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

2019 ◽  
Vol 10 (48) ◽  
pp. 10979-10990 ◽  
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.

Optimizing dimodular nonribosomal peptide synthetases and natural dipeptides in an Escherichia coli heterologous host

2013 ◽  
Vol 91 (4) ◽  
pp. 203-208 ◽  
Author(s):  
Morgan A. Wyatt ◽  
Nathan A. Magarvey
Keyword(s):  
Escherichia Coli ◽  
Biological Activities ◽  
Structural Complexity ◽  
Biosynthetic Gene Cluster ◽  
Nonribosomal Peptides ◽  
Heterologous Host ◽  
T7 Promoter ◽  
Nonribosomal Peptide ◽  
Nonribosomal Peptide Synthetases ◽  
Peptide Synthetases

Nonribosomal peptides are an important class of natural products that have a broad range of biological activities. Their structural complexity often prevents simple chemical synthesis, and production from the natural producer is often low, which deters pharmaceutical development. Expression of biosynthetic machinery in heterologous host organisms like Escherichia coli is one way to access these structures, and subsequent optimization of these systems is critical for future development. We utilized the aureusimine biosynthetic gene cluster as a model system to identify the optimal conditions to produce nonribosomal peptides in the isopropyl β-d-1-thiogalactopyranoside (IPTG)-inducible T7 promoter system of pET28. Single reaction monitoring of nonribosomal products was used to find the optimal concentration of IPTG, postinduction temperature, and the effect of amino acid precursor supplementation. In addition, principle component analysis of these extracts identified 3 previously undiscovered pyrazine products of the aureusimine biosynthetic locus, highlighting the utility of heterologously expressing nonribosomal peptide synthetases to find new products.

scholarly journals Nonprocessive [2 + 2]e- off-loading reductase domains from mycobacterial nonribosomal peptide synthetases

2012 ◽  
Vol 109 (15) ◽  
pp. 5681-5686 ◽  
Author(s):  
A. Chhabra ◽  
A. S. Haque ◽  
R. K. Pal ◽  
A. Goyal ◽  
R. Rai ◽  
...  
Keyword(s):  
Nonribosomal Peptide ◽  
Nonribosomal Peptide Synthetases ◽  
Peptide Synthetases

scholarly journals Core Assembly Mechanism of Quinocarcin/SF-1739: Bimodular Complex Nonribosomal Peptide Synthetases for Sequential Mannich-type Reactions

2013 ◽  
Vol 20 (12) ◽  
pp. 1523-1535 ◽  
Author(s):  
Tomoshige Hiratsuka ◽  
Kento Koketsu ◽  
Atsushi Minami ◽  
Shunsuke Kaneko ◽  
Chiaki Yamazaki ◽  
...  
Keyword(s):  
Nonribosomal Peptide ◽  
Nonribosomal Peptide Synthetases ◽  
Peptide Synthetases ◽  
Assembly Mechanism

Kinetics Profiling of Gramicidin S Synthetase A, a Member of Nonribosomal Peptide Synthetases

Biochemistry ◽  
2014 ◽  
Vol 53 (50) ◽  
pp. 7983-7989 ◽  
Author(s):  
Xun Sun ◽  
Hao Li ◽  
Jonas Alfermann ◽  
Henning D. Mootz ◽  
Haw Yang
Keyword(s):  
Nonribosomal Peptide ◽  
Nonribosomal Peptide Synthetases ◽  
Peptide Synthetases ◽  
Gramicidin S
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