Unknown

Dataset Information

0

Kinetics and mechanism of catalysis by proteolytic enzymes. A comparison of the kinetics of hydrolysis of synthetic substrates by bovine alpha- and beta-trypsin.


ABSTRACT: Several esters of the alpha-N-toluene-p-sulphonyl and alpha-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 alpha-N-toluene-p-sulphonyl and alpha-N-benzoyl derivatives of l-arginine, l-lysine, S-(2-aminoethyl)-l-cysteine and esters of gamma-guanidino-l-alpha-toluene-p-sulphonamidobutyric acid and alpha-N-toluene-p-sulphonyl-l-homoarginine by alpha- and beta-trypsin were compared. On the basis of values of the specificity constants (k(cat.)/K(m)), the two enzymes display similar catalytic efficiency towards some substrates. In other cases alpha-trypsin is less efficient than beta-trypsin. It is possible that alpha-trypsin possesses greater molecular flexibility than beta-trypsin.

SUBMITTER: Roberts DV 

PROVIDER: S-EPMC1168109 | biostudies-other | 1974 Aug

REPOSITORIES: biostudies-other

Similar Datasets

| S-EPMC1270320 | biostudies-other
| S-EPMC1207211 | biostudies-other
| S-EPMC3964991 | biostudies-literature
| S-EPMC4702814 | biostudies-literature
| S-EPMC1154347 | biostudies-other
| S-EPMC1177769 | biostudies-other
| S-EPMC1152404 | biostudies-other
| S-EPMC4678819 | biostudies-literature
| S-EPMC1302179 | biostudies-other
| S-EPMC4081944 | biostudies-literature