NosA catalyzing carboxyl-terminal amide formation in nosiheptide maturation via an enamine dealkylation on the serine-extended precursor peptide.

Yi Yu, Heng Guo, Qi Zhang, Lian Duan, Ying Ding, Rijing Liao, Chun Lei, Ben Shen, Wen Liu

State Key Laboratory of Bioorganic and Natural Products Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, 345 Lingling Road, Shanghai 200032, China.

Journal of the American Chemical Society 2010 Nov 24

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The carboxyl-terminal amide group has been often found in many bioactive peptide natural products, including nosiheptide belonging to the over 80 entity-containing thiopeptide family. Upon functional characterization of a novel protein NosA in nosiheptide bios ynthesis, herein we report an unusual C-terminal amide forming strategy in general for maturating certain amide-terminated thiopeptides by processing their precursor peptides featuring a serine extension. NosA acts on an intermediate bearing a bis-dehydroalanine tail and catalyzes an enamide dealkylation to remove the acrylate unit originating from the extended serine residue.

Citation

Yi Yu, Heng Guo, Qi Zhang, Lian Duan, Ying Ding, Rijing Liao, Chun Lei, Ben Shen, Wen Liu. NosA catalyzing carboxyl-terminal amide formation in nosiheptide maturation via an enamine dealkylation on the serine-extended precursor peptide. Journal of the American Chemical Society. 2010 Nov 24;132(46):16324-6