ArticleNature chemical biology2017
Structures of carboxylic acid reductase reveal domain dynamics underlying catalysis.
Article in Nature chemical biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
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Who cites it
48 citing papers in PubMed, 138 citations in OpenAlex.
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- Computation-driven redesign of an NRPS-like carboxylic acid reductase improves activity and selectivity.Science advances · 2024Article
- Engineering carboxylic acid reductases and unspecific peroxygenases for flavor and fragrance biosynthesis.Journal of biotechnology · 2024Review
- Broad Spectrum Enantioselective Amide Bond Synthetase fromACS catalysis · 2024Article
- Structural advances toward understanding the catalytic activity and conformational dynamics of modular nonribosomal peptide synthetases.Natural product reports · 2023Review
- Enzymatic reactions towards aldehydes: An overview.Flavour and fragrance journal · 2023Review
- Computational Study of Base-Catalyzed Thiohemiacetal Decomposition inThe journal of physical chemistry. B · 2023Article
- From Protein Film Electrochemistry to Nanoconfined Enzyme Cascades and the Electrochemical Leaf.Chemical reviews · 2023Review
- Structural Studies of Modular Nonribosomal Peptide Synthetases.Methods in molecular biology (Clifton, N.J.) · 2023Article
- A Nanoconfined Four-Enzyme Cascade Simultaneously Driven by Electrical and Chemical Energy, with Built-in Rapid, Confocal Recycling of NADP(H) and ATP.ACS catalysis · 2022Article
- Protein-protein interface analysis of the non-ribosomal peptide synthetase peptidyl carrier protein and enzymatic domains.Synthetic and systems biotechnology · 2022Review
- Chemogenomics identifies acetyl-coenzyme A synthetase as a target for malaria treatment and prevention.Cell chemical biology · 2022Article
- Novel Variation in Acyl-CoA Synthetase Long Chain Family Member 6 (ACSL6) Results in Protein Structural Modification and Multiple Non-Related Neoplasia in a 46-Year-Old: Case Report.Frontiers in oncology · 2022Article
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
Abstract
Carboxylic acid reductase (CAR) catalyzes the ATP- and NADPH-dependent reduction of carboxylic acids to the corresponding aldehydes. The enzyme is related to the nonribosomal peptide synthetases, consisting of an adenylation domain fused via a peptidyl carrier protein (PCP) to a reductase termination domain. Crystal structures of the CAR adenylation-PCP didomain demonstrate that large-scale domain motions occur between the adenylation and thiolation states. Crystal structures of the PCP-reductase didomain reveal that phosphopantetheine binding alters the orientation of a key Asp, resulting in a productive orientation of the bound nicotinamide. This ensures that further reduction of the aldehyde product does not occur. Combining crystallography with small-angle X-ray scattering (SAXS), we propose that molecular interactions between initiation and termination domains are limited to competing PCP docking sites. This theory is supported by the fact that (R)-pantetheine can support CAR activity for mixtures of the isolated domains. Our model suggests directions for further development of CAR as a biocatalyst.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.