Isolation, Structure Elucidation, and Biosynthesis of a Cysteate-Containing Nonribosomal Peptide in Streptomyces lincolnensis

Min Wang; Dandan Chen; Qunfei Zhao; Wen Liu

doi:10.1021/acs.joc.8b00044

Isolation, Structure Elucidation, and Biosynthesis of a Cysteate-Containing Nonribosomal Peptide in Streptomyces lincolnensis

The Journal of Organic Chemistry ◽

10.1021/acs.joc.8b00044 ◽

2018 ◽

Vol 83 (13) ◽

pp. 7102-7108 ◽

Cited By ~ 5

Author(s):

Min Wang ◽

Dandan Chen ◽

Qunfei Zhao ◽

Wen Liu

Keyword(s):

Structure Elucidation ◽

Nonribosomal Peptide ◽

Streptomyces Lincolnensis

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Structure elucidation and biosynthesis of fuscachelins, peptide siderophores from the moderate thermophileThermobifida fusca

Proceedings of the National Academy of Sciences ◽

10.1073/pnas.0805451105 ◽

2008 ◽

Vol 105 (40) ◽

pp. 15311-15316 ◽

Cited By ~ 48

Author(s):

Eric J. Dimise ◽

Paul F. Widboom ◽

Steven D. Bruner

Keyword(s):

Natural Products ◽

Natural Product ◽

Gene Cluster ◽

Structure Elucidation ◽

Biochemical Characterization ◽

Gene Clusters ◽

Biologically Active ◽

Biosynthetic Gene ◽

Nonribosomal Peptide

Bacteria belonging to the order Actinomycetales have proven to be an important source of biologically active and often therapeutically useful natural products. The characterization of orphan biosynthetic gene clusters is an emerging and valuable approach to the discovery of novel small molecules. Analysis of the recently sequenced genome of the thermophilic actinomyceteThermobifida fuscarevealed an orphan nonribosomal peptide biosynthetic gene cluster coding for an unknown siderophore natural product.T. fuscais a model organism for the study of thermostable cellulases and is a major degrader of plant cell walls. Here, we report the isolation and structure elucidation of the fuscachelins, siderophore natural products produced byT. fusca. In addition, we report the purification and biochemical characterization of the termination module of the nonribosomal peptide synthetase. Biochemical analysis of adenylation domain specificity supports the assignment of this gene cluster as the producer of the fuscachelin siderophores. The proposed nonribosomal peptide biosynthetic pathway exhibits several atypical features, including a macrocyclizing thioesterase that produces a 10-membered cyclic depsipeptide and a nonlinear assembly line, resulting in the unique heterodimeric architecture of the siderophore natural product.

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Structure Elucidation and Activity of Kolossin A, theD-/L-Pentadecapeptide Product of a Giant Nonribosomal Peptide Synthetase

Angewandte Chemie International Edition ◽

10.1002/anie.201502835 ◽

2015 ◽

Vol 54 (35) ◽

pp. 10352-10355 ◽

Cited By ~ 35

Author(s):

Helge B. Bode ◽

Alexander O. Brachmann ◽

Kirtikumar B. Jadhav ◽

Lydia Seyfarth ◽

Christina Dauth ◽

...

Keyword(s):

Structure Elucidation ◽

Nonribosomal Peptide Synthetase ◽

Nonribosomal Peptide ◽

Peptide Synthetase

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Structure elucidation of the syringafactin lipopeptides provides insight in the evolution of nonribosomal peptide synthetases

Chemical Science ◽

10.1039/c9sc03633d ◽

2019 ◽

Vol 10 (48) ◽

pp. 10979-10990 ◽

Cited By ~ 5

Author(s):

Sebastian Götze ◽

Johannes Arp ◽

Gerald Lackner ◽

Shuaibing Zhang ◽

Hajo Kries ◽

...

Keyword(s):

Structure Elucidation ◽

Nonribosomal Peptides ◽

Biosynthetic Genes ◽

Nonribosomal Peptide ◽

Nonribosomal Peptide Synthetases ◽

Peptide Synthetases

A snapshot of evolution in flagrante shows that recombination within and between biosynthetic genes leads to diversification of nonribosomal peptides.

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