Gulcin_2015_J.Enzyme.Inhib.Med.Chem__1

Reference

Title : The effect of caffeic acid phenethyl ester (CAPE) on metabolic enzymes including acetylcholinesterase, butyrylcholinesterase, glutathione S-transferase, lactoperoxidase, and carbonic anhydrase isoenzymes I, II, IX, and XII - Gulcin_2015_J.Enzyme.Inhib.Med.Chem__1
Author(s) : Gulcin I , Scozzafava A , Supuran CT , Akincioglu H , Koksal Z , Turkan F , Alwasel S
Ref : J Enzyme Inhib Med Chem , :1 , 2015
Abstract : Caffeic acid phenethyl ester (CAPE) is an active component of honeybee propolis extracts. Carbonic anhydrases (CAs, EC 4.2.1.1) are widespread and intensively studied metalloenzymes present in higher vertebrates including humans as many diverse isoforms. Acetylcholinesterase (AChE) is responsible for acetyl choline (ACh) hydrolysis and plays a fundamental role in nerve impulse transmission by terminating the action of the ACh neurotransmitter at cholinergic synapses and neuromuscular junctions. Butyrylcholinesterase (BChE) is another enzyme abundantly present in the liver and released into blood in a soluble form. Lactoperoxidase (LPO) is an enzyme involved in fighting pathogenic microorganisms whereas glutathione S-transferases (GSTs) are dimeric proteins present both in prokaryotic and eukaryotic organisms and involved in cellular detoxification mechanisms. In the present study, the inhibition effect of CAPE on human carbonic anhydrase (hCA) isoforms I, II, IX, and XII, AChE, BChE, LPO, and GST was evaluated. CAPE inhibited these enzymes with Kis in the range between micromolar to picomolar. The best inhibitory effect was observed against AChE and BChE.
ESTHER : Gulcin_2015_J.Enzyme.Inhib.Med.Chem__1
PubMedSearch : Gulcin_2015_J.Enzyme.Inhib.Med.Chem__1
PubMedID: 26453427

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Citations formats

Gulcin I, Scozzafava A, Supuran CT, Akincioglu H, Koksal Z, Turkan F, Alwasel S (2015)
The effect of caffeic acid phenethyl ester (CAPE) on metabolic enzymes including acetylcholinesterase, butyrylcholinesterase, glutathione S-transferase, lactoperoxidase, and carbonic anhydrase isoenzymes I, II, IX, and XII
J Enzyme Inhib Med Chem :1

Gulcin I, Scozzafava A, Supuran CT, Akincioglu H, Koksal Z, Turkan F, Alwasel S (2015)
J Enzyme Inhib Med Chem :1