Analysis of 21 Apiospora genomes reveals a genus with tremendous synthesis potential for carbohydrate-active enzymes and secondary metabolites. [PDF]
Sørensen T +7 more
europepmc +1 more source
Genome sequences of seven <i>Streptomyces</i> isolates for genome prospecting. [PDF]
Babka D +14 more
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Recent progress on collagen triple helix structure, stability and assembly
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Evolution and Taxonomic Distribution of Nonribosomal Peptide and Polyketide Synthases
The majority of nonribosomal peptide synthases and type I polyketide synthases are multimodular megasynthases of oligopeptide and polyketide secondary metabolites, respectively. Owing to their multimodular architecture, they synthesize their metabolites in assembly line logic.
Dimitris Mossialos +2 more
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Post-translational modification of polyketide and nonribosomal peptide synthases
Current Opinion in Chemical Biology, 1997The past year has witnessed a major advance in the study of polyketide and nonribosomal peptide biosynthesis with the identification of the phosphopantetheinyl transferase enzyme family, enzymes required to produce active, post-translationally modified polyketide and peptide synthases.
Christopher Walsh +2 more
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Computational structural enzymology methodologies for the study and engineering of fatty acid synthases, polyketide synthases and nonribosomal peptide synthetases [PDF]
Various computational methodologies can be applied to enzymological studies on enzymes in the fatty acid, polyketide, and non-ribosomal peptide biosynthetic pathways. These multi-domain complexes are called fatty acid synthases, polyketide synthases, and
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Biosynthesis of Tetronates by a Nonribosomal Peptide Synthetase–Polyketide Synthase System
Organic Letters, 2023A cryptic tetronate biosynthetic pathway was identified in Kitasatospora niigatensis DSM 44781 via heterologous expression. Distinct from the currently known biosynthetic pathways, this system utilizes a partially functional nonribosomal peptide synthetase and a broadly selective polyketide synthase to direct the assembly and lactonization of the ...
Wenya Tian +6 more
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Nitration of a peptide phytotoxin by bacterial nitric oxide synthase
Nature, 2004Nitric oxide (NO) is a potent intercellular signal in mammals that mediates key aspects of blood pressure, hormone release, nerve transmission and the immune response of higher organisms. Proteins homologous to full-length mammalian nitric oxide synthases (NOSs) are found in lower multicellular organisms. Recently, genome sequencing has shown that some
Johan A, Kers +8 more
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Esherichia coli microcin B17 is a posttranslationally modified peptide that inhibits bacterial DNA gyrase. It contains four oxazole and four thiazole rings and is representative of a broad class of pharmaceutically important natural products with five-membered heterocycles derived from peptide precursors.
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