Degradation and reconstruction of moenomycin A and derivatives: Dissecting the function of the isoprenoid chain
Degradation and reconstruction of moenomycin A and derivatives: Dissecting the function of the isoprenoid chain
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DOI：
10.1021/ja065905c
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发表时间：
2006-11-01
影响因子：
15
通讯作者：
Kahne, Daniel E.
中科院分区：
文献类型：
--
作者：
Adachi, Masaatsu;Zhang, Yi;Kahne, Daniel E.
Moenomycin A is the only known natural product that inhibits peptidoglycan biosynthesis by binding the bacterial transglycosylases. We describe a degradation/reconstruction route to manipulate the reducing end of moenomycin A. A comparison of the biological and enzyme inhibitory activity of moenomycin A and an analogue containing a nerol lipid in place of the natural C25lipid chain provides insight into the role of the moenocinol unit. Our results show that a lipid chain having ten carbons in moenocinol is sufficient for enzyme inhibition, but a longer chain is required for biological acitivity, apparently because the molecule must partition into biological membranes to reach its target in bacterial cells.
