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

Research output: Contribution to journalArticle

31 Citations (Scopus)

Abstract

HSAF is an antifungal natural product with a new mode of action. A rare bacterial iterative PKS-NRPS 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 PKSNRPS 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.

Original languageEnglish (US)
Pages (from-to)4-6
Number of pages3
JournalBiochemistry
Volume51
Issue number1
DOIs
StatePublished - Jan 10 2012

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Lysobacter
Mutagenesis
Biosynthesis
Ligases
Multigene Family
Circular Dichroism
Biological Products
Skeleton
Catalytic Domain
Peptide Hydrolases
Genes
Peptides

ASJC Scopus subject areas

  • Biochemistry

Cite this

Unusual activities of the thioesterase domain for the biosynthesis of the polycyclic tetramate macrolactam HSAF in lysobacter enzymogenes C3. / Lou, Lili; Chen, Haotong; Cerny, Ronald; Li, Yaoyao; Shen, Yuemao; Du, Liangcheng.

In: Biochemistry, Vol. 51, No. 1, 10.01.2012, p. 4-6.

Research output: Contribution to journalArticle

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