The unique substrate specificity of human AOC2, a semicarbazide-sensitive amine oxidase
| Autor: | Kati Elima, Heidi Kidron, Janne Liukkonen, Sirpa Jalkanen, Kirsi Grön, Tiina A. Salminen, Sam Kaitaniemi, Marko Salmi, Heli Elovaara |
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| Rok vydání: | 2009 |
| Předmět: |
Models
Molecular Tryptamine AOC3 Tyramine Eye Substrate Specificity Cellular and Molecular Neuroscience chemistry.chemical_compound Benzylamine Phenethylamines Humans RNA Messenger Cloning Molecular Eye Proteins Molecular Biology Pharmacology chemistry.chemical_classification Oxidoreductases Acting on CH-NH Group Donors biology Methylamine Oxidative deamination Cell Biology Tryptamines Enzyme assay Protein Structure Tertiary Kinetics Enzyme chemistry Biochemistry Mutagenesis Site-Directed biology.protein Molecular Medicine Amine gas treating Amine Oxidase (Copper-Containing) Cell Adhesion Molecules Dimerization |
| Zdroj: | Cellular and Molecular Life Sciences. 66:2743-2757 |
| ISSN: | 1420-9071 1420-682X |
| DOI: | 10.1007/s00018-009-0076-5 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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