Interrupted adenylation domains: unique bifunctional enzymes involved in nonribosomal peptide biosynthesis

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Interrupted adenylation domains: unique bifunctional enzymes involved in nonribosomal peptide biosynthesis is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1039/C4NP00120F
P698PubMed publication ID25622971

P50authorSylvie Garneau-TsodikovaQ38323827
P2093author name stringKristin J Labby
Stoyan G Watsula
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P433issue5
P304page(s)641-653
P577publication date2015-05-01
P1433published inNatural Product ReportsQ2376904
P1476titleInterrupted adenylation domains: unique bifunctional enzymes involved in nonribosomal peptide biosynthesis
P478volume32

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cites work (P2860)
Q39010613Diversity of nature's assembly lines - recent discoveries in non-ribosomal peptide synthesis.
Q51351857Expanding Substrate Promiscuity by Engineering a Novel Adenylating-Methylating NRPS Bifunctional Enzyme.
Q36316177Nonribosomal Peptide Synthesis-Principles and Prospects
Q49893928Nonribosomal peptides for iron acquisition: pyochelin biosynthesis as a case study.
Q90859974Pass-back chain extension expands multimodular assembly line biosynthesis
Q52647836Structural basis for backbone N-methylation by an interrupted adenylation domain.
Q38965803Structural insight into the necessary conformational changes of modular nonribosomal peptide synthetases
Q27728008Structures of a Nonribosomal Peptide Synthetase Module Bound to MbtH-Like Proteins Support a Highly Dynamic Domain Architecture
Q90330715Stuffed Methyltransferase Catalyzes the Penultimate Step of Pyochelin Biosynthesis
Q90480958Trapping interactions between catalytic domains and carrier proteins of modular biosynthetic enzymes with chemical probes
Q90587824Type II non-ribosomal peptide synthetase proteins: structure, mechanism, and protein-protein interactions

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