Literature DB >> 25893707

Acetylcholinesterase and carbonic anhydrase isoenzymes I and II inhibition profiles of taxifolin.

Hulya Gocer1, Fevzi Topal2, Meryem Topal2, Murat Küçük3, Dilek Teke3, İlhami Gülçin3,4, Saleh H Alwasel4, Claudiu T Supuran5,6.   

Abstract

Taxifolin, also known as dihydroquercetin, is a flavonoid commonly found in plants. Carbonic anhydrase (CA, EC 4.2.1.1) plays an important role in many critical physiological events including carbon dioxide (CO2)/bicarbonate (HCO3(-)) respiration and pH regulation. There are 16 known CA isoforms in humans, of which human hCA isoenzymes I and II (hCA I and II) are ubiquitous cytosolic isoforms. In this study, the inhibition properties of taxifolin against the slow cytosolic isoenzyme hCA I, and the ubiquitous and dominant rapid cytosolic isoenzyme hCA II were studied. Taxifolin, as a naturally bioactive flavonoid, has a K(i) of 29.2 nM against hCA I, and 24.2 nM against hCA II. For acetylcholinesterase enzyme (AChE) inhibition, K(i) parameter of taxifolin was determined to be 16.7 nM. These results clearly show that taxifolin inhibited both CA isoenzymes and AChE at the nM levels.

Entities:  

Keywords:  Acetylcholinesterase; carbonic anhydrase; enzyme inhibition; enzyme purification; taxifolin

Mesh:

Substances:

Year:  2015        PMID: 25893707     DOI: 10.3109/14756366.2015.1036051

Source DB:  PubMed          Journal:  J Enzyme Inhib Med Chem        ISSN: 1475-6366            Impact factor:   5.051


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