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Carbonic anhydrase and acetylcholinesterase inhibitory effects of carbamates and sulfamoylcarbamates.
J Enzyme Inhib Med Chem. 2015 Apr; 30(2):316-20.JE

Abstract

Carbonic anhydrases (CA), as a family of metalloenzymes, are found in almost every type of tissue and play an important role in catalyzing the equilibration of carbon dioxide and carbonic acid. In this study, a series of carbamate derivative was synthesized, and their inhibition effects on hCA I, hCA II and acetylcholinesterase (AChE) enzymes were investigated. They were determined to be very good inhibitor against for both isoenzymes (hCA I and hCA II) and AChE. The hCA I and hCA II were effectively inhibited by the carbamate derivatives, with inhibition constants (Ki) in the range of 194.4-893.5 nM (for hCA I) and 103.9-835.7 nM (for hCA II). On the other hand, Ki parameters of these compounds for AChE enzyme inhibition were determined in the range of 12.0-61.3 nM. The results clearly showed that both CA isoenzymes and AChE were inhibited by carbamate derivatives at the nM levels.

Authors+Show Affiliations

Central Researching Laboratory, Agri Ibrahim Cecen University , Agri , Turkey .No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article

Language

eng

PubMed ID

24964347

Citation

Göçer, Hülya, et al. "Carbonic Anhydrase and Acetylcholinesterase Inhibitory Effects of Carbamates and Sulfamoylcarbamates." Journal of Enzyme Inhibition and Medicinal Chemistry, vol. 30, no. 2, 2015, pp. 316-20.
Göçer H, Akincioğlu A, Göksu S, et al. Carbonic anhydrase and acetylcholinesterase inhibitory effects of carbamates and sulfamoylcarbamates. J Enzyme Inhib Med Chem. 2015;30(2):316-20.
Göçer, H., Akincioğlu, A., Göksu, S., Gülçin, İ., & Supuran, C. T. (2015). Carbonic anhydrase and acetylcholinesterase inhibitory effects of carbamates and sulfamoylcarbamates. Journal of Enzyme Inhibition and Medicinal Chemistry, 30(2), 316-20. https://doi.org/10.3109/14756366.2014.928704
Göçer H, et al. Carbonic Anhydrase and Acetylcholinesterase Inhibitory Effects of Carbamates and Sulfamoylcarbamates. J Enzyme Inhib Med Chem. 2015;30(2):316-20. PubMed PMID: 24964347.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Carbonic anhydrase and acetylcholinesterase inhibitory effects of carbamates and sulfamoylcarbamates. AU - Göçer,Hülya, AU - Akincioğlu,Akın, AU - Göksu,Süleyman, AU - Gülçin,İlhami, AU - Supuran,Claudiu T, Y1 - 2014/06/25/ PY - 2014/6/26/entrez PY - 2014/6/26/pubmed PY - 2016/1/13/medline KW - AChE KW - Acetylcholinesterase KW - CA KW - carbamates KW - carbonic anhydrase KW - enzyme inhibition SP - 316 EP - 20 JF - Journal of enzyme inhibition and medicinal chemistry JO - J Enzyme Inhib Med Chem VL - 30 IS - 2 N2 - Carbonic anhydrases (CA), as a family of metalloenzymes, are found in almost every type of tissue and play an important role in catalyzing the equilibration of carbon dioxide and carbonic acid. In this study, a series of carbamate derivative was synthesized, and their inhibition effects on hCA I, hCA II and acetylcholinesterase (AChE) enzymes were investigated. They were determined to be very good inhibitor against for both isoenzymes (hCA I and hCA II) and AChE. The hCA I and hCA II were effectively inhibited by the carbamate derivatives, with inhibition constants (Ki) in the range of 194.4-893.5 nM (for hCA I) and 103.9-835.7 nM (for hCA II). On the other hand, Ki parameters of these compounds for AChE enzyme inhibition were determined in the range of 12.0-61.3 nM. The results clearly showed that both CA isoenzymes and AChE were inhibited by carbamate derivatives at the nM levels. SN - 1475-6374 UR - https://www.unboundmedicine.com/medline/citation/24964347/Carbonic_anhydrase_and_acetylcholinesterase_inhibitory_effects_of_carbamates_and_sulfamoylcarbamates_ L2 - http://www.tandfonline.com/doi/full/10.3109/14756366.2014.928704 DB - PRIME DP - Unbound Medicine ER -