ArticleThe Journal of antibiotics2017
Substrate specificity of radical S-adenosyl-l-methionine dehydratase AprD4 and its partner reductase AprD3 in the C3'-deoxygenation of aminoglycoside antibiotics.
Article in The Journal of antibiotics, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 24 citations in OpenAlex.
- Beyond native reactivity: radical SAM enzymes as platforms for new-to-nature chemistry.RSC chemical biology · 2026Review
- Metabolome profiling by untargeted metabolomics and biomarker panel selection using machine-learning for patients in different stages of peripheral neuropathy induced by oxaliplatin.Frontiers in oncology · 2025Article
- Improving the production of carbamoyltobramycin by an industrial Streptoalloteichus tenebrarius through metabolic engineering.Applied microbiology and biotechnology · 2024Article
- CompleteJournal of the American Chemical Society · 2024Article
- Biosynthetic Origin of the Octose Core and Its Mechanism of Assembly during Apramycin Biosynthesis.Journal of the American Chemical Society · 2023Article
- Characterization and utilization of methyltransferase for apramycin production in Streptoalloteichus tenebrarius.Journal of industrial microbiology & biotechnology · 2022Article
- Mechanistic Investigation of 1,2-Diol Dehydration of Paromamine Catalyzed by the RadicalJournal of the American Chemical Society · 2021Article
- Pyridoxal-5'-phosphate-dependent enzyme GenB3 Catalyzes C-3',4'-dideoxygenation in gentamicin biosynthesis.Microbial cell factories · 2021Article
- Following the electrons: peculiarities in the catalytic cycles of radical SAM enzymes.Natural product reports · 2018Review
- Parallel pathways in the biosynthesis of aminoglycoside antibiotics.F1000Research · 2017Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A radical S-adenosyl-l-methionine dehydratase AprD4 and an NADPH-dependent reductase AprD3 are responsible for the C3'-deoxygenation of pseudodisaccharide paromamine in the biosynthesis of apramycin. These enzymes are involved in the construction of the characteristic structural motif that is not modified by 3'-phosphotransferase in aminoglycoside-resistant bacterial strains. AprD4 catalyzes the C3'-dehydration of paromamine via a radical-mediated reaction mechanism to give 4'-oxolividamine, which is then reduced by AprD3 with NADPH to afford lividamine. In the present study, the substrate specificity of this unique combination of enzymes has been investigated. AprD4 was found to recognize paromamine, neamine, kanamycin C, and kanamycin B to afford 5'-deoxyadenosine as one of products during the C3'-dehydration of aminoglycosides, but not 2'-N-acetylparomamine and paromomycin. Only paromamine and kanamycin C were converted to the corresponding C3'-deoxygenated compounds by AprD4 and AprD3. AprD3 recognizes the 4'-oxolividamine moiety, including the pseudotrisaccharide kanamycin C, and seems to reject the amino group at C6' of neamine and kanamycin B. Chirally deuterium-labeled NADPH was used to identify that that AprD3 transfers the pro-S hydrogen atom of NADPH when reducing 4'-oxolividamine to give lividamine.
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