Kinetics of hydrolysis of peptide thioester derivatives of arginine by human and bovine thrombins

1984 ◽  
Vol 234 (1) ◽  
pp. 82-88 ◽  
Author(s):  
Robert R. Cook ◽  
Brian J. McRae ◽  
James C. Powers
Life Sciences ◽  
1999 ◽  
Vol 65 (18-19) ◽  
pp. 2007-2010 ◽  
Author(s):  
M. Stankovičová ◽  
Ž. Bezáková ◽  
L. Beneš

1974 ◽  
Vol 141 (2) ◽  
pp. 545-554 ◽  
Author(s):  
D. V. Roberts ◽  
D. T. Elmore

Several esters of the α-N-toluene-p-sulphonyl and α-N-benzoyl derivatives of S-(3-aminopropyl)-l-cysteine and the methyl ester of S-(4-aminobutyl)-N-toluene-p-sulphonyl-l-cysteine were synthesized. The kinetics of hydrolysis of these and esters of the α-N-toluene-p-sulphonyl and α-N-benzoyl derivatives of l-arginine, l-lysine, S-(2-aminoethyl)-l-cysteine and esters of γ-guanidino-l-α-toluene-p-sulphonamidobutyric acid and α-N-toluene-p-sulphonyl-l-homoarginine by α- and β-trypsin were compared. On the basis of values of the specificity constants (kcat./Km), the two enzymes display similar catalytic efficiency towards some substrates. In other cases α-trypsin is less efficient than β-trypsin. It is possible that α-trypsin possesses greater molecular flexibility than β-trypsin.


1994 ◽  
Vol 49 (10) ◽  
pp. 1425-1433 ◽  
Author(s):  
Syed Safdar Ali ◽  
Hartmut Echner ◽  
Khalid Mohammed Khan ◽  
Christoph Schröder ◽  
Mashooda Hasan ◽  
...  

AbstractThe kinetics of hydrolysis of new, NG-protected 2,4,6-triisopropylbenzene-sulphonyl (6). 4-methoxy-3,5-di-tert-butylbenzenesulphonyl (12) and phenanthrene-3-sulphonyl (17) Fmoc derivatives of L-arginine (1) in comparison with commercially available Fmoc-Arg(Mtr)-OH (Mtr = 4-methoxy-2,3,6-trimethyl-benzenesulphonyl (2)) are studies. The acid lability of the arylsulphonyl group is decreasing as follows Mtr > Tip > Mtbs > Phen. The effect of electron- donating alkyl groups as substituents in increasing the acid lability of the arylsulphonyl residue seems to be in the order of methyl > isopropyl > tert-butyl while the effect of extended derealization does not appreciably increase the acid lability.


1967 ◽  
Vol 102 (3) ◽  
pp. 728-734 ◽  
Author(s):  
D. T. Elmore ◽  
D. V. Roberts ◽  
J.J. Smyth

1. Several esters of the alpha-N-toluene-p-sulphonyl and N-benzoyl derivatives of l-lysine and S-(beta-aminoethyl)-l-cysteine have been synthesized. 2. The kinetics of hydrolysis of the esters by bovine trypsin have been compared. Values of k(0) are similar for corresponding derivatives of the isosteric amino acids and deacylation of an acyl-enzyme appears to be rate-determining in each case. There are, however, some quantitative kinetic differences between the various series of substrates.


1981 ◽  
Vol 46 (5) ◽  
pp. 1229-1236 ◽  
Author(s):  
Jan Balej ◽  
Milada Thumová

The rate of hydrolysis of S2O82- ions in acidic medium to peroxomonosulphuric acid was measured at 20 and 30 °C. The composition of the starting solution corresponded to the anolyte flowing out from an electrolyser for production of this acid or its ammonium salt at various degrees of conversion and starting molar ratios of sulphuric acid to ammonium sulphate. The measured data served to calculate the rate constants at both temperatures on the basis of the earlier proposed mechanism of the hydrolysis, and their dependence on the ionic strength was studied.


1986 ◽  
Vol 51 (12) ◽  
pp. 2786-2797
Author(s):  
František Grambal ◽  
Jan Lasovský

Kinetics of formation of 1,2,4-oxadiazoles from 24 substitution derivatives of O-benzoylbenzamidoxime have been studied in sulphuric acid and aqueous ethanol media. It has been found that this medium requires introduction of the Hammett H0 function instead of the pH scale beginning as low as from 0.1% solutions of mineral acids. Effects of the acid concentration, ionic strength, and temperature on the reaction rate and on the kinetic isotope effect have been followed. From these dependences and from polar effects of substituents it was concluded that along with the cyclization to 1,2,4-oxadiazoles there proceeds hydrolysis to benzamidoxime and benzoic acid. The reaction is thermodynamically controlled by the acid-base equilibrium of the O-benzylated benzamidoximes.


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