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Linear competitive inhibition of human tissue kallikrein by 4-aminobenzamidine and benzamidine and linear mixed inhibition by 4-nitroaniline and aniline BJMBR
Sousa,M.O.; Miranda,T.L.S.; Costa,E.B.; Bittar,E.R.; Santoro,M.M.; Figueiredo,A.F.S..
Hydrolysis of D-valyl-L-leucyl-L-arginine p-nitroanilide (7.5-90.0 µM) by human tissue kallikrein (hK1) (4.58-5.27 nM) at pH 9.0 and 37ºC was studied in the absence and in the presence of increasing concentrations of 4-aminobenzamidine (96-576 µM), benzamidine (1.27-7.62 mM), 4-nitroaniline (16.5-66 µM) and aniline (20-50 mM). The kinetic parameters determined in the absence of inhibitors were: Km = 12.0 ± 0.8 µM and k cat = 48.4 ± 1.0 min-1. The data indicate that the inhibition of hK1 by 4-aminobenzamidine and benzamidine is linear competitive, while the inhibition by 4-nitroaniline and aniline is linear mixed, with the inhibitor being able to bind both to the free enzyme with a dissociation constant Ki yielding an EI complex, and to the ES complex with...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Kinetics of human tissue kallikrein inhibition; Tissue kallikrein; 4-nitroaniline; Aniline; Benzamidine; 4-aminobenzamidine; Enzyme inhibition.
Ano: 2001 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2001000100004
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Thermodynamic evaluation and modeling of proton and water exchange associated with benzamidine and berenil binding to ß-trypsin BJMBR
Pereira,M.T.; Silva-Alves,J.M.; Martins-José,A.; Lopes,J.C.D.; Santoro,M.M..
Serine-proteases are involved in vital processes in virtually all species. They are important targets for researchers studying the relationships between protein structure and activity, for the rational design of new pharmaceuticals. Trypsin was used as a model to assess a possible differential contribution of hydration water to the binding of two synthetic inhibitors. Thermodynamic parameters for the association of bovine ß-trypsin (homogeneous material, observed 23,294.4 ± 0.2 Da, theoretical 23,292.5 Da) with the inhibitors benzamidine and berenil at pH 8.0, 25ºC and with 25 mM CaCl2, were determined using isothermal titration calorimetry and the osmotic stress method. The association constant for berenil was about 12 times higher compared to the one for...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Benzamidine; Berenil; Calorimetry; Protein modeling; Trypsin; Osmotic stress.
Ano: 2005 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2005001100005
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