New insights into the structures and functions of human monoamine oxidases A and B

D. E. Edmondson, L. DeColibus, C. Binda, M. Li, A. Mattevi

Research output: Contribution to journalArticle

Abstract

Structural studies on recombinant human monoamine oxidase A (hMAO-A) provides interesting insights on comparison with that determined for human MAO-B (hMAO-B) as well as comparison with that previously published for rat MAO-A. The active site cavity of hMAO-A is monopartite (as with rat MAO-A) while hMAO-B is a bipartite cavity. hMAO-A crystallizes as a monomeric form, in contrast to the dimeric forms exhibited by hMAO-B and rat MAO-A. All of the known MAO structures show nearly identical geometries around the covalent FAD sites. Differences in active site cavity structures occur away from the FAD site through conformational alterations (MAO-A's) and by changes in amino acid residues (hMAO-A and hMAO-B). Differences observed between human and rat MAO-A's raise questions regarding the appropriateness of the rat model in the development of MAO-A specific inhibitors as drugs for eventual human use.

Original languageEnglish (US)
Pages (from-to)703-705
Number of pages3
JournalJournal of Neural Transmission
Volume114
Issue number6
DOIs
StatePublished - Jun 2007
Externally publishedYes

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Monoamine Oxidase
Flavin-Adenine Dinucleotide
Catalytic Domain
human monoamine oxidase A
Amino Acids

Keywords

  • Human MAO-A
  • Human MAO-B
  • Rat MAO-A
  • X-ray crystal structures

ASJC Scopus subject areas

  • Neuroscience(all)

Cite this

New insights into the structures and functions of human monoamine oxidases A and B. / Edmondson, D. E.; DeColibus, L.; Binda, C.; Li, M.; Mattevi, A.

In: Journal of Neural Transmission, Vol. 114, No. 6, 06.2007, p. 703-705.

Research output: Contribution to journalArticle

Edmondson, D. E. ; DeColibus, L. ; Binda, C. ; Li, M. ; Mattevi, A. / New insights into the structures and functions of human monoamine oxidases A and B. In: Journal of Neural Transmission. 2007 ; Vol. 114, No. 6. pp. 703-705.
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