ArticleMethods in enzymology2018
Methods for Expression, Purification, and Characterization of PqqE, a Radical SAM Enzyme in the PQQ Biosynthetic Pathway.
Article in Methods in enzymology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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9 citing papers in PubMed.
- Characterization of a Heme-Binding Radical SAM Enzyme HemW fromACS bio & med chem Au · 2026Article
- A Novel Genetic Engineering Approach for DON Detoxification Using a Yeast-Based Multi-Enzyme System.Biology · 2026Article
- Chemical Proteomics Reveal the Inventory of Pyrroloquinoline Quinone Binding Proteins in Bacteria.Journal of the American Chemical Society · 2026Article
- Novel Insights into the Antimicrobial and Antibiofilm Activity of Pyrroloquinoline Quinone (PQQ);Biomolecules · 2024Article
- Improving the alcohol respiratory chain and energy metabolism by enhancing PQQ synthesis in Acetobacter pasteurianus.Journal of industrial microbiology & biotechnology · 2024Article
- Post-translational formation of strained cyclophanes in bacteria.Nature chemistry · 2020Article
- Improved Production of Pyrroloquinoline Quinone by Simultaneous Augmentation of Its Synthesis Gene Expression and Glucose Metabolism in Klebsiella pneumoniae.Current microbiology · 2020Article
- Identification of the Enzymes Mediating the Maturation of the Seryl-tRNA Synthetase Inhibitor SB-217452 during the Biosynthesis of Albomycins.Angewandte Chemie (International ed. in English) · 2020Article
- Electron Paramagnetic Resonance Spectroscopic Identification of the Fe-S Clusters in the SPASM Domain-Containing Radical SAM Enzyme PqqE.Biochemistry · 2019Article
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3 authors.
Funding
Abstract
PqqE is the first enzyme in the biosynthetic pathway of the redox cofactor pyrroloquinoline quinone (PQQ), catalyzing the formation of a carbon-carbon bond in the precursor peptide PqqA. PqqE is a radical S-adenosyl-l-methionine (SAM) (RS) enzyme, a family of enzymes that use the reductive cleavage of a [4Fe-4S] cluster-bound SAM molecule to generate a 5'-deoxyadenosyl radical. This radical is then used to initiate an array of reactions that otherwise would be unlikely to occur. PqqE is a founding member of a subset family of RS enzymes that, additionally to the SAM [4Fe-4S] cluster, have a SPASM domain containing additional, auxiliary Fe-S clusters. Most radical SAM enzymes are highly sensitive to oxygen, which destroys their Fe-S clusters. This can pose several limitations when working with these enzymes, since most of the work has to be done under anaerobic conditions. Here, we summarize the methods developed in our lab for the expression and purification of PqqE. We also highlight the several methods we have used for the characterization of the enzyme.
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