The Ync13-Rga7-Rng10 complex selectively coordinates secretory vesicle trafficking and secondary septum formation during cytokinesis. [PDF]
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Deciphering the Role of Different Ceramide Synthases in the Human Cardiomyocyte Hypertrophic Response. [PDF]
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Elucidation of the Verrucofortine Biosynthetic Pathway Enables Identification of a Cyclodipeptide Prenyltransferase with High Catalytic Efficiency. [PDF]
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ActSeek: fast and accurate search algorithm of active sites in alphafold database. [PDF]
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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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Combinatorialization of Fungal Polyketide Synthase–Peptide Synthetase Hybrid Proteins
Journal of the American Chemical Society, 2014The programming of the fungal polyketide synthase (PKS) is quite complex, with a simple domain architecture leading to elaborate products. An additional level of complexity has been found within PKS-based pathways where the PKS is fused to a single module nonribosomal peptide synthetase (NRPS) to synthesize polyketides conjugated to amino acids.
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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.
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Biosynthesis of Tetronates by a Nonribosomal Peptide Synthetase–Polyketide Synthase System
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