thiourea and 4-nitrophenyl-acetate

thiourea has been researched along with 4-nitrophenyl-acetate* in 1 studies

Other Studies

1 other study(ies) available for thiourea and 4-nitrophenyl-acetate

Article	Year
Synthesis and biological activity of novel thiourea derivatives as carbonic anhydrase inhibitors. Journal of enzyme inhibition and medicinal chemistry, 2015, Volume: 30, Issue:1 A new series of chiral thiourea derivatives (5a-5c) and thiourea containing benzimidazole moieties (9b-9e) were synthesized from different amino acids (l-valine, l-isoleucine, l-methionine, l-phenylalanine, and d-phenylglycine). The compounds were characterized and tested against the two most studied members of the pH regulatory enzyme family, carbonic anhydrase (CA, EC 4.2.1.1). KI values of the novel compounds were measured in the range of 3.4-73.6 μM for hCA I isozyme and 8.7-1.44.2 μM for hCA II isozyme, respectively. Phenol was also tested as standard in order to understand the structure activity relationship and the clinically used sulfonamide acetazolamide was tested for comparison reasons. All of the compounds exhibited competitive inhibition with 4-nitrophenylacetate as substrate. Topics: Acetazolamide; Amino Acids; Benzimidazoles; Carbonic Anhydrase I; Carbonic Anhydrase II; Carbonic Anhydrase Inhibitors; Enzyme Assays; Humans; Kinetics; Nitrophenols; Phenol; Recombinant Proteins; Structure-Activity Relationship; Thiourea	2015

Article

Year

Synthesis and biological activity of novel thiourea derivatives as carbonic anhydrase inhibitors.

Journal of enzyme inhibition and medicinal chemistry, 2015, Volume: 30, Issue:1

A new series of chiral thiourea derivatives (5a-5c) and thiourea containing benzimidazole moieties (9b-9e) were synthesized from different amino acids (l-valine, l-isoleucine, l-methionine, l-phenylalanine, and d-phenylglycine). The compounds were characterized and tested against the two most studied members of the pH regulatory enzyme family, carbonic anhydrase (CA, EC 4.2.1.1). KI values of the novel compounds were measured in the range of 3.4-73.6 μM for hCA I isozyme and 8.7-1.44.2 μM for hCA II isozyme, respectively. Phenol was also tested as standard in order to understand the structure activity relationship and the clinically used sulfonamide acetazolamide was tested for comparison reasons. All of the compounds exhibited competitive inhibition with 4-nitrophenylacetate as substrate.

Topics: Acetazolamide; Amino Acids; Benzimidazoles; Carbonic Anhydrase I; Carbonic Anhydrase II; Carbonic Anhydrase Inhibitors; Enzyme Assays; Humans; Kinetics; Nitrophenols; Phenol; Recombinant Proteins; Structure-Activity Relationship; Thiourea

2015