Izumikawa Miho, Cheng Qian, Moore Bradley S
College of Pharmacy, University of Arizona, Tucson, Arizona 85721, USA.
J Am Chem Soc. 2006 Feb 8;128(5):1428-9. doi: 10.1021/ja0559707.
Benzoic acid priming of the enterocin and actinorhodin type II polyketide synthase complexes was accomplished in vitro via an unprecedented type II nonribosomal peptide synthetase-like mechanism involving the benzoate:acyl carrier protein (ACP) ligase EncN and the ACP EncC. The transfer of the aryl acid to the ACP is ATP-dependent, yet coenzyme A-independent, as characterized with radiolabeled substrates and protein mass spectrometry. Subsequent transport of the ACP-bound aryl group to the native enterocin and the aberrant actinorhodin ketosynthase chain length factor heterodimers was further demonstrated, thereby demonstrating the potential of this biocatalyst for engineering diverse aryl-primed aromatic polyketide agents.
通过一种前所未有的II型非核糖体肽合成酶样机制，在体外实现了对肠球菌素和放线紫红素II型聚酮合酶复合物的苯甲酸引发，该机制涉及苯甲酸：酰基载体蛋白（ACP）连接酶EncN和ACP EncC。正如用放射性标记底物和蛋白质质谱法所表征的那样，芳酸向ACP的转移是ATP依赖性的，但不依赖辅酶A。进一步证明了与ACP结合的芳基随后向天然肠球菌素和异常的放线紫红素酮合成酶链长因子异二聚体的转移，从而证明了这种生物催化剂用于工程化多种芳基引发的芳香族聚酮化合物的潜力。
