Priming Type II Polyketide Synthases via a Type II Nonribosomal Peptide Synthetase Mechanism
نویسندگان
چکیده
منابع مشابه
Regeneration of misprimed nonribosomal peptide synthetases by type II thioesterases.
Nonribosomal peptide synthetases (NRPSs) assemble structurally complex peptides from simple building blocks such as amino and carboxyl acids. Product release by macrocyclization or hydrolysis is catalyzed by a thioesterase domain that is an integrated part of the NRPS enzyme. A second thioesterase of type II (TEII) encoded by a distinct gene associated with the NRPS cluster was previously shown...
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Polyketides draw much attention because of their potential use in pharmaceutical and biotechnological applications. This study identifies an abundant pool of polyketide synthase (PKS) genes from local isolates of tropical fungi found in Thailand in three different ecological niches: insect pathogens, marine inhabitants, and lichen mutualists. We detected 149 PKS genes from 48 fungi using PCR wi...
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Wang et al. (1) report on the cataloging and phylogenetic analysis of gene clusters that encode nonribosomal peptide synthetases (NRPSs) and type I polyketide synthases (PKSs) in sequenced genomes from all three domains of life. We read this article with great interest. However, a few points require a more detailed discussion, and we would like to highlight some complementary analyses previousl...
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متن کاملStructural and functional analysis of two di-domain aromatase/cyclases from type II polyketide synthases.
Aromatic polyketides make up a large class of natural products with diverse bioactivity. During biosynthesis, linear poly-β-ketone intermediates are regiospecifically cyclized, yielding molecules with defined cyclization patterns that are crucial for polyketide bioactivity. The aromatase/cyclases (ARO/CYCs) are responsible for regiospecific cyclization of bacterial polyketides. The two most com...
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ژورنال
عنوان ژورنال: Journal of the American Chemical Society
سال: 2006
ISSN: 0002-7863,1520-5126
DOI: 10.1021/ja0559707