Efficient biocatalytic C–H bond oxidation: an engineered heme-thiolate peroxygenase from a thermostable cytochrome P450
作者:Alecia R. Gee、Isobella S. J. Stone、Tegan P. Stockdale、Tara L. Pukala、James J. De Voss、Stephen G. Bell
DOI:10.1039/d3cc04626e
日期:——
highly sought after reaction in chemical synthesis is the activation of unactivated carbon–hydrogen bonds. We demonstrate the hydroxylation of fatty acidsusing an engineered thermostable archaeal cytochrome P450 enzyme. By replacing a seven aminoacid section of the I-helix, the nicotinamide cofactor-dependent monooxygenase was converted into a hydrogen peroxide using peroxygenase, enabling the efficient
化学合成中备受追捧的反应是未活化的碳氢键的活化。我们使用工程化的热稳定古菌细胞色素 P450 酶演示了脂肪酸的羟基化。通过替换 I 螺旋的 7 个氨基酸部分,烟酰胺辅因子依赖性单加氧酶使用过加氧酶转化为过氧化氢,从而能够在室温至 90 °C 下对 C-H 键进行有效的生物催化氧化。
Method of inhibiting parasitic activity
申请人:WASHINGTON UNIVERSITY
公开号:EP0498783A2
公开(公告)日:1992-08-12
A method of inhibiting parasitic activity is disclosed in which the biosynthesis of the glycosyl phosphatidylinositol (GPI) anchor of said parasite is inhibited by incorporating into said GPI anchor an oxy-substituted fatty acid analog in place of myristate. The inhibitory compounds are C₁₃ and C₁₄ fatty acids or alkyl esters thereof in which a methylene group normally in carbon position 4 to 13 of said fatty acid is replaced with oxygen.