ArticleNature chemical biology2016
A pyridoxal phosphate-dependent enzyme that oxidizes an unactivated carbon-carbon bond.
Article in Nature chemical biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 46 citations in OpenAlex.
- Unconventional Biocatalytic Strategies Orchestrate the Synthesis of the Nucleoside Analog Sinefungin.Journal of the American Chemical Society · 2026Article
- Toward an Understanding of the Mechanistic Differences Between the Hydroxylating and Desaturating Pyridoxal 5'-Phosphate-Dependent L-Arginine Oxidases.Chembiochem : a European journal of chemical biology · 2026Article
- Terminal alkyne formation by a pyridoxal phosphate-dependent enzyme.Nature chemical biology · 2026Article
- Molecular basis for the diversification of lincosamide biosynthesis by pyridoxal phosphate-dependent enzymes.Nature chemistry · 2025Article
- Bioisosteric replacement of pyridoxal-5'-phosphate to pyridoxal-5'-tetrazole targeting Bacillus subtilis GabR.Protein science : a publication of the Protein Society · 2025Article
- Nature-Inspired Radical Pyridoxal-Mediated C-C Bond Formation.Journal of the American Chemical Society · 2024Article
- Deciphering chemical logic of fungal natural product biosynthesis through heterologous expression and genome mining.Natural product reports · 2023Review
- A shared mechanistic pathway for pyridoxal phosphate-dependent arginine oxidases.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- An engineered biosynthetic-synthetic platform for production of halogenated indolmycin antibiotics.Chemical science · 2021Article
- Oxygen reactivity with pyridoxal 5'-phosphate enzymes: biochemical implications and functional relevance.Amino acids · 2020Review
- Pyridoxal-5'-phosphate-dependent bifunctional enzyme catalyzed biosynthesis of indolizidine alkaloids in fungi.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Article
- Convergent biosynthetic transformations to a bacterial specialized metabolite.Nature chemical biology · 2019Article
- The hidden enzymology of bacterial natural product biosynthesis.Nature reviews. Chemistry · 2019Article
- Pyridoxal-5'-phosphate as an oxygenase cofactor: Discovery of a carboxamide-forming, α-amino acid monooxygenase-decarboxylase.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Inhibitors of Serine Proteases from a Microcystis sp. Bloom Material Collected from Timurim Reservoir, Israel.Marine drugs · 2017Article
- Investigating the Biosynthesis of Natural Products from Marine Proteobacteria: A Survey of Molecules and Strategies.Marine drugs · 2017Review
- Enzyme classification using complex dynamic hemithioacetal systems.Chemical communications (Cambridge, England) · 2016Article
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7 authors at 1 institution in 1 country.
Funding
Abstract
Pyridoxal 5'-phosphate (PLP)-dependent enzymes have wide catalytic versatility but are rarely known for their ability to react with oxygen to catalyze challenging reactions. Here, using in vitro reconstitution and kinetic analysis, we report that the indolmycin biosynthetic enzyme Ind4, from Streptomyces griseus ATCC 12648, is an unprecedented O2- and PLP-dependent enzyme that carries out a four-electron oxidation of L-arginine, including oxidation of an unactivated carbon-carbon (C-C) bond. We show that the conjugated product of this reaction, which is susceptible to nonenzymatic deamination, is efficiently intercepted and stereospecifically reduced by the partner enzyme Ind5 to give D-4,5-dehydroarginine. Thus, Ind4 couples the redox potential of O2 with the ability of PLP to stabilize anions to efficiently oxidize an unactivated C-C bond, with the subsequent stereochemical inversion by Ind5 preventing off-pathway reactions. Altogether, these results expand our knowledge of the catalytic versatility of PLP-dependent enzymes and enrich the toolbox for oxidative biocatalysis.
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Registered trials
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.