The unique substrate specificity of human AOC2, a semicarbazide-sensitive amine oxidase |
| |
Authors: | Sam Kaitaniemi Heli Elovaara Kirsi Grön Heidi Kidron Janne Liukkonen Tiina Salminen Marko Salmi Sirpa Jalkanen Kati Elima |
| |
Institution: | 1. MediCity Research Laboratory, University of Turku, and National Institute for Health and Welfare, Tykist?katu 6, 20520, Turku, Finland 2. Department of Biochemistry and Pharmacy, ?bo Akademi University, 20520, Turku, Finland 3. Department of Ophthalmology, Turku University Hospital, 20521, Turku, Finland
|
| |
Abstract: | Semicarbazide-sensitive amine oxidases (SSAOs) catalyze oxidative deamination of primary amines, but the true physiological
function of these enzymes is still poorly understood. Here, we have studied the functional and structural characteristics
of a human cell-surface SSAO, AOC2, which is homologous to the better characterized family member, AOC3. The preferred in
vitro substrates of AOC2 were found to be 2-phenylethylamine, tryptamine and p-tyramine instead of methylamine and benzylamine, the favored substrates of AOC3. Molecular modeling suggested structural
differences between AOC2 and AOC3, which provide AOC2 with the capability to use the larger monoamines as substrates. Even
though AOC2 mRNA was expressed in many tissues, the only tissues with detectable AOC2-like enzyme activity were found in the
eye. Characterization of AOC2 will help in evaluating the contribution of this enzyme to the pathological processes attributed
to the SSAO activity and in designing specific inhibitors for the individual members of the SSAO family.
Electronic supplementary material The online version of this article (doi:) contains supplementary material, which is available to authorized users. |
| |
Keywords: | SSAO AOC2 Retina Monoamine |
本文献已被 SpringerLink 等数据库收录! |
|