98200-56-7Relevant academic research and scientific papers
SPECIFIC WATER-SOLUBLE SUBSTRATES FOR CHYMOTRYPSIN: ATTEMPTS FOR COMPENSATING DIMINISHED P1-S1 INTERACTION
Schellenberger, Volker,Schellenberger, Ute,Jakubke, Hans-Dieter
, p. 2884 - 2889 (2007/10/02)
N-Maleyl-L-amino acid and peptide esters were synthesized and employed as substrates for α-chymotrypsin.From the kcat/KM values can be suggested that benzyl esters are significantly better substrates than the appropriate methyl esters.Further improvement in the substrate properties results from the introduction of the p-nitrobenzyl ester moiety.The choline ester of benzyloxycarbonyl-L-phenylalanine with the highest kcat/KM value confirmed the P'1 leaving group specifity for positively charged residues.From the kinetic data can be concluded that acyl donors with high kcat/KM values, which are useful in kinetically controlled enzymatic peptide synthesis, need not contain aromatic amino acid residue in the P1 position.
