ArticleBiochemistry2017
Mechanism of Flavoprotein l-6-Hydroxynicotine Oxidase: pH and Solvent Isotope Effects and Identification of Key Active Site Residues.
Article in Biochemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
8 citing papers in PubMed, 16 citations in OpenAlex.
- Ancestral evolution of oxidase activity in a class of (S)-nicotine and (S)-6-hydroxynicotine-degrading flavoenzymes.The Journal of biological chemistry · 2025Article
- Dehydrogenases in the Flavoprotein Amine Oxidoreductase Superfamily.Biochemistry · 2025Article
- 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
- 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
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The flavoenzyme l-6-hydroxynicotine oxidase is a member of the monoamine oxidase family that catalyzes the oxidation of (S)-6-hydroxynicotine to 6-hydroxypseudooxynicotine during microbial catabolism of nicotine. While the enzyme has long been understood to catalyze oxidation of the carbon-carbon bond, it has recently been shown to catalyze oxidation of a carbon-nitrogen bond [Fitzpatrick, P. F., et al. (2016) Biochemistry 55, 697-703]. The effects of pH and mutagenesis of active site residues have now been utilized to study the mechanism and roles of active site residues. Asn166 and Tyr311 bind the substrate, while Lys287 forms a water-mediated hydrogen bond with flavin N5. The N166A and Y311F mutations result in ∼30- and ∼4-fold decreases in k
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Registered trials
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