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.

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.

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 The kinetics of hydrolysis of some extended N-aminoacyl-l-arginine methyl esters by porcine pancreatic kallikrein. A comparison with human plasma Kallikrein

1982 ◽  
Vol 203 (1) ◽  
pp. 299-302 ◽  
Author(s):  
P R Levison ◽  
G Tomalin
Keyword(s):  
Human Plasma ◽  
Methyl Esters ◽  
Catalytic Efficiency ◽  
Plasma Kallikrein ◽  
Kinetics Of Hydrolysis ◽  
Relative Differences ◽  
Rate Limiting ◽  
Kinetics Of ◽  
Hydrolysis Of ◽  
Limiting Values

The effects of subsite interactions in the S2-S4 region [Schechter & Berger (1967) Biochem. Biophys. Res. Commun. 27, 157-162] of porcine pancreatic kallikrein (EC 3.4.21.8) on its catalytic efficiency have been investigated. Kinetic constants (Kcat, Km) have been determined for a series of seven extended N-aminoacyl-L-arginine methyl esters whose sequence is based on either the C-terminal sequence of kallidin (-Pro-Phe-Arg) or (-Gly-)nArg. With these substrates it has been found that neither acylation nor deacylation of the enzyme is rate-limiting. Values of Kcat. range from 21.5 to 2320s-1, indicating that there are interactions with different residues in the N-aminoacyl chain and enzyme subsites in the S2-S4 region. It is shown that possible hydrogen-bonded interactions with the enzyme in the S3-S4 region have a significant effect on catalysis. The presence of L-phenylalanine at P2 has a very large effect on both Kcat, and Km, giving a greatly enhanced catalytic efficiency. Substrates with L-proline at P3 also have a marked effect, but in this case the overall effect is one of lowered catalytic efficiency. By comparison with the results of a similar study with human plasma kallikrein I (EC 3.4.21.8), it has been possible to demonstrate that there are considerable differences in kinetic behaviour between the two enzymes. These are related to relative differences in the rates of acylation and deacylation with ester substrates and also the roles of subsites S2 and S3 of the two enzymes.

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.

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