ArticleThe Journal of biological chemistry2008
Function and structure of a prokaryotic formylglycine-generating enzyme.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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Who cites it
47 citing papers in PubMed, 102 citations in OpenAlex.
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- Mammalian Expression and Mass Spectrometric Characterization of Highly Active Human Arylsulfatase A.Biotechnology journal · 2026Article
- Characterisation of Aequorivita ciconiae sp. nov., isolated from oriental stork, Ciconia boyciana.Antonie van Leeuwenhoek · 2024Article
- Structural insights into the convergent evolution of sulfoxide synthase EgtB-IV, an ergothioneine-biosynthetic homolog of ovothiol synthase OvoA.Structure (London, England : 1993) · 2024Article
- A Novel Sulfatase for Acesulfame Degradation in Wastewater Treatment Plants as Evidenced fromEnvironmental science & technology · 2024Article
- Preparation and Application of an Inexpensive α-Formylglycine Building Block Compatible with Fmoc Solid-Phase Peptide Synthesis.Organic letters · 2023Article
- Genome-Wide Study of Drug ResistantMicroorganisms · 2022Article
- The discovery of penta-peptides inhibiting the activity of the formylglycine-generating enzyme and their potential antibacterial effects againstRSC advances · 2022Article
- Structural insights into choline-O-sulfatase reveal the molecular determinants for ligand binding.Acta crystallographica. Section D, Structural biology · 2022Article
- Purification, Characterization, and Structural Studies of a Sulfatase fromMolecules (Basel, Switzerland) · 2021Article
- Formylglycine-Generating Enzyme-Like Proteins Constitute a Novel Family of Widespread Type VI Secretion System Immunity Proteins.Journal of bacteriology · 2021Article
- Combining functional metagenomics and glycoanalytics to identify enzymes that facilitate structural characterization of sulfated N-glycans.Microbial cell factories · 2021Article
- Discovery of Electrophiles and Profiling of Enzyme Cofactors.Current protocols in chemical biology · 2020Article
- Structure-seq2 probing of RNA structure upon amino acid starvation reveals both known and novel RNA switches inRNA (New York, N.Y.) · 2020Article
- Structure of formylglycine-generating enzyme in complex with copper and a substrate reveals an acidic pocket for binding and activation of molecular oxygen.Chemical science · 2019Article
- Metabolic functions of the human gut microbiota: the role of metalloenzymes.Natural product reports · 2019Review
- Formylglycine-generating enzyme binds substrate directly at a mononuclear Cu(I) center to initiate OProceedings of the National Academy of Sciences of the United States of America · 2019Article
- Anaerobic Degradation of Sulfated Polysaccharides by Two NovelFrontiers in microbiology · 2019Article
- Enzyme-Based Labeling Strategies for Antibody-Drug Conjugates and Antibody Mimetics.Antibodies (Basel, Switzerland) · 2018Review
- Systematic, multiparametric analysis of Mycobacterium tuberculosis intracellular infection offers insight into coordinated virulence.PLoS pathogens · 2017Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
Type I sulfatases require an unusual co- or post-translational modification for their activity in hydrolyzing sulfate esters. In eukaryotic sulfatases, an active site cysteine residue is oxidized to the aldehyde-containing C(alpha)-formylglycine residue by the formylglycine-generating enzyme (FGE). The machinery responsible for sulfatase activation is poorly understood in prokaryotes. Here we describe the identification of a prokaryotic FGE from Mycobacterium tuberculosis. In addition, we solved the crystal structure of the Streptomyces coelicolor FGE homolog to 2.1 A resolution. The prokaryotic homolog exhibits remarkable structural similarity to human FGE, including the position of catalytic cysteine residues. Both biochemical and structural data indicate the presence of an oxidized cysteine modification in the active site that may be relevant to catalysis. In addition, we generated a mutant M. tuberculosis strain lacking FGE. Although global sulfatase activity was reduced in the mutant, a significant amount of residual sulfatase activity suggests the presence of FGE-independent sulfatases in this organism.
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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.