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 on activation of the amine substrate by the aromatic cage residues in MAO-B catalysis and have relevance to the MAO-A catalytic mechanism.
Akyüz
M A
MA
Department of Chemistry, Faculty of Arts and Sciences, Marmara University, Göztepe, Istanbul, Turkey.
Erdem
S S
SS
Edmondson
D E
DE
D024322:Amino Acids, Aromatic / Q000737:chemistry; D000818:Animals; D001596:Benzylamines / Q000737:chemistry*; D020134:Catalytic Domain; D004583:Electrons; D006801:Humans; D008958:Models, Molecular; D015394:Molecular Structure; D008995:Monoamine Oxidase / Q000737:chemistry*; D009566:Nitrates / Q000737:chemistry; D009574:Nitro Compounds / Q000737:chemistry; D014443:Tyrosine / Q000737:chemistry
D024322:Amino Acids, Aromatic; D001596:Benzylamines; D009566:Nitrates; D009574:Nitro Compounds; D014443:Tyrosine; C048768:4-nitrobenzylamine; C030796:benzylamine; D008995:Monoamine Oxidase