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

Akyuz M. A., Erdem S., Edmondson D. E.

JOURNAL OF NEURAL TRANSMISSION, cilt.114, sa.6, ss.693-698, 2007 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 114 Sayı: 6
  • Basım Tarihi: 2007
  • Doi Numarası: 10.1007/s00702-007-0670-3
  • Dergi Adı: JOURNAL OF NEURAL TRANSMISSION
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.693-698
  • Anahtar Kelimeler: ONIOM calculations, neurotransmitter, FAD binding site, enzyme modeling, OXIDATION, MUTANT
  • Marmara Üniversitesi Adresli: Evet

Özet

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.