ArticleChembiochem : a European journal of chemical biology2016
Fluorescent Mechanism-Based Probe for Aerobic Flavin-Dependent Enzyme Activity.
Article in Chembiochem : a European journal of chemical biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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Who cites it
5 citing papers in PubMed.
- Flipping the Switch: Innovations in Inducible Probes for Protein Profiling.ACS chemical biology · 2021Review
- Identification of a Bromodomain-like Region in 15-Lipoxygenase-1 Explains Its Nuclear Localization.Angewandte Chemie (International ed. in English) · 2021Article
- Activity-Based Protein Profiling (ABPP) of Oxidoreductases.Chembiochem : a European journal of chemical biology · 2021Review
- Active site labeling of fatty acid and polyketide acyl-carrier protein transacylases.Organic & biomolecular chemistry · 2019Article
- Enzymatic Halogenation and Dehalogenation Reactions: Pervasive and Mechanistically Diverse.Chemical reviews · 2017Review
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Diversity in non-ribosomal peptide and polyketide secondary metabolism is facilitated by interactions between biosynthetic domains with discrete monomer loading and their cognate tailoring enzymes, such as oxidation or halogenation enzymes. The cooperation between peptidyl carrier proteins and flavin-dependent enzymes offers a specialized strategy for monomer selectivity for oxidization of small molecules from within a complex cellular milieu. In an effort to study this process, we have developed fluorescent probes to selectively label aerobic flavin-dependent enzymes. Here we report the preparation and implementation of these tools to label oxidase, monooxygenase, and halogenase flavin-dependent enzymes.
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Registered trials
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