scholarly journals Unprecedented Noncanonical Features of the Nonlinear Nonribosomal Peptide Synthetase Assembly Line for WS9326A Biosynthesis

2021 ◽  
Author(s):  
Myoun‐Su Kim ◽  
Munhyung Bae ◽  
Ye‐Eun Jung ◽  
Jung Min Kim ◽  
Sunghoon Hwang ◽  
...  
Keyword(s):  
Assembly Line ◽  
Nonribosomal Peptide Synthetase ◽  
Nonribosomal Peptide ◽  
Peptide Synthetase

Towards the structure of an unusual nonribosomal peptide synthetase

2014 ◽  
Vol 70 (a1) ◽  
pp. C433-C433
Author(s):  
Diego Alonzo ◽  
Janice Reimer ◽  
Nathan Magarvey ◽  
T. Martin Schmeing
Keyword(s):  
Assembly Line ◽  
Biochemical Characterization ◽  
Food Poisoning ◽  
Structural Features ◽  
Nonribosomal Peptide Synthetase ◽  
Hydroxy Acids ◽  
Nonribosomal Peptide ◽  
X Ray Crystallography ◽  
Family Protein ◽  
Peptide Synthetase

Cereulide synthetase (Ces) is a macromolecular machine that produces a toxin involved in severe and lethal food poisoning. Ces belongs to the nonribosomal peptide synthetase (NRPS) family protein, and as such, it employs an assembly line mechanism to generate its cereulide product. The assembly line for cereulide differs from the canonical NRPS pathway because it adds hydroxy acids instead of amino acids at half of the positions in the molecule. To achieve this, the megaenzyme selects alpha keto acids through specialized adenylation domains and then reduces them to hydroxy acids in embedded ketoreductase domains, before adding them to the growing depsipeptide. Several details on the structural features of this unusual NRPS remain unknown. Here we report a full biochemical characterization of this highly complex megaenzyme. We obtained the kinetic constants of each of its four adenylation domains and probed the side chain selectivity for its alpha keto acid – recognizing adenylation domains. Also, we report that the activating protein MbtH is not required for full activity of the assembly line. Finally, we show that each of the modules can be inhibited through mechanism-based inhibitors, which can restrain the conformational flexibility paving the way for structural studies by X-ray crystallography.

scholarly journals Fungal siderophore biosynthesis catalysed by an iterative nonribosomal peptide synthetase

2020 ◽  
Vol 11 (42) ◽  
pp. 11525-11530
Author(s):  
Yang Hai ◽  
Matthew Jenner ◽  
Yi Tang
Keyword(s):  
Mass Spectrometry ◽  
Assembly Line ◽  
Nonribosomal Peptide Synthetase ◽  
Intact Protein ◽  
Nonribosomal Peptide ◽  
Protein Mass ◽  
Siderophore Biosynthesis ◽  
Protein Mass Spectrometry ◽  
Peptide Synthetase

Snapshots of fungal siderophore biosynthesis on the biosynthetic assembly-line captured by intact protein mass-spectrometry.

scholarly journals Draft Genome Sequence of Saccharomonospora sp. Strain LRS4.154, a Moderately Halophilic Actinobacterium with the Biotechnologically Relevant Polyketide Synthase and Nonribosomal Peptide Synthetase Systems

2017 ◽  
Vol 5 (21) ◽  
Author(s):  
Scarlett Alonso-Carmona ◽  
Blanca Vera-Gargallo ◽  
Rafael R. de la Haba ◽  
Antonio Ventosa ◽  
Horacio Sandoval-Trujillo ◽  
...  
Keyword(s):  
Genome Sequence ◽  
Polyketide Synthase ◽  
Draft Genome ◽  
Nonribosomal Peptide Synthetase ◽  
Open Reading Frames ◽  
Draft Genome Sequence ◽  
Nonribosomal Peptide ◽  
Moderately Halophilic ◽  
Peptide Synthetase ◽  
Reading Frames

ABSTRACT The draft genome sequence of Saccharomonospora sp. strain LRS4.154, a moderately halophilic actinobacterium, has been determined. The genome has 4,860,108 bp, a G+C content of 71.0%, and 4,525 open reading frames (ORFs). The clusters of PKS and NRPS genes, responsible for the biosynthesis of a large number of biomolecules, were identified in the genome.

Engineered Nonribosomal Peptide Synthetase Shows Opposite Amino Acid Loading and Condensation Specificity

ACS Catalysis ◽  
2021 ◽  
pp. 8692-8700
Author(s):  
Aleksa Stanišić ◽  
Annika Hüsken ◽  
Philipp Stephan ◽  
David L. Niquille ◽  
Jochen Reinstein ◽  
...  
Keyword(s):  
Amino Acid ◽  
Nonribosomal Peptide Synthetase ◽  
Nonribosomal Peptide ◽  
Peptide Synthetase ◽  
Acid Loading
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