ArticleThe Journal of biological chemistry2012
Crystal structure of the acyltransferase domain of the iterative polyketide synthase in enediyne biosynthesis.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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22 citing papers in PubMed, 45 citations in OpenAlex.
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- Prokaryotic PfaB is a terminal acyltransferase that determines the final PUFA product.Protein science : a publication of the Protein Society · 2026Article
- Molecular Decoration and Unconventional Double Bond Migration in Irumamycin Biosynthesis.Antibiotics (Basel, Switzerland) · 2024Article
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- Module-Based Polyketide Synthase Engineering forACS synthetic biology · 2023Review
- C-N bond formation by a polyketide synthase.Nature communications · 2023Article
- A single amino acid residue controls acyltransferase activity in a polyketide synthase fromiScience · 2022Article
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- Loading of malonyl-CoA onto tandem acyl carrier protein domains of polyunsaturated fatty acid synthases.The Journal of biological chemistry · 2018Article
- Characterization of the Jomthonic Acids Biosynthesis Pathway and Isolation of Novel Analogues inMarine drugs · 2018Article
- Identification of a biosynthetic gene cluster for the polyene macrolactam sceliphrolactam in a Streptomyces strain isolated from mangrove sediment.Scientific reports · 2018Article
- Substrate Specificity of Acyltransferase Domains for Efficient Transfer of Acyl Groups.Frontiers in microbiology · 2018Article
- Structure-based analysis of the molecular interactions between acyltransferase and acyl carrier protein in vicenistatin biosynthesis.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Comparison of 10,11-Dehydrocurvularin Polyketide Synthases from Alternaria cinerariae and Aspergillus terreus Highlights Key Structural Motifs.Chembiochem : a European journal of chemical biology · 2015Article
- Biochemical and Structural Basis for Controlling Chemical Modularity in Fungal Polyketide Biosynthesis.Journal of the American Chemical Society · 2015Article
- Reprogramming acyl carrier protein interactions of an Acyl-CoA promiscuous trans-acyltransferase.Chemistry & biology · 2014Article
- Article
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- Biochemical determination of enzyme-bound metabolites: preferential accumulation of a programmed octaketide on the enediyne polyketide synthase CalE8.Journal of the American Chemical Society · 2013Article
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7 authors at 2 institutions in 2 countries.
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No grant is acknowledged in the PubMed record.
Abstract
Biosynthesis of the enediyne natural product dynemicin in Micromonospora chersina is initiated by DynE8, a highly reducing iterative type I polyketide synthase that assembles polyketide intermediates from the acetate units derived solely from malonyl-CoA. To understand the substrate specificity and the evolutionary relationship between the acyltransferase (AT) domains of DynE8, fatty acid synthase, and modular polyketide synthases, we overexpressed a 44-kDa fragment of DynE8 (hereafter named AT(DYN10)) encompassing its entire AT domain and the adjacent linker domain. The crystal structure at 1.4 Å resolution unveils a α/β hydrolase and a ferredoxin-like subdomain with the Ser-His catalytic dyad located in the cleft between the two subdomains. The linker domain also adopts a α/β fold abutting the AT catalytic domain. Co-crystallization with malonyl-CoA yielded a malonyl-enzyme covalent complex that most likely represents the acyl-enzyme intermediate. The structure explains the preference for malonyl-CoA with a conserved arginine orienting the carboxylate group of malonate and several nonpolar residues that preclude α-alkyl malonyl-CoA binding. Co-crystallization with acetyl-CoA revealed two noncovalently bound acetates generated by the enzymatic hydrolysis of acetyl-CoA that acts as an inhibitor for DynE8. This suggests that the AT domain can upload the acyl groups from either malonyl-CoA or acetyl-CoA onto the catalytic Ser(651) residue. However, although the malonyl group can be transferred to the acyl carrier protein domain, transfer of the acetyl group to the acyl carrier protein domain is suppressed. Local structural differences may account for the different stability of the acyl-enzyme intermediates.
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