的晶体结构。 PAMC 26605及其构象底物结合

获取原文
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

Enzymatic alkane hydroxylation reactions are useful for producing pharmaceutical and agricultural chemical intermediates from hydrocarbons. Several cytochrome P450 enzymes catalyze the regio- and stereo-specific hydroxylation of alkanes. We evaluated the substrate binding of a putative CYP alkane hydroxylase (CYP153D17) from the bacterium Sphingomonas sp. PAMC 26605. Substrate affinities to C10–C12 n-alkanes and C10–C14 fatty acids with K d values varied from 0.42 to 0.59 μM. A longer alkane (C12) bound more strongly than a shorter alkane (C10), while shorter fatty acids (C10, capric acid; C12, lauric acid) bound more strongly than a longer fatty acid (C14, myristic acid). These data displayed a broad substrate specificity of CYP153D17, hence it was named as a putative CYP alkane hydroxylase. Moreover, the crystal structure of CYP153D17 was determined at 3.1 ? resolution. This is the first study to provide structural information for the CYP153D family. Structural analysis showed that a co-purified alkane-like compound bound near the active-site heme group. The alkane-like substrate is in the hydrophobic pocket containing Thr74, Met90, Ala175, Ile240, Leu241, Val244, Leu292, Met295, and Phe393. Comparison with other CYP structures suggested that conformational changes in the β1–β2, α3–α4, and α6–α7 connecting loop are important for incorporating the long hydrophobic alkane-like substrate. These results improve the understanding of the catalytic mechanism of CYP153D17 and provide valuable information for future protein engineering studies.
机译：酶链烷烃羟基化反应可用于从烃类生产医药和农业化学中间体。几种细胞色素P450酶催化烷烃的区域特异性和立体特异性羟基化。我们评估了从细菌鞘氨醇单胞菌属细菌推测的CYP烷烃羟化酶（CYP153D17）的底物结合。 PAMC 26605. K d值与C10-C12正构烷烃和C10-C14脂肪酸的亲和力在0.42至0.59μM之间变化。较长的烷烃（C12）比较短的烷烃（C10）结合更牢固，而较短的脂肪酸（C10，癸酸; C12，月桂酸）比较长的脂肪酸（C14，肉豆蔻酸）结合更牢固。这些数据显示CYP153D17具有广泛的底物特异性，因此将其命名为推定的CYP烷烃羟化酶。此外，CYP153D17的晶体结构确定为3.1≤α。解析度。这是第一项为CYP153D家族提供结构信息的研究。结构分析表明，共纯化的烷烃样化合物结合在活性部位血红素基团附近。烷烃样底物在含有Thr74，Met90，Ala175，Ile240，Leu241，Val244，Leu292，Met295和Phe393的疏水袋中。与其他CYP结构的比较表明，β1-β2，α3-α4和α6-α7连接环的构象变化对于掺入长疏水性烷烃样底物很重要。这些结果增进了对CYP153D17催化机理的理解，并为将来的蛋白质工程研究提供了有价值的信息。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号