ArticleBiochemistry2009
Structure and inhibition of human diamine oxidase.
Article in Biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.
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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
60 citing papers in PubMed, 121 citations in OpenAlex.
- Article
- Diamine Oxidase and Gastrointestinal Diseases.Biomolecules · 2026Review
- Recombinant human diamine oxidase prevents histamine-induced hypoxia, shock and death in guinea pigs.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2026Article
- Is histamine intolerance a treatable subtype of fibromyalgia? evidence and clinical implications-narrative review.Frontiers in pain research (Lausanne, Switzerland) · 2026Review
- Toward food-grade production of the Glutamicibacter halophytocola diamine oxidase using Komagataella phaffii.AMB Express · 2025Article
- SLC45A4 encodes a peroxisomal putrescine transporter that promotes GABA de novo synthesis.Nature communications · 2025Article
- Research on the potential mechanisms and therapeutic drug for the co-occurrence of major depressive disorder in castration-resistant prostate cancer.Scientific reports · 2025Article
- A Diamine Oxidase fromFoods (Basel, Switzerland) · 2025Article
- Potential Role of Probiotic StrainBiology · 2025Article
- COVID-19 mRNA-1273 vaccination induced mast cell activation with strongly elevated ThInflammation research : official journal of the European Histamine Research Society ... [et al.] · 2025Article
- The tree of life of copper-containing amine oxidases.Frontiers in plant science · 2025Article
- Histamine Promotes Pseudomonas aeruginosa Biofilm Formation and Renders P. aeruginosa Biofilms More Resistant to Gentamicin and Azithromycin.Medical principles and practice : international journal of the Kuwait University, Health Science Centre · 2025Article
- Markers of intestinal barrier damage in patients with chronic insomnia disorder.Frontiers in psychiatry · 2024Article
- Lower Urinary Tract Symptoms (LUTS) as a New Clinical Presentation of Histamine Intolerance: A Prevalence Study of Genetic Diamine Oxidase Deficiency.Journal of clinical medicine · 2023Article
- Expression of Amine Oxidase Proteins in Adrenal Cortical Neoplasm and Pheochromocytoma.Biomedicines · 2023Article
- Enzymatic reactions towards aldehydes: An overview.Flavour and fragrance journal · 2023Review
- A Review on Bio- and Chemosensors for the Detection of Biogenic Amines in Food Safety Applications: The Status in 2022.Sensors (Basel, Switzerland) · 2023Review
- Morphological Assessment and Biomarkers of Low-Grade, Chronic Intestinal Inflammation in Production Animals.Animals : an open access journal from MDPI · 2022Review
- Recent advances in the application of microbial diamine oxidases and other histamine-oxidizing enzymes.World journal of microbiology & biotechnology · 2022Review
- How "Neuronal" Are Human Skin Mast Cells?International journal of molecular sciences · 2022Review
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
Humans have three functioning genes that encode copper-containing amine oxidases. The product of the AOC1 gene is a so-called diamine oxidase (hDAO), named for its substrate preference for diamines, particularly histamine. hDAO has been cloned and expressed in insect cells and the structure of the native enzyme determined by X-ray crystallography to a resolution of 1.8 A. The homodimeric structure has the archetypal amine oxidase fold. Two active sites, one in each subunit, are characterized by the presence of a copper ion and a topaquinone residue formed by the post-translational modification of a tyrosine. Although hDAO shares 37.9% sequence identity with another human copper amine oxidase, semicarbazide sensitive amine oxidase or vascular adhesion protein-1, its substrate binding pocket and entry channel are distinctly different in accord with the different substrate specificities. The structures of two inhibitor complexes of hDAO, berenil and pentamidine, have been refined to resolutions of 2.1 and 2.2 A, respectively. They bind noncovalently in the active-site channel. The inhibitor binding suggests that an aspartic acid residue, conserved in all diamine oxidases but absent from other amine oxidases, is responsible for the diamine specificity by interacting with the second amino group of preferred diamine substrates.
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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.