ReviewACS chemical biology2015
Formylglycine, a post-translationally generated residue with unique catalytic capabilities and biotechnology applications.
Review in ACS chemical biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
75 citing papers in PubMed.
- Beyond native reactivity: radical SAM enzymes as platforms for new-to-nature chemistry.RSC chemical biology · 2026Review
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- Excited-State Intramolecular Proton Transfer Enables Self-Reporting Fluorescent Photoaffinity Labeling in Live Cells.Journal of the American Chemical Society · 2026Article
- The evolving landscape of enzymatic technologies for precision synthesis of antibody-drug conjugates.Antibody therapeutics · 2026Review
- Production and inhibition of human Heparan 6-O-Endosulfatase SULF1.Glycobiology · 2025Article
- Effect of Copper-Catalyzed Oxidation on the Aggregation of the Islet Amyloid Polypeptide.Antioxidants (Basel, Switzerland) · 2025Article
- Design and evolution of artificial enzyme with in-situ biosynthesized non-canonical amino acid.Nature communications · 2025Article
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- Engineering protein prenylation: an emerging tool for selective protein modification.Biochemical Society transactions · 2025Review
- Mechanism of OACS central science · 2025Article
- Characterisation of Aequorivita ciconiae sp. nov., isolated from oriental stork, Ciconia boyciana.Antonie van Leeuwenhoek · 2024Article
- Initiation, Propagation, and Termination in the Chemistry of Radical SAM Enzymes.Biochemistry · 2024Review
- Review
- Substrate selectivity and inhibition of the human lysyl hydroxylase JMJD7.Protein science : a publication of the Protein Society · 2024Article
- A Four-Coordinate End-On Superoxocopper(II) Complex: Probing the Link between Coordination Number and Reactivity.Journal of the American Chemical Society · 2024Article
- Boolean Modeling of Biological Network Applied to Protein-Protein Interaction Network of Autism Patients.Biology · 2024Article
- Copper-oxygen adducts: new trends in characterization and properties towards C-H activation.Chemical science · 2024Review
- Bioinspired Synthesis of Allysine for Late-Stage Functionalization of Peptides.Angewandte Chemie (International ed. in English) · 2024Article
- Darobactin Substrate Engineering and Computation Show Radical Stability Governs Ether versus C-C Bond Formation.Journal of the American Chemical Society · 2024Article
- Cloning and Characterization of a NovelMarine drugs · 2024Article
15 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Formylglycine (fGly) is a catalytically essential residue found almost exclusively in the active sites of type I sulfatases. Formed by post-translational oxidation of cysteine or serine side chains, this aldehyde-functionalized residue participates in a unique and highly efficient catalytic mechanism for sulfate ester hydrolysis. The enzymes that produce fGly, formylglycine-generating enzyme (FGE) and anaerobic sulfatase-maturating enzyme (anSME), are as unique and specialized as fGly itself. FGE especially is structurally and mechanistically distinct, and serves the sole function of activating type I sulfatase targets. This review summarizes the current state of knowledge regarding the mechanism by which fGly contributes to sulfate ester hydrolysis, the molecular details of fGly biogenesis by FGE and anSME, and finally, recent biotechnology applications of fGly beyond its natural catalytic function.
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