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dc.contributor.authorRamsay, Rona R.
dc.contributor.authorAlbreht, Alen
dc.date.accessioned2021-09-02T08:30:07Z
dc.date.available2021-09-02T08:30:07Z
dc.date.issued2021-08-31
dc.identifier275669868
dc.identifier26b3534b-c8f5-4c9f-990e-1daafe39681d
dc.identifier000703015300001
dc.identifier85124125247
dc.identifier.citationRamsay , R R & Albreht , A 2021 , ' Questions in the chemical enzymology of MAO ' , Chemistry , vol. 3 , no. 3 , pp. 959-978 . https://doi.org/10.3390/chemistry3030069en
dc.identifier.issn2624-8549
dc.identifier.urihttps://hdl.handle.net/10023/23890
dc.descriptionA.A. is supported by the Slovenian Research Agency (Research Program P1-0005).en
dc.description.abstractWe have structure, a wealth of kinetic data, thousands of chemical ligands, and clinical 8 information for the effects of a range of drugs on monoamine oxidase activity in vivo. We have 9 comparative information from various species and mutations on kinetics, and effects of inhibition. 10 Yet there are what seem like simple questions still to be answered. This article presents a brief sum-11 mary of existing experimental evidence the background and poses questions that remain intriguing 12 for chemists and biochemists researching the chemical enzymology of and drug design for mono-13 amine oxidases (FAD-containing EC 4.1.3.4).
dc.format.extent2681206
dc.language.isoeng
dc.relation.ispartofChemistryen
dc.subjectChemical mechanismen
dc.subjectKinetic mechanismen
dc.subjectOxidationen
dc.subjectProtein flexibiityen
dc.subjectCysteine modificationen
dc.subjectReversible/irreversible inhibitionen
dc.subjectMolecular dynmaicsen
dc.subjectSimulationen
dc.subjectQD Chemistryen
dc.subject.lccQDen
dc.titleQuestions in the chemical enzymology of MAOen
dc.typeJournal itemen
dc.contributor.institutionUniversity of St Andrews. School of Biologyen
dc.identifier.doi10.3390/chemistry3030069
dc.description.statusPeer revieweden


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