The aromatic cage in the active site of monoamine oxidase B: effect on the structural and electronic properties of bound benzylamine and p-nitrobenzylamine

Computational studies using the ONIOM methods have been performed to probe the catalytic roles of tyrosine residues 398 and 435 which constitute the "aromatic cage" in the active site of MAO-B. The results presented here provide additional new insights into the interactions that take place...

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Bibliographic Details
Published inJournal of Neural Transmission Vol. 114; no. 6; pp. 693 - 698
Main Authors Akyüz, M A, Erdem, S S, Edmondson, D E
Format Journal Article
LanguageEnglish
Published Austria Springer Nature B.V 01.06.2007
Subjects
Amino Acids, Aromatic - chemistry
Animals
Benzylamines - chemistry
Catalytic Domain
Electrons
Humans
Models, Molecular
Molecular Structure
Monoamine Oxidase - chemistry
Nitrates - chemistry
Nitro Compounds - chemistry
Tyrosine - chemistry
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Summary:Computational studies using the ONIOM methods have been performed to probe the catalytic roles of tyrosine residues 398 and 435 which constitute the "aromatic cage" in the active site of MAO-B. The results presented here provide additional new insights into the interactions that take place on activation of the amine substrate by the aromatic cage residues in MAO-B catalysis and have relevance to the MAO-A catalytic mechanism.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
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ISSN:0300-9564
1435-1463
DOI:10.1007/s00702-007-0670-3