Subdomain dynamics enable chemical chain reactions in non-ribosomal peptide synthetases
Por um escritor misterioso
Descrição
The inherent flexibility of type I non-ribosomal peptide synthetase multienzymes drives their catalytic activities
The tyrocidine NRPS and the derived TycB1 FRET sensors. A) The
Structures of a non-ribosomal peptide synthetase condensation domain suggest the basis of substrate selectivity. - Abstract - Europe PMC
Explorations of catalytic domains in non-ribosomal peptide synthetase enzymology. - Abstract - Europe PMC
Biosynthesis of depsipeptides, or Depsi: The peptides with varied generations - Alonzo - 2020 - Protein Science - Wiley Online Library
Subdomain dynamics enable chemical chain reactions in non-ribosomal peptide synthetases
Structures of a dimodular nonribosomal peptide synthetase reveal conformational flexibility
Nonribosomal Peptide Synthesis
Structural advances toward understanding the catalytic activity and conformational dynamics of modular nonribosomal peptide synthetases - Natural Product Reports (RSC Publishing) DOI:10.1039/D3NP00003F
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Type S Non‐Ribosomal Peptide Synthetases for the Rapid Generation of Tailormade Peptide Libraries** - Abbood - 2022 - Chemistry – A European Journal - Wiley Online Library
Structural and functional aspects of the nonribosomal peptide synthetase condensation domain superfamily: discovery, dissection and diversity - ScienceDirect
Structures of a dimodular nonribosomal peptide synthetase reveal conformational flexibility
