Comparative Study
[Comparative study of hydrolysis of methyl esters of N-arylsulfonyl-valyl-arginine by thrombin and trypsin]
[Article in
Russian]
- PMID: 35247
Item in Clipboard
Comparative Study
[Comparative study of hydrolysis of methyl esters of N-arylsulfonyl-valyl-arginine by thrombin and trypsin]
[Article in
Russian]
Biokhimiia.
1979 Apr.
Abstract
The esterase action of thrombin and trypsin on N-arylsulfonyl-valyl-arginine methyl esters was studied. The values of Km and kcat under steady-state conditions at pH 8,5 were determined. It was shown that the nature of the arylsulfonyl group does not affect the kinetic parameters of the reactions under study. The Michaelis constants of the thrombin-catalyzed reactions appeared to be one order of magnitude lower than the Km values of the corresponding TAME analogs.
Similar articles
-
[Dependence of thrombin- and trypsin-catalyzed hydrolysis of N-alpha-arylsulfonyl-L-arginine methyl esters on the structure of acylamide part of substrates].Biokhimiia. 1977 Sep;42(9):1595-602. Biokhimiia. 1977. PMID: 20997 Russian.
-
[Hydrolysis of the methyl esters of the N-arylsulfonyl derivatives of L-arginine by thrombin and trypsin].Biokhimiia. 1975 Jan-Feb;40(1):103-6. Biokhimiia. 1975. PMID: 166707 Russian.
-
[Hydrolysis of methyl esters of N alpha-arylsulfonyl-arginine and N-arylsulfonyl-valyl-arginine by alpha- and beta/gamma-thrombins].Biokhimiia. 1982 Apr;47(4):528-33. Biokhimiia. 1982. PMID: 7082687 Russian.
-
Nonconventional amide bond formation catalysis: programming enzyme specificity with substrate mimetics.Braz J Med Biol Res. 2000 May;33(5):469-85. doi: 10.1590/s0100-879x2000000500001. Braz J Med Biol Res. 2000. PMID: 10775878 Review.
-
[Development of "inverse substrates" for trypsin. Application to the studies on the structure and function of the enzyme and to the design for biologically active compounds].Yakugaku Zasshi. 1985 May;105(5):430-41. doi: 10.1248/yakushi1947.105.5_430. Yakugaku Zasshi. 1985. PMID: 3162015 Review. Japanese. No abstract available.