ArticleInternational journal of molecular sciences2012
The role of protein crystallography in defining the mechanisms of biogenesis and catalysis in copper amine oxidase.
Article in International journal of molecular sciences, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 45 citations in OpenAlex.
- Real-time capture of domain movements during copper amine oxidase catalysis by mix-and-inject serial crystallography.Nature communications · 2025Article
- [Functional study of amine oxidase copper-containing 1 (AOC1) in lipid metabolism].Sheng wu yi xue gong cheng xue za zhi = Journal of biomedical engineering = Shengwu yixue gongchengxue zazhi · 2024Article
- A New Activity Assay Method for Diamine Oxidase Based on Matrix-Assisted Laser Desorption/Ionization Time-of-Flight Mass Spectrometry.Molecules (Basel, Switzerland) · 2024Article
- Cuproptosis-related DNA methylation signature predict prognosis and immune microenvironment in cutaneous melanoma.Discover oncology · 2024Article
- Identifying Metal Binding Sites in Proteins Using Homologous Structures, the MADE Approach.Journal of chemical information and modeling · 2023Article
- Direct Activation of the C(spJournal of the American Chemical Society · 2023Article
- Insight into the Spatial Arrangement of the Lysine Tyrosylquinone and CuInternational journal of molecular sciences · 2022Article
- Molecular mechanism of a large conformational change of the quinone cofactor in the semiquinone intermediate of bacterial copper amine oxidase.Chemical science · 2022Article
- Re-evaluation of protein neutron crystallography with and without X-ray/neutron joint refinement.IUCrJ · 2022Article
- Metalloprotein catalysis: structural and mechanistic insights into oxidoreductases from neutron protein crystallography.Acta crystallographica. Section D, Structural biology · 2021Review
- CytochromeThe Journal of biological chemistry · 2019Article
- Article
- Empirical Valence Bond Simulations Suggest a Direct Hydride Transfer Mechanism for Human Diamine Oxidase.ACS omega · 2018Article
- Crystal structure of human lysyl oxidase-like 2 (hLOXL2) in a precursor state.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Small Molecule Lysyl Oxidase-like 2 (LOXL2) Inhibitors: The Identification of an Inhibitor Selective for LOXL2 over LOX.ACS medicinal chemistry letters · 2017Article
- Probing the Catalytic Mechanism of Copper Amine Oxidase from Arthrobacter globiformis with Halide Ions.The Journal of biological chemistry · 2015Article
- Copper active sites in biology.Chemical reviews · 2014Review
- Human copper-dependent amine oxidases.Archives of biochemistry and biophysics · 2014Review
- Structural analysis of aliphatic versus aromatic substrate specificity in a copper amine oxidase from Hansenula polymorpha.Biochemistry · 2013Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Copper amine oxidases (CAOs) are a ubiquitous group of enzymes that catalyze the conversion of primary amines to aldehydes coupled to the reduction of O(2) to H(2)O(2). These enzymes utilize a wide range of substrates from methylamine to polypeptides. Changes in CAO activity are correlated with a variety of human diseases, including diabetes mellitus, Alzheimer's disease, and inflammatory disorders. CAOs contain a cofactor, 2,4,5-trihydroxyphenylalanine quinone (TPQ), that is required for catalytic activity and synthesized through the post-translational modification of a tyrosine residue within the CAO polypeptide. TPQ generation is a self-processing event only requiring the addition of oxygen and Cu(II) to the apoCAO. Thus, the CAO active site supports two very different reactions: TPQ synthesis, and the two electron oxidation of primary amines. Crystal structures are available from bacterial through to human sources, and have given insight into substrate preference, stereospecificity, and structural changes during biogenesis and catalysis. In particular both these processes have been studied in crystallo through the addition of native substrates. These latter studies enable intermediates during physiological turnover to be directly visualized, and demonstrate the power of this relatively recent development in protein crystallography.
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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.