Document Detail


New insights into the structures and functions of human monoamine oxidases A and B.
MedLine Citation:
PMID:  17393064     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
D E Edmondson; L DeColibus; C Binda; M Li; A Mattevi
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Publication Detail:
Type:  Comparative Study; Journal Article     Date:  2007-03-29
Journal Detail:
Title:  Journal of neural transmission (Vienna, Austria : 1996)     Volume:  114     ISSN:  0300-9564     ISO Abbreviation:  J Neural Transm     Publication Date:  2007  
Date Detail:
Created Date:  2007-05-23     Completed Date:  2007-11-28     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9702341     Medline TA:  J Neural Transm     Country:  Austria    
Other Details:
Languages:  eng     Pagination:  703-5     Citation Subset:  IM    
Affiliation:
Department of Biochemistry and Chemistry, Emory University, Atlanta, GA 30322, USA. deedmon@emory.edu
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence / physiology
Animals
Binding Sites / physiology
Dimerization
Flavin-Adenine Dinucleotide / chemistry,  metabolism
Humans
Models, Molecular
Monoamine Oxidase / chemistry*,  metabolism
Nanoparticles / chemistry
Protein Conformation
Protein Structure, Tertiary / physiology
Rats
Recombinant Proteins / chemistry,  metabolism
Species Specificity
Chemical
Reg. No./Substance:
0/Recombinant Proteins; 146-14-5/Flavin-Adenine Dinucleotide; EC 1.4.3.4/Monoamine Oxidase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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