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

页码：703 / 705

页数：3

共 9 条

[1] Positive selection in MAOA gene is human exclusive:: determination of the putative amino acid change selected in the human lineage
Andrés, AM
Soldevila, M
Navarro, A
Kidd, KK
Oliva, B
Bertranpetit, J
[J]. HUMAN GENETICS, 2004, 115 (05) : 377 - 386
[2] Structure of human monoamine oxidase B, a drug target for the treatment of neurological disorders
Binda, C
Newton-Vinson, P
Hubálek, F
Edmondson, DE
Mattevi, A
[J]. NATURE STRUCTURAL BIOLOGY, 2002, 9 (01) : 22 - 26
[3] Insights into the mode of inhibition of human mitochondrial monoamine oxidase B from high-resolution crystal structures
Binda, C
Li, M
Hubálek, F
Restelli, N
Edmondson, DE
Mattevi, A
[J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2003, 100 (17) : 9750 - 9755
[4] Three-dimensional structure of human monoamine oxidase A (MAO A): Relation to the structures of rat MAO A and human MAO B
De Colibus, L
Li, M
Binda, C
Lustig, A
Edmondson, DE
Mattevi, A
[J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2005, 102 (36) : 12684 - 12689
[5] Demonstration of isoleucine 199 as a structural determinant for the selective inhibition of human monoamine oxidase B by specific reversible inhibitors
Hubálek, F
Binda, C
Khalil, A
Li, M
Mattevi, A
Castagnoli, N
Edmondson, DE
[J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2005, 280 (16) : 15761 - 15766
[6] High-level expression of human liver monoamine oxidase a in Pichia pastoris:: Comparison with the enzyme expressed in Saccharomyces cerevisiae
Li, M
Hubálek, F
Newton-Vinson, P
Edmondson, DE
[J]. PROTEIN EXPRESSION AND PURIFICATION, 2002, 24 (01) : 152 - 162
[7] Structure of rat monoamine oxidase A and its specific recognitions for substrates and inhibitors
Ma, JC
Yoshimura, M
Yamashita, E
Nakagawa, A
Ito, A
Tsukihara, T
[J]. JOURNAL OF MOLECULAR BIOLOGY, 2004, 338 (01) : 103 - 114
[8] High-level expression of human liver monoamine oxidase B in Pichia pastoris
Newton-Vinson, P
Hubalek, F
Edmondson, DE
[J]. PROTEIN EXPRESSION AND PURIFICATION, 2000, 20 (02) : 334 - 345
[9] Do monomeric vs dimeric forms of MAO-A make a difference?: A direct comparison of the catalytic properties of rat and human MAO-A's
Wang, J.
Edmondson, D. E.
[J]. JOURNAL OF NEURAL TRANSMISSION, 2007, 114 (06) : 721 - 724

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