Characterization of three amidinotransferases involved in the biosynthesis of ketomemicins
Characterization of three amidinotransferases involved in the biosynthesis of ketomemicins
复制标题
参与酮霉素生物合成的三种脒基转移酶的表征
DOI：
10.1016/j.bmcl.2016.05.090
复制
发表时间：
2016
期刊：
影响因子：
--
通讯作者：
and T. Dairi
中科院分区：
文献类型：
--
作者：
Y. Ogasawara;M. Fujimori;J. Kawata;and T. Dairi
我们最近报道了一类新的酰胺键形成酶（肽连接酶）参与的生物合成的pheganomycins，resorcinomycins和ketomemicins。这类酶专门利用N α-脒基氨基酸作为N-末端底物。在这封信中，我们表征了三种新的参与酮霉素生物合成的脒基转移酶，并表明L-精氨酸是小单孢菌和原链霉菌簇中脒基转移酶的脒基受体，而热带盐孢菌酶识别L-缬氨酸。出乎意料的是，S Tropicaenzyme接受几种不同的氨基酸作为除甲苯-缬氨酸之外的脒基受体。因此，我们重新研究了由S基因簇控制的特定代谢产物。tropica和确定了几个次要的同系物酮霉素C与不同的N-末端脒基氨基酸。这些结果表明，S.热带植物是混杂的，并且可用于产生新的酮霉素型天然产物。
We recently reported a novel class of amide bond forming enzymes (peptide ligases) involved in the biosynthesis of pheganomycins, resorcinomycins and ketomemicins. This class of enzymes exclusively utilizesNα-amidino amino acids as the N-terminal substrate. In this Letter, we characterized three new amidinotransferases involved in the biosynthesis of ketomemicins and showed thatl-arginine was the amidino-acceptor of amidinotransferases in both the Micromonospora sp. and Streptomycesmobaraensisclusters, while theSalinispora tropicaenzyme recognizedl-valine. Unexpectedly, theS. tropicaenzyme accepted several different amino acids as amidino acceptors in addition tol-valine. Accordingly, we re-investigated the specific metabolites governed by the gene cluster ofS. tropicaand identified several minor congeners of ketomemicin C with different N-terminal amidino-amino acids. These results indicate that the amidinotransferase ofS. tropicais promiscuous and could be useful to generate new ketomemicin-type natural products.