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Medicinal-Pharmaceutical Chemistry Commons

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Ronald Cerny Publications

2012

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Full-Text Articles in Medicinal-Pharmaceutical Chemistry

Unusual Activities Of The Thioesterase Domain For The Biosynthesis Of The Polycyclic Tetramate Macrolactam Hsaf In Lysobacter Enzymogenes C3, Lili Lou, Haotong Chen, Ronald Cerny, Yaoyao Li, Yuemao Shen, Liangcheng Du Jan 2012

Unusual Activities Of The Thioesterase Domain For The Biosynthesis Of The Polycyclic Tetramate Macrolactam Hsaf In Lysobacter Enzymogenes C3, Lili Lou, Haotong Chen, Ronald Cerny, Yaoyao Li, Yuemao Shen, Liangcheng Du

Ronald Cerny Publications

HSAF is an antifungal natural product with a new mode of action. A rare bacterial iterative PKSNRPS assembles the HSAF skeleton. The biochemical characterization of the NRPS revealed that the thioesterase (TE) domain possesses the activities of both a protease and a peptide ligase. Active site mutagenesis, circular dichroism spectra and homology modeling of the TE structure suggested that the TE may possess uncommon features that may lead to the unusual activities. The iterative PKS-NRPS is found in all polycyclic tetramate macrolactam gene clusters, and the unusual activities of the TE may be common to this type of hybrid PKS-NRPS.