Enediyne antitumor antibiotic maduropeptin biosynthesis featuring a C-methyltransferase that acts on a CoA-tethered aromatic substrate

Authors :: Jianya Ling
Horsman, Geoffrey P.
Sheng-Xiong Huang
Yinggang Luo
Shuangjun Lin
Ben Shen
Source :: Journal of the American Chemical Society. Sept 15, 2010, Vol. 132 Issue 36, 12534-12536
Publication Year :: 2010
Abstract: The biosynthetic pathway for the 3,6-dimethylsalicylic acid moiety of the enediyne antitumor antibiotic maduropeptin (MDP) chromophore which is produced by Actinomadura madurae ATCC 39144 is described. The unique property of enzyme MdpB1 to C-methylate a CoA-tethered aromatic acid demonstrated its capability to activating a variety of salicylic acid analogues that could be applied to engineer MDP analogues.

Subjects :: Antimitotic agents -- Chemical properties
Antineoplastic agents -- Chemical properties
Chromophores -- Structure
Chromophores -- Chemical properties
Methylation -- Analysis
Methyltransferases -- Chemical properties
Salicylic acid -- Chemical properties
Chemistry

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