ArticleAnalytical biochemistry2010
A continuous kinetic assay for adenylation enzyme activity and inhibition.
Article in Analytical biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed.
- Adenylation Domain Engineering Enables Biosynthesis of an Improved Polymyxin Antibiotic.Angewandte Chemie (International ed. in English) · 2026Article
- Mapping the nonribosomal specificity code through promiscuity-guided A-domain engineering.Chemical science · 2026Article
- The Intricate Nonribosomal Assembly of a Potent Antifungal Lipopeptide from theJournal of the American Chemical Society · 2025Article
- Direct and quantitative analysis of tRNA acylation using intact tRNA liquid chromatography-mass spectrometry.Nature protocols · 2025Review
- A single Leishmania adenylate-forming enzyme of the ANL superfamily generates both acetyl- and acetoacetyl-CoA.The Journal of biological chemistry · 2024Article
- Structural, biochemical and bioinformatic analyses of nonribosomal peptide synthetase adenylation domains.Natural product reports · 2024Review
- Deciphering the Biosynthesis and Physiological Function of 5-Methylated Pyrazinones Produced by Myxobacteria.ACS central science · 2024Article
- TheiScience · 2024Article
- Chemical structure metagenomics of microbial natural products: surveying nonribosomal peptides and beyond.Beilstein journal of organic chemistry · 2024Article
- Biosynthesis and engineering of the nonribosomal peptides with a C-terminal putrescine.Nature communications · 2023Article
- Biosynthetic incorporation of fluorinated amino acids into the nonribosomal peptide gramicidin S.RSC chemical biology · 2023Article
- Structural basis for the development of potential inhibitors targeting FadD23 from Mycobacterium tuberculosis.Acta crystallographica. Section F, Structural biology communications · 2023Article
- Advances in the adenylation domain: discovery of diverse non-ribosomal peptides.Applied microbiology and biotechnology · 2023Review
- Elucidating the molecular programming of a nonlinear non-ribosomal peptide synthetase responsible for fungal siderophore biosynthesis.Nature communications · 2023Article
- Polyfluorinated salicylic acid analogs do not interfere with siderophore biosynthesis.Tuberculosis (Edinburgh, Scotland) · 2023Article
- Synthesis of functionalized 2,3-diaminopropionates and their potential for directed monobactam biosynthesis.Chemical science · 2023Article
- Bioinformatic Analysis Reveals both Oversampled and Underexplored Biosynthetic Diversity in Nonribosomal Peptides.ACS chemical biology · 2023Article
- Colorimetric Determination of Adenylation Domain Activity in Nonribosomal Peptide Synthetases by Using Chrome Azurol S.Chembiochem : a European journal of chemical biology · 2023Article
- Exploring a chemical scaffold for rapid and selective photoaffinity labelling of non-ribosomal peptide synthetases in living bacterial cells.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2023Article
- The Key Roles ofFrontiers in microbiology · 2023Article
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2 authors.
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Abstract
Adenylation/adenylate-forming enzymes catalyze the activation of a carboxylic acid at the expense of ATP to form an acyl-adenylate intermediate and pyrophosphate (PP(i)). In a second half-reaction, adenylation enzymes catalyze the transfer of the acyl moiety of the acyl-adenylate onto an acceptor molecule, which can be either a protein or a small molecule. We describe the design, development, and validation of a coupled continuous spectrophotometric assay for adenylation enzymes that employs hydroxylamine as a surrogate acceptor molecule, leading to the formation of a hydroxamate. The released pyrophosphate from the first half-reaction is measured using the pyrophosphatase-purine nucleoside phosphorylase coupling system with the chromogenic substrate 7-methylthioguanosine (MesG). The coupled hydroxamate-MesG assay is especially useful for characterizing the activity and inhibition of adenylation enzymes that acylate a protein substrate and/or fail to undergo rapid ATP-PP(i) exchange.
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