Peptide Macrocyclization: The Reductase of the Nostocyclopeptide Synthetase Triggers the Self-Assembly of a Macrocyclic Imine

详细信息    查看全文

• 作者：Florian Kopp ; Christoph Mahlert ; Jan Grü ; newald ; Mohamed A. Marahiel
• 刊名：Journal of the American Chemical Society
• 出版年：2006
• 出版时间：December 27, 2006
• 年：2006
• 卷：128
• 期：51
• 页码：16478 - 16479
• 全文大小：370K
• 年卷期：v.128,no.51(December 27, 2006)
• ISSN：1520-5126

文摘

Many biologically active natural products have macrocyclic structures. In nonribosomal peptides macrocyclization is commonly achieved via the formation of intramolecular ester or amide bond catalyzed by thioesterase domains during biosynthesis. A unique and so far unknown type of peptide cyclization occurs in the nostocyclopeptide, a macrocyclic imine produced by the terrestrial cyanobacterium Nostoc sp. ATCC53789. In this work we show that a C-terminal reductase domain of the nostocyclopeptide nonribosomal peptide synthetase catalyzes the reductive release of a linear peptide aldehyde and thereby triggers the spontaneous formation of a stable imino head-to-tail linkage. This type of molecular self-assembly induced by the reductive release of reactive aldehydes may be more commonplace in other complex nonribosomal peptides than originally thought.