Show simple item record

Files in this item


Item metadata

dc.contributor.authorRamsay, Rona R.
dc.contributor.authorAlbreht, Alen
dc.identifier.citationRamsay , R R & Albreht , A 2021 , ' Questions in the chemical enzymology of MAO ' , Chemistry , vol. 3 , no. 3 , pp. 959-978 .
dc.identifier.otherPURE: 275669868
dc.identifier.otherPURE UUID: 26b3534b-c8f5-4c9f-990e-1daafe39681d
dc.identifier.otherWOS: 000703015300001
dc.identifier.otherScopus: 85124125247
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
dc.rightsCopyright © 2021 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (
dc.subjectChemical mechanismen
dc.subjectKinetic mechanismen
dc.subjectProtein flexibiityen
dc.subjectCysteine modificationen
dc.subjectReversible/irreversible inhibitionen
dc.subjectMolecular dynmaicsen
dc.subjectQD Chemistryen
dc.titleQuestions in the chemical enzymology of MAOen
dc.typeJournal itemen
dc.description.versionPublisher PDFen
dc.contributor.institutionUniversity of St Andrews. School of Biologyen
dc.description.statusPeer revieweden

This item appears in the following Collection(s)

Show simple item record