Cobb Steven L, Deng Hai, McEwan Andrew R, Naismith James H, O'Hagan David, Robinson David A
School of Chemistry, Centre for Biomolecular Sciences, University of St Andrews, Purdie Building, North Haugh, St Andrews, KY16 9ST, UK.
Org Biomol Chem. 2006 Apr 21;4(8):1458-60. doi: 10.1039/b600574h. Epub 2006 Mar 8.
The fluorinase enzyme from Streptomyces cattleya displays an unusual ability in biocatalysis in that it forms a C-F bond. We now report that the enzyme will accept 2'-deoxyadenosine in place of adenosine substrates, and structural evidence reveals a reorganisation in hydrogen bonding to accommodate this substrate series. It emerges from this study that the enzyme does not require a planar ribose conformation of the substrate to catalyse C-F bond formation.
来自卡特利链霉菌的氟化酶在生物催化方面展现出一种不同寻常的能力，即它能形成碳氟键。我们现在报告该酶能够接受2'-脱氧腺苷来替代腺苷底物，并且结构证据显示氢键发生了重新排列以适应这一底物系列。从这项研究中可以看出，该酶在催化碳氟键形成时并不需要底物具有平面核糖构象。
