ArticleThe Journal of biological chemistry2015
An unprecedented NADPH domain conformation in lysine monooxygenase NbtG provides insights into uncoupling of oxygen consumption from substrate hydroxylation.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 50 citations in OpenAlex.
- Hydrazinoacetic acid is a biosynthetic precursor of the bacterially produced nitramine,Applied and environmental microbiology · 2026Article
- Article
- Characterization of the N-Hydroxylating Monooxygenase TheA from Thermocrispum agreste Reveals a Broad Substrate Spectrum.Chembiochem : a European journal of chemical biology · 2025Article
- Functional analysis of R144 in the flavin oxidation mechanism of a flavin-dependent N-monooxygenase.Protein science : a publication of the Protein Society · 2025Article
- The Heme Oxygenase-Like Diiron Enzyme HrmI Reveals Altered Regulatory Mechanisms for Dioxygen Activation and Substrate N-Oxygenation.Journal of the American Chemical Society · 2025Article
- Flavin-dependent enzymatic and photochemical interconversions between phenylarsonic and phenylarsonous acids.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2025Article
- Characterization of the Flavin-Dependent Monooxygenase Involved in the Biosynthesis of the Nocardiosis-Associated Polyketide†.Biochemistry · 2024Article
- The dynamics of the flavin, NADPH, and active site loops determine the mechanism of activation of class B flavin-dependent monooxygenases.Protein science : a publication of the Protein Society · 2024Article
- A biosynthetic aspartate N-hydroxylase performs successive oxidations by holding intermediates at a site away from the catalytic center.The Journal of biological chemistry · 2023Article
- Characterization of a broadly specific cadaverine N-hydroxylase involved in desferrioxamine B biosynthesis in Streptomyces sviceus.PloS one · 2021Article
- Structure and function of a flavin-dependent S-monooxygenase from garlic (The Journal of biological chemistry · 2020Article
- Flavin-dependent N-hydroxylating enzymes: distribution and application.Applied microbiology and biotechnology · 2020Review
- Comparative Investigation into Formycin A and Pyrazofurin A Biosynthesis Reveals Branch Pathways for the Construction ofApplied and environmental microbiology · 2020Article
- Flavin oxidation in flavin-dependent N-monooxygenases.Protein science : a publication of the Protein Society · 2019Article
- Side-Chain Pruning Has Limited Impact on Substrate Preference in a Promiscuous Enzyme.ACS catalysis · 2018Article
- Characterization of the Ornithine Hydroxylation Step in Albachelin Biosynthesis.Molecules (Basel, Switzerland) · 2017Article
- Regulated methionine oxidation by monooxygenases.Free radical biology & medicine · 2017Review
- Characterization of the flavoenzyme XiaK as anChemical science · 2017Article
- Heteroatom-Heteroatom Bond Formation in Natural Product Biosynthesis.Chemical reviews · 2017Review
- Mechanism of Rifampicin Inactivation in Nocardia farcinica.PloS one · 2016Article
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
N-Hydroxylating monooxygenases are involved in the biosynthesis of iron-chelating hydroxamate-containing siderophores that play a role in microbial virulence. These flavoenzymes catalyze the NADPH- and oxygen-dependent hydroxylation of amines such as those found on the side chains of lysine and ornithine. In this work we report the biochemical and structural characterization of Nocardia farcinica Lys monooxygenase (NbtG), which has similar biochemical properties to mycobacterial homologs. NbtG is also active on d-Lys, although it binds l-Lys with a higher affinity. Differently from the ornithine monooxygenases PvdA, SidA, and KtzI, NbtG can use both NADH and NADPH and is highly uncoupled, producing more superoxide and hydrogen peroxide than hydroxylated Lys. The crystal structure of NbtG solved at 2.4 Å resolution revealed an unexpected protein conformation with a 30° rotation of the NAD(P)H domain with respect to the flavin adenine dinucleotide (FAD) domain that precludes binding of the nicotinamide cofactor. This "occluded" structure may explain the biochemical properties of NbtG, specifically with regard to the substantial uncoupling and limited stabilization of the C4a-hydroperoxyflavin intermediate. Biological implications of these findings are discussed.
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