Results 161 to 170 of about 5,756 (191)
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Adenylation Domains in Nonribosomal Peptide Engineering
ChemBioChem, 2019AbstractNonribosomal peptides are a prolific source of bioactive molecules biosynthesized on large, modular assembly line synthetases. Synthetic biologists seek to obtain tailored peptides with tuned or novel bioactivities by engineering modules and domains of these nonribosomal peptide synthetases.
Aleksa Stanišić, Hajo Kries
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Combinatorial biosynthesis of polyketides and nonribosomal peptides
Current Opinion in Chemical Biology, 2001The engineering of polyketide biosynthesis has begun to provide robust targeted libraries for screening against pharmaceutically relevant targets. New technologies that offer methodology for the rapid generation of more structurally diverse libraries have now been demonstrated.
J, Staunton, B, Wilkinson
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A Practical Guideline to Engineering Nonribosomal Peptide Synthetases
2023The bioengineering of nonribosomal peptide synthetases (NRPSs) is a rapidly developing field to access natural product derivatives and new-to-nature natural products like scaffolds with changed or improved properties. However, the rational (re-)design of these often gigantic assembly-line proteins is by no means trivial and needs in-depth insights into
Abbood, N. +3 more
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FRET monitoring of a nonribosomal peptide synthetase
Nature Chemical Biology, 2017Nonribosomal peptide synthetases (NRPSs) are multidomain enzyme templates for the synthesis of bioactive peptides. Large-scale conformational changes during peptide assembly are obvious from crystal structures, yet their dynamics and coupling to catalysis are poorly understood.
Jonas Alfermann +8 more
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Pseudoaeruginosins, Nonribosomal Peptides in Nodularia spumigena
ACS Chemical Biology, 2014Nodularia spumigena is a filamentous cyanobacterium that forms toxic blooms in brackish waters around the world through the production of the pentapeptide toxin nodularin. This cyanobacterium also produces large amounts of protease inhibitors belonging to the aeruginosin and spumigin families. Here we report the discovery of previously unknown protease
Liwei, Liu +9 more
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Synthesis of the Nonribosomal Peptide Phevalin and Analogs
The Journal of Organic Chemistry, 2019Phevalin, a cyclic nonribosomal peptide produced by Staphylococcus aureus, has intriguing biological properties. A synthetic route to access phevalin and similar pyrazinone natural products tyrvalin, leuvalin, phileucin, and a few synthetic analogs is described.
Remya Ramesh +3 more
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Metagenome Driven Discovery of Nonribosomal Peptides
ACS Chemical Biology, 2019Declining rates of novel natural product discovery and exponential rates of rediscovery heralded the end of the 1940s to 1960s "golden era" of antibiotic discovery. Fifty years later, the implementation of molecular screening methodologies revealed that standard culture-based screening approaches had failed to capture the vast majority of environmental
Luke J. Stevenson +2 more
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De Novo Sequencing of Nonribosomal Peptides
2008While nonribosomal peptides (NRPs) are of tremendous pharmacological importance, there is currently no technology capable of high-throughput sequencing of NRPs. Difficulties in sequencing NRPs slow down the progress in elucidating the non-ribosomal genetic code and negatively affect various screening programs aimed at the discovery of natural compounds
Nuno Bandeira +5 more
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Structural Studies of Modular Nonribosomal Peptide Synthetases
2023The non-ribosomal peptide synthetases (NRPSs) are a family of modular enzymes involved in the production of peptide natural products. Not restricted by the constraints of ribosomal peptide and protein production, the NRPSs are able to incorporate unusual amino acids and other suitable building blocks into the final product.
Ketan D, Patel +3 more
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Macrocyclization strategies in polyketide and nonribosomal peptide biosynthesis
Natural Product Reports, 2007AbstractChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 200 leading journals. To access a ChemInform Abstract, please click on HTML or PDF.
Florian, Kopp, Mohamed A, Marahiel
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