PROTEOLYTIC-ENZYMES .8. TRYPTIC HYDROLYSIS OF OMEGA-AMIDINO ALPHA-AMINO-ACID (INDOSPECINE) ESTERS
- 1 January 1980
- journal article
- research article
- Vol. 87 (4) , 1229-1234
Abstract
Several esters of a series of .omega.-amidino .alpha.-amino acids were synthesized. Some were efficiently hydrolyzed by bovine trypsin [EC 3.4.21.4]. The kinetics of hydrolysis of the esters were compared with those of the .omega.-guanidino series. The relationships between length of the side chain and the susceptibility to hydrolysis by trypsin were different in the 2 series. These slight differences are discussed in terms of the molecular structures and their relation to the structural requirements of the trypsin active site.This publication has 3 references indexed in Scilit:
- The interaction of α-N-(p-toluenesulphonyl)-p-guanidino-L-phenylalanine methyl ester with thrombin and trypsinBiochemical Journal, 1978
- 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 trypsinBiochemical Journal, 1967
- Kinetics and mechanism of catalysis by proteolytic enzymes. The kinetics of hydrolysis of esters of γ-guanidino-l-α-toluene-p-sulphonamidobutyric acid by bovine trypsin and thrombinBiochemical Journal, 1965