ArticleBiochemistry2007
Biochemical characterization of a flavin adenine dinucleotide-dependent monooxygenase, ornithine hydroxylase from Pseudomonas aeruginosa, suggests a novel reaction mechanism.
Article in Biochemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 61 citations in OpenAlex.
- Characterization of the N-Hydroxylating Monooxygenase TheA from Thermocrispum agreste Reveals a Broad Substrate Spectrum.Chembiochem : a European journal of chemical biology · 2025Article
- Unlocking the catalytic precision of ligand-controlled enzymatic halogenation.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Unifying and versatile features of flavin-dependent monooxygenases: Diverse catalysis by a common C4a-(hydro)peroxyflavin.The Journal of biological chemistry · 2023Review
- Microbial siderophores as molecular shuttles for metal cations: sources, sinks and application perspectives.Archives of microbiology · 2023Review
- 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
- l-Ornithine-N5-monooxygenase (PvdA) Substrate Analogue Inhibitors forBiomolecules · 2022Article
- Mechanistic Insights and Potential Use of Siderophores Producing Microbes in Rhizosphere for Mitigation of Stress in Plants Grown in Degraded Land.Frontiers in microbiology · 2022Review
- Characterization of a broadly specific cadaverine N-hydroxylase involved in desferrioxamine B biosynthesis in Streptomyces sviceus.PloS one · 2021Article
- Flavin-dependent N-hydroxylating enzymes: distribution and application.Applied microbiology and biotechnology · 2020Review
- PvdF of pyoverdin biosynthesis is a structurally unique NArchives of biochemistry and biophysics · 2019Article
- Characterization of the Ornithine Hydroxylation Step in Albachelin Biosynthesis.Molecules (Basel, Switzerland) · 2017Article
- Nonribosomal peptide synthetase biosynthetic clusters of ESKAPE pathogens.Natural product reports · 2017Review
- Characterization of the flavoenzyme XiaK as anChemical science · 2017Article
- Heteroatom-Heteroatom Bond Formation in Natural Product Biosynthesis.Chemical reviews · 2017Review
- Burkholderia phytofirmans Inoculation-Induced Changes on the Shoot Cell Anatomy and Iron Accumulation Reveal Novel Components of Arabidopsis-Endophyte Interaction that Can Benefit Downstream Biomass Deconstruction.Frontiers in plant science · 2016Article
- 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
- Crystallographic evidence of drastic conformational changes in the active site of a flavin-dependent N-hydroxylase.Biochemistry · 2014Article
- How pH modulates the reactivity and selectivity of a siderophore-associated flavin monooxygenase.Biochemistry · 2014Article
- Flavoprotein monooxygenases for oxidative biocatalysis: recombinant expression in microbial hosts and applications.Frontiers in microbiology · 2014Review
- Role of Ser-257 in the sliding mechanism of NADP(H) in the reaction catalyzed by the Aspergillus fumigatus flavin-dependent ornithine N5-monooxygenase SidA.The Journal of biological chemistry · 2013Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Pyoverdin is the hydroxamate siderophore produced by the opportunistic pathogen Pseudomonas aeruginosa under the iron-limiting conditions of the human host. This siderophore includes derivatives of ornithine in the peptide backbone that serve as iron chelators. PvdA is the ornithine hydroxylase, which performs the first enzymatic step in preparation of these derivatives. PvdA requires both flavin adenine dinucleotide (FAD) and nicotinamide adenine dinucleotide phosphate (NADPH) for activity; it was found to be a soluble monomer most active at pH 8.0. The enzyme demonstrated Michaelis-Menten kinetics in an NADPH oxidation assay, but a hydroxylation assay indicated substrate inhibition at high ornithine concentration. PvdA is highly specific for both substrate and coenzyme, and lysine was shown to be a nonsubstrate effector and mixed inhibitor of the enzyme with respect to ornithine. Chloride is a mixed inhibitor of PvdA with respect to ornithine but a competitive inhibitor with respect to NADPH, and a bulky mercurial compound (p-chloromercuribenzoate) is a mixed inhibitor with respect to ornithine. Steady-state experiments indicate that PvdA/FAD forms a ternary complex with NADPH and ornithine for catalysis. PvdA in the absence of ornithine shows slow substrate-independent flavin reduction by NADPH. Biochemical comparison of PvdA to p-hydroxybenzoate hydroxylase (PHBH, from Pseudomonas fluorescens) and flavin-containing monooxygenases (FMOs, from Schizosaccharomyces pombe and hog liver microsomes) leads to the hypothesis that PvdA catalysis proceeds by a novel reaction mechanism.
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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.