scholarly journals Kinetics and mechanism of catalysis by proteolytic enzymes: The kinetics of hydrolysis of derivatives of l-lysine and S-(β-aminoethyl)-l-cysteine(thialysine)by bovine trypsin

1967 ◽  
Vol 102 (3) ◽  
pp. 728-734 ◽  
Author(s):  
D. T. Elmore ◽  
D. V. Roberts ◽  
J.J. Smyth
Keyword(s):  
Amino Acids ◽  
Proteolytic Enzymes ◽  
Kinetics And Mechanism ◽  
Kinetics Of Hydrolysis ◽  
Bovine Trypsin ◽  
Mechanism Of Catalysis ◽  
Kinetics Of ◽  
Hydrolysis Of ◽  
Derivatives Of

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.

scholarly journals Kinetics and mechanism of catalysis by proteolytic enzymes. A comparison of the kinetics of hydrolysis of synthetic substrates by bovine α- and β-trypsin

1974 ◽  
Vol 141 (2) ◽  
pp. 545-554 ◽  
Author(s):  
D. V. Roberts ◽  
D. T. Elmore
Keyword(s):  
Methyl Ester ◽  
Proteolytic Enzymes ◽  
Catalytic Efficiency ◽  
Kinetics And Mechanism ◽  
Molecular Flexibility ◽  
Kinetics Of Hydrolysis ◽  
Mechanism Of Catalysis ◽  
Kinetics Of ◽  
Hydrolysis Of ◽  
Derivatives Of

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.

Kinetics of hydrolysis of acetyl, valeroyl and nicotinoyl acyl derivatives of stobadine

Life Sciences ◽  
1999 ◽  
Vol 65 (18-19) ◽  
pp. 2007-2010 ◽  
Author(s):  
M. Stankovičová ◽  
Ž. Bezáková ◽  
L. Beneš
Keyword(s):  
Kinetics Of Hydrolysis ◽  
Kinetics Of ◽  
Hydrolysis Of ◽  
Derivatives Of ◽  
Acyl Derivatives

scholarly journals Factors Influencing the Acid Lability of Substituted Arylsulphonyl Arginine Protecting Groups

1994 ◽  
Vol 49 (10) ◽  
pp. 1425-1433 ◽  
Author(s):  
Syed Safdar Ali ◽  
Hartmut Echner ◽  
Khalid Mohammed Khan ◽  
Christoph Schröder ◽  
Mashooda Hasan ◽  
...  
Keyword(s):  
Protecting Groups ◽  
Tert Butyl ◽  
Factors Influencing ◽  
Kinetics Of Hydrolysis ◽  
Alkyl Groups ◽  
Kinetics Of ◽  
Hydrolysis Of ◽  
Derivatives Of

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.

scholarly journals Complex formation reactions of palladium(II)-1,3-diaminopropane with various biologically relevant ligands. Kinetics of hydrolysis of glycine methyl ester through complex formation

2010 ◽  
Vol 8 (4) ◽  
pp. 919-927 ◽  
Author(s):  
Ahmed El-Sherif ◽  
Mohamed Shoukry ◽  
Ramadan El-Bahnasawy ◽  
Dalia Ahmed
Keyword(s):  
Amino Acids ◽  
Ionic Strength ◽  
Methyl Ester ◽  
Complex Formation ◽  
Dicarboxylic Acids ◽  
Dna Constituents ◽  
Kinetics Of Hydrolysis ◽  
Glycine Methyl Ester ◽  
Kinetics Of ◽  
Hydrolysis Of

AbstractThe interaction of [Pd(DAP)(H2O)2]2+ (DAP = 1,3-diaminopropane) with some selected bio-relevant ligands, containing different functional groups, were investigated. The ligands used are dicarboxylic acids, amino acids, peptides and DNA constituents. Stoichiometry and stability constants of the complexes formed are reported at 25°C and 0.1 M ionic strength. The results show the formation of 1:1 complexes with amino acids and dicarboxylic acids. The effect of chelate ring size of the dicarboxylic acid complexes on their stability constants is examined. Peptides form both 1:1 complexes and the corresponding deprotonated amide species. DNA constituents form 1:1 and 1:2 complexes. The effect of dioxane on the acid dissociation constants of CBDCA and the formation constant of its complex with Pd(DAP)2+ was reported. The kinetics of hydrolysis of glycine methyl ester bound to [Pd(DAP)(H2O)2]2+ was studied at 25°C and 0.1M ionic strength.

Sign in / Sign up

Export Citation Format

Share Document