Substrate-inhibitory analysis of monoamine oxidase from hepatopancreas of the octopus Bathypolypus arcticus
| Autor: | I. N. Basova, O. V. Yagodina |
|---|---|
| Rok vydání: | 2012 |
| Předmět: |
Tryptamine
chemistry.chemical_classification biology Physiology Stereochemistry Monoamine oxidase Bathypolypus arcticus Tyramine biology.organism_classification Biochemistry chemistry.chemical_compound Monoamine neurotransmitter Enzyme chemistry Hepatopancreas Diamine oxidase Ecology Evolution Behavior and Systematics |
| Zdroj: | Journal of Evolutionary Biochemistry and Physiology. 48:401-408 |
| ISSN: | 1608-3202 0022-0930 |
| DOI: | 10.1134/s0022093012040032 |
| Popis: | Study of the substrate-inhibitory specificity of mitochondrial monoamine oxidase (MAO) of hepatopancreas of the octopus Bathypolypus arcticus revealed distinctive peculiarities of catalytic properties of this enzyme. The studied enzyme, on one hand, like the classic MAO of homoiothermal animals, is able to deaminate tyramine, serotonin, benzylamine, tryptamine, b-phenylethylamine, while, on the other hand, it deaminates histamine and does not deaminate putrescine-classic substrates of diamine oxidase (DAO). Results of the substrate-inhibitory analysis with use of chlorgiline and deprenyl are indirect proofs for the existence in the octopus hepatopancreas of one molecular MAO form. Semicarbazide and pyronine G turned out to be weak irreversible inhibitors, four derivatives of acridine-irreversible inhibitors of the intermediate effectiveness with respect to the octopus hepatopancreas MAO; specificity of action of inhibitors at deamination of different substrates was equal. |
| Databáze: | OpenAIRE |
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