Zheng Chang-Ji, Sohn Mi-Jin, Kim Won-Gon
Functional Metabolomics Research Center, Korea Research Institute of Bioscience and Biotechnology, Yusong, Daejeon 305-806, Republic of Korea.
J Antibiot (Tokyo). 2006 Dec;59(12):808-12. doi: 10.1038/ja.2006.108.
Two potent inhibitors of FabK, the enoyl-acyl carrier protein (ACP) reductase of Streptococcus pneumoniae, were isolated from the solid state fermentation of an unidentified fungus F010248. Their structures were identified to be atromentin and leucomelone by various spectral analysis. Atromentin and leucomelone inhibited the FabK with IC50 values of 0.24 and 1.57 microM, respectively, while did not inhibit FabI, the enoyl-ACP reductase of either Escherichia coli or Staphylococcus aureus, even at 200 microM. Atromentin and leucomelone are the first inhibitors specific to the enoyl-ACP reductase (FabK) of Streptococcus pneumoniae.
从一株未鉴定的真菌F010248的固态发酵产物中分离出两种有效的肺炎链球菌烯酰-酰基载体蛋白（ACP）还原酶FabK抑制剂。通过各种光谱分析确定它们的结构分别为紫铆茵素和白黑菌素。紫铆茵素和白黑菌素对FabK的抑制中浓度（IC50）值分别为0.24和1.57微摩尔，而即使在200微摩尔浓度下，它们对大肠杆菌或金黄色葡萄球菌的烯酰-ACP还原酶FabI也没有抑制作用。紫铆茵素和白黑菌素是肺炎链球菌烯酰-ACP还原酶（FabK）的首批特异性抑制剂。
