ArticleStructure (London, England : 1993)2020
Repurposing the GNAT Fold in the Initiation of Polyketide Biosynthesis.
Article in Structure (London, England : 1993), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 17 citations in OpenAlex.
- A single viral enzyme drives tRNA-dependent hypermodification of DNA at adenine.Nature communications · 2026Article
- Redefining the role of the EryM acetyltransferase in natural product biosynthetic pathways.Structure (London, England : 1993) · 2025Article
- GCN5L: a critical target in energy metabolism pathways.Frontiers in cell and developmental biology · 2025Review
- Structure-function analysis of carrier protein-dependent 2-sulfamoylacetyl transferase in the biosynthesis of altemicidin.Nature communications · 2024Article
- Unique Initiation and Termination Mechanisms Involved in the Biosynthesis of a Hybrid Polyketide-Nonribosomal Peptide Lyngbyapeptin B Produced by the Marine CyanobacteriumACS chemical biology · 2023Article
- C-N bond formation by a polyketide synthase.Nature communications · 2023Article
- Thiamyxins: Structure and Biosynthesis of Myxobacterial RNA-Virus Inhibitors.Angewandte Chemie (International ed. in English) · 2022Article
- Genome-based discovery and total synthesis of janustatins, potent cytotoxins from a plant-associated bacterium.Nature chemistry · 2022Article
- Structural Basis for Control of Methylation Extent in Polyketide Synthase Metal-DependentACS chemical biology · 2022Article
- Initiating polyketide biosynthesis by on-line methyl esterification.Nature communications · 2021Article
- Gcn5-RelatedFrontiers in molecular biosciences · 2021Article
- The LnmK Bifunctional Acyltransferase/Decarboxylase Specifying (2Biochemistry · 2020Article
- Repurposing Modular Polyketide Synthases and Non-ribosomal Peptide Synthetases for Novel Chemical Biosynthesis.Frontiers in molecular biosciences · 2020Review
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
Natural product biosynthetic pathways are replete with enzymes repurposed for new catalytic functions. In some modular polyketide synthase (PKS) pathways, a GCN5-related N-acetyltransferase (GNAT)-like enzyme with an additional decarboxylation function initiates biosynthesis. Here, we probe two PKS GNAT-like domains for the dual activities of S-acyl transfer from coenzyme A (CoA) to an acyl carrier protein (ACP) and decarboxylation. The GphF and CurA GNAT-like domains selectively decarboxylate substrates that yield the anticipated pathway starter units. The GphF enzyme lacks detectable acyl transfer activity, and a crystal structure with an isobutyryl-CoA product analog reveals a partially occluded acyltransfer acceptor site. Further analysis indicates that the CurA GNAT-like domain also catalyzes only decarboxylation, and the initial acyl transfer is catalyzed by an unidentified enzyme. Thus, PKS GNAT-like domains are re-classified as GNAT-like decarboxylases. Two other decarboxylases, malonyl-CoA decarboxylase and EryM, reside on distant nodes of the superfamily, illustrating the adaptability of the GNAT fold.
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