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

被引：31

作者：

Edmondson, D. E.

DeColibus, L.

Binda, C.

Li, M.

Mattevi, A.

机构：

[1] Emory Univ, Sch Med, Dept Biochem, Atlanta, GA 30322 USA

[2] Emory Univ, Dept Chem, Atlanta, GA 30322 USA

[3] Univ Pavia, Dept Genet & Microbiol, I-27100 Pavia, Italy

来源：

JOURNAL OF NEURAL TRANSMISSION | 2007年 / 114卷 / 06期

关键词：

X-ray crystal structures; human MAO-A; human MAO-B; rat MAO-A;

D O I：

10.1007/s00702-007-0674-z

中图分类号：

R74 [神经病学与精神病学];

学科分类号：

摘要：

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.

引用

收藏

页码：703 / 705

页数：3

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