ReviewJournal of molecular evolution2013
Structure-function relationships in the evolutionary framework of spermine oxidase.
Review in Journal of molecular evolution, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 27 citations in OpenAlex.
- Article
- Polyamine oxidation enzymes regulate sexual mating/filamentation and pathogenicity in Sporisorium scitamineum.Molecular plant pathology · 2024Article
- Influence of Some Heterocyclic, Cyclic, and Nitrogen-Containing Compounds on Oxidative Deamination of Polyamines in a Cell-Free Test System.Bulletin of experimental biology and medicine · 2024Article
- Unveiling the hidden players: noncoding RNAs orchestrating polyamine metabolism in disease.Cell & bioscience · 2024Review
- Characterization of polyamine metabolism predicts prognosis, immune profile, and therapeutic efficacy in lung adenocarcinoma patients.Frontiers in cell and developmental biology · 2024Article
- Spermine oxidase induces DNA damage and sensitizes fusion negative rhabdomyosarcoma cells to irradiation.Frontiers in cell and developmental biology · 2023Article
- Transcriptome and co-expression network analysis reveals the molecular mechanism of inosine monophosphate-specific deposition in chicken muscle.Frontiers in physiology · 2023Article
- The Impact of Spermidine on C2C12 Myoblasts Proliferation, Redox Status and Polyamines Metabolism under HInternational journal of molecular sciences · 2022Article
- Structure of human spermine oxidase in complex with a highly selective allosteric inhibitor.Communications biology · 2022Article
- The tree of life of polyamine oxidases.Scientific reports · 2020Article
- Discovery and antitumor evaluation of novel inhibitors of spermine oxidase.Journal of enzyme inhibition and medicinal chemistry · 2019Article
- Exploring the activity of polyamine analogues on polyamine and spermine oxidase: methoctramine, a potent and selective inhibitor of polyamine oxidase.Journal of enzyme inhibition and medicinal chemistry · 2019Article
- Glutamate Excitotoxicity Linked to Spermine Oxidase Overexpression.Molecular neurobiology · 2018Article
- Targeting polyamine metabolism for cancer therapy and prevention.The Biochemical journal · 2016Review
- Astrocyte-Dependent Vulnerability to Excitotoxicity in Spermine Oxidase-Overexpressing Mouse.Neuromolecular medicine · 2016Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Spermine oxidase is a FAD-dependent enzyme that specifically oxidizes spermine, and plays a central role in the highly regulated catabolism of polyamines in vertebrates. The spermine oxidase substrate is specifically spermine, a tetramine that plays mandatory roles in several cell functions, such as DNA synthesis, cellular proliferation, modulation of ion channels function, cellular signalling, nitric oxide synthesis and inhibition of immune responses. The oxidative products of spermine oxidase activity are spermidine, H2O2 and the aldehyde 3-aminopropanal that spontaneously turns into acrolein. In this study the reconstruction of the phylogenetic relationships among spermine oxidase proteins from different vertebrate taxa allowed to infer their molecular evolutionary history, and assisted in elucidating the conservation of structural and functional properties of this enzyme family. The amino acid residues, which have been hypothesized or demonstrated to play a pivotal role in the enzymatic activity, and substrate specificity are here analysed to obtain a comprehensive and updated view of the structure-function relationships in the evolution of spermine oxidase.
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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.