ArticleBiochemistry2014
Crystallographic evidence of drastic conformational changes in the active site of a flavin-dependent N-hydroxylase.
Article in Biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Crystal Structure and Conformational Dynamics of N─N Bond-Forming Piperazate Synthase.Chembiochem : a European journal of chemical biology · 2026Article
- 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
- Recent Developments and Challenges in the Enzymatic Formation of Nitrogen-Nitrogen Bonds.ACS catalysis · 2025Review
- 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
- TheFrontiers in microbiology · 2024Article
- Molecular mechanism of a large conformational change of the quinone cofactor in the semiquinone intermediate of bacterial copper amine oxidase.Chemical science · 2022Article
- Characterization of a broadly specific cadaverine N-hydroxylase involved in desferrioxamine B biosynthesis in Streptomyces sviceus.PloS one · 2021Article
- Trapping conformational states of a flavin-dependentThe Journal of biological chemistry · 2020Article
- Flavin-dependent N-hydroxylating enzymes: distribution and application.Applied microbiology and biotechnology · 2020Review
- Antifungal peptides produced by actinomycetes and their biological activities against plant diseases.The Journal of antibiotics · 2020Review
- A heme-dependent enzyme forms the nitrogen-nitrogen bond in piperazate.Nature chemical biology · 2017Article
- Characterization of the flavoenzyme XiaK as anChemical science · 2017Article
- Structural and mechanistic basis of differentiated inhibitors of the acute pancreatitis target kynurenine-3-monooxygenase.Nature communications · 2017Article
- Mechanism of Rifampicin Inactivation in Nocardia farcinica.PloS one · 2016Article
- Contribution to catalysis of ornithine binding residues in ornithine N5-monooxygenase.Archives of biochemistry and biophysics · 2015Article
- An unprecedented NADPH domain conformation in lysine monooxygenase NbtG provides insights into uncoupling of oxygen consumption from substrate hydroxylation.The Journal of biological chemistry · 2015Article
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Authors and funding
4 authors.
Funding
Abstract
The soil actinomycete Kutzneria sp. 744 produces a class of highly decorated hexadepsipeptides, which represent a new chemical scaffold that has both antimicrobial and antifungal properties. These natural products, known as kutznerides, are created via nonribosomal peptide synthesis using various derivatized amino acids. The piperazic acid moiety contained in the kutzneride scaffold, which is vital for its antibiotic activity, has been shown to derive from the hydroxylated product of l-ornithine, l-N(5)-hydroxyornithine. The production of this hydroxylated species is catalyzed by the action of an FAD- and NAD(P)H-dependent N-hydroxylase known as KtzI. We have been able to structurally characterize KtzI in several states along its catalytic trajectory, and by pairing these snapshots with the biochemical and structural data already available for this enzyme class, we propose a structurally based reaction mechanism that includes novel conformational changes of both the protein backbone and the flavin cofactor. Further, we were able to recapitulate these conformational changes in the protein crystal, displaying their chemical competence. Our series of structures, with corroborating biochemical and spectroscopic data collected by us and others, affords mechanistic insight into this relatively new class of flavin-dependent hydroxylases and adds another layer to the complexity of flavoenzymes.
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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.