CAS Key Laboratory of Tropical Marine Bio-resources and Ecology, Guangdong Key Laboratory of Marine Materia Medica, RNAM Center for Marine Microbiology, South China Sea Institute of Oceanology, Chinese Academy of Sciences , 164 West Xingang Road, Guangzhou 510301, China.
Org Lett. 2015 Feb 6;17(3):628-31. doi: 10.1021/ol5036497. Epub 2015 Jan 26.
Bioinformatic analyses indicate that TrdC, SlgL, LipX2, KirHI, and FacHI belong to a group of highly homologous proteins involved in biosynthesis of actinomycete-derived tirandamycin B, streptolydigin, α-lipomycin, kirromycin, and factumycin, respectively. However, assignment of their biosynthetic roles has remained elusive. Gene inactivation and complementation, in vitro biochemical assays with synthetic analogues, point mutations, and phylogenetic tree analyses reveal that these proteins represent a new family of Dieckmann cyclases that drive tetramic acid and pyridone scaffold biosynthesis.
生物信息学分析表明,TrdC、SgL、LipX2、KirHI 和 FacHI 分别属于参与放线菌来源的 tirandamycin B、streptolydigin、α-lipomycin、kirromycin 和 factumycin 生物合成的一组高度同源蛋白。然而,它们的生物合成作用仍未确定。基因失活和互补、用合成类似物进行体外生化分析、点突变和系统发育树分析表明,这些蛋白代表了一种新的狄克曼环化酶家族,它们驱动四氢酸和吡啶酮支架的生物合成。