3.4.22.43 additional information - additional information - 667305 3.4.22.43 additional information - additional information presence of DNA reduces the turnover rate up to 50% indicating that the binding of DNA changes the active site of cathepsin V such that the enzyme interacts with peptide substrates differently 683662 3.4.22.43 0.6 - 2-aminobenzoyl-ELKLQ-N-(2,4-dinitrophenyl)ethylenediamine recombinant enzyme, pH 5.5, 37°C 667305 3.4.22.43 0.9 - 2-aminobenzoyl-KLRVSKQ-N-(2,4-dinitrophenyl)ethylenediamine recombinant enzyme, pH 5.5, 37°C 667305 3.4.22.43 1.3 - 2-aminobenzoyl-EE-epsilon-amino-caproic acid-ELKLQ-N-(2,4-dinitrophenyl)ethylenediamine recombinant enzyme, pH 5.5, 37°C 667305 3.4.22.43 1.3 - 2-aminobenzoyl-KLRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine recombinant enzyme, pH 5.5, 37°C 667305 3.4.22.43 1.5 - 2-aminobenzoyl-KLRSIKQ-N-(2,4-dinitrophenyl)ethylenediamine recombinant enzyme, pH 5.5, 37°C 667305 3.4.22.43 1.7 - 2-aminobenzoyl-KK-epsilon-amino-caproic acid-ELKLQ-N-(2,4-dinitrophenyl)ethylenediamine recombinant enzyme, pH 5.5, 37°C 667305 3.4.22.43 3.4 - Z-Phe-Arg-4-methyl-7-coumaryl amide recombinant enzyme, pH 5.5, 25°C 669257 3.4.22.43 3.7 - Z-Phe-Arg-4-methyl-7-coumaryl amide recombinant enzyme, pH 5.5, 25°C, in presence of 0.3 M NaCl 669257