ArticleBiochemistry2016
Mechanism of the Flavoprotein L-Hydroxynicotine Oxidase: Kinetic Mechanism, Substrate Specificity, Reaction Product, and Roles of Active-Site Residues.
Article in Biochemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers, 1 of them a synthesis that pooled it.
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Who cites it
13 citing papers in PubMed, 1 synthesis or guideline pooled it, 22 citations in OpenAlex.
- Insights into Pharmacological Activities of Nicotine and 6-Hydroxy-L-nicotine, a Bacterial Nicotine Derivative: A Systematic Review.Biomolecules · 2023Pooled it
- Dehydrogenases in the Flavoprotein Amine Oxidoreductase Superfamily.Biochemistry · 2025Article
- Directed evolution unlocks oxygen reactivity for a nicotine-degrading flavoenzyme.Nature chemical biology · 2023Article
- Computational Analysis of the Nicotine Oxidoreductase Mechanism by the ONIOM Method.ACS omega · 2021Article
- A cytochrome c is the natural electron acceptor for nicotine oxidoreductase.Nature chemical biology · 2021Article
- Mechanistic study of L-6-hydroxynicotine oxidase by DFT and ONIOM methods.Journal of molecular modeling · 2021Article
- Mechanism of the Flavoprotein d-6-Hydroxynicotine Oxidase: Substrate Specificity, pH and Solvent Isotope Effects, and Roles of Key Active-Site Residues.Biochemistry · 2019Article
- From aggression to autism: new perspectives on the behavioral sequelae of monoamine oxidase deficiency.Journal of neural transmission (Vienna, Austria : 1996) · 2018Review
- Crystallography Coupled with Kinetic Analysis Provides Mechanistic Underpinnings of a Nicotine-Degrading Enzyme.Biochemistry · 2018Article
- The enzymes of microbial nicotine metabolism.Beilstein journal of organic chemistry · 2018Review
- Mechanism of Flavoprotein l-6-Hydroxynicotine Oxidase: pH and Solvent Isotope Effects and Identification of Key Active Site Residues.Biochemistry · 2017Article
- Measurement of Kinetic Isotope Effects in an Enzyme-Catalyzed Reaction by Continuous-Flow Mass Spectrometry.Methods in enzymology · 2017Article
- Structural Analysis Provides Mechanistic Insight into Nicotine Oxidoreductase from Pseudomonas putida.Biochemistry · 2016Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
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Abstract
The flavoprotein L-hydroxynicotine oxidase (LHNO) catalyzes an early step in the bacterial catabolism of nicotine. Although the structure of the enzyme establishes that it is a member of the monoamine oxidase family, LHNO is generally accepted to oxidize a carbon-carbon bond in the pyrrolidine ring of the substrate and has been proposed to catalyze the subsequent tautomerization and hydrolysis of the initial oxidation product to yield 6-hydroxypseudooxynicotine [Kachalova, G., et al. (2011) Proc. Natl. Acad. Sci. U.S.A. 108, 4800-4805]. Analysis of the product of the enzyme from Arthrobacter nicotinovorans by nuclear magnetic resonance and continuous-flow mass spectrometry establishes that the enzyme catalyzes the oxidation of the pyrrolidine carbon-nitrogen bond, the expected reaction for a monoamine oxidase, and that hydrolysis of the amine to form 6-hydroxypseudooxynicotine is nonenzymatic. On the basis of the kcat/Km and kred values for (S)-hydroxynicotine and several analogues, the methyl group contributes only marginally (∼ 0.5 kcal/mol) to transition-state stabilization, while the hydroxyl oxygen and pyridyl nitrogen each contribute ∼ 4 kcal/mol. The small effects on activity of mutagenesis of His187, Glu300, or Tyr407 rule out catalytic roles for all three of these active-site residues.
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