Matej Repič
14 Papers
124 Citations
Matej Repič is an academic researcher. The author has contributed to research in topics: Monoamine oxidase B & Chemistry. The author has an hindex of 11, co-authored 14 publications.
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Papers
How are Biogenic Amines Metabolized by Monoamine Oxidases
TL;DR: A new two-step hydride mechanism for the MAO-catalysed oxidative deamination of amines is proposed that is in agreement with available experimental data and provided evidence against both traditional polar nucleophilic and single-electron radical pathways.
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The Chemistry of Neurodegeneration: Kinetic Data and Their Implications.
TL;DR: The role of the heavy metal ions, selected scavengers and scavenging enzymes, and the relevance of certain foods and food supplements, including curcumin, garlic, N-acetyl cysteine, caffeine and red wine, as well as the long-term administration of non-steroid anti-inflammatory drugs and occasional tobacco smoking, are considered.
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Computational Study of the pKa Values of Potential Catalytic Residues in the Active Site of Monoamine Oxidase B
TL;DR: Tory evidence is offered that the amine is most likely to be present in the active site in its protonated form, which is similar to the conclusion from experimental studies of MAO A, which can allow for the design of novel and improved MAO B inhibitors.
Examining electrostatic preorganization in monoamine oxidases A and B by structural comparison and pKa calculations.
TL;DR: The results show that the electrostatic preorganizations in both active sites are very similar, supporting the idea that both enzymes work by the same mechanism.
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Empirical valence bond simulations of the hydride transfer step in the monoamine oxidase B catalyzed metabolism of dopamine: EVB Simulations of Hydride Transfer in MAO B
Matej Repič,Robert Vianello,Miha Purg,Fernanda Duarte,Paul Bauer,Shina Caroline Lynn Kamerlin,Janez Mavri +6 more
TL;DR: In this paper, the authors present a comprehensive study of the rate-limiting step of dopamine degradation by MAO B, which consists in the hydride transfer from the methylene group of the substrate to the flavin moiety of the FAD prosthetic group.