ArticlePloS one2015
Primary Amine Oxidase of Escherichia coli Is a Metabolic Enzyme that Can Use a Human Leukocyte Molecule as a Substrate.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 30 citations in OpenAlex.
- Polyamines control inorganic polyphosphate levels during bacterial nitrogen starvation.bioRxiv : the preprint server for biology · 2026Article
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- Haplotype-resolved genome assembly provides insights into the unique floral scent of Rosa rugosa originated in China.Molecular horticulture · 2026Article
- Metabolic engineering ofApplied and environmental microbiology · 2025Article
- Pathway Driven Target Selection inFrontiers in cellular and infection microbiology · 2022Article
- Phenelzine and Amoxapine Inhibit Tyramine and d-Glucuronic Acid Catabolism in Clinically SignificantPathogens (Basel, Switzerland) · 2021Article
- The ORC ubiquitin ligase OBI1 promotes DNA replication origin firing.Nature communications · 2019Article
- Vascular Adhesion Protein-1: A Cell Surface Amine Oxidase in Translation.Antioxidants & redox signaling · 2019Review
- Article
- Resveratrol, Metabolic Syndrome, and Gut Microbiota.Nutrients · 2018Review
- Copper-dependent amino oxidase 3 governs selection of metabolic fuels in adipocytes.PLoS biology · 2018Article
- Computational Analysis of Host-Pathogen Protein Interactions between Humans and Different Strains of EnterohemorrhagicFrontiers in cellular and infection microbiology · 2017Article
- Microarray studies on the effect of silencing tynA in Escherichia coli K-12.Genomics data · 2016Article
Corrections and comments
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Authors and funding
11 authors at 5 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Escherichia coli amine oxidase (ECAO), encoded by the tynA gene, catalyzes the oxidative deamination of aromatic amines into aldehydes through a well-established mechanism, but its exact biological role is unknown. We investigated the role of ECAO by screening environmental and human isolates for tynA and characterizing a tynA-deletion strain using microarray analysis and biochemical studies. The presence of tynA did not correlate with pathogenicity. In tynA+ Escherichia coli strains, ECAO enabled bacterial growth in phenylethylamine, and the resultant H2O2 was released into the growth medium. Some aminoglycoside antibiotics inhibited the enzymatic activity of ECAO, which could affect the growth of tynA+ bacteria. Our results suggest that tynA is a reserve gene used under stringent environmental conditions in which ECAO may, due to its production of H2O2, provide a growth advantage over other bacteria that are unable to manage high levels of this oxidant. In addition, ECAO, which resembles the human homolog hAOC3, is able to process an unknown substrate on human leukocytes.
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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.