116912-22-2Relevant articles and documents
Effect of enzyme-substrate interactions away from the reaction site on carboxypeptidase A catalysis
Sebastian, John F.,Liang, Guiqing,Jabarin, Annissa,Thomas, Karen,Wu, H. Bonnie
, p. 290 - 303 (2007/10/03)
The kinetics of 14 peptide substrates of carboxypeptidase A have been studied for the purpose of evaluating P1-P3/S1-S3 interactions. It was found that the amide group at P1-P2 is required
The Phenylacetyl (PhAc) Group as Enzymatically Removable Protecting Function for Peptides and Carbohydrates: Selective Deprotections with Penicillin Acylase
Waldmann, Herbert
, p. 1175 - 1180 (2007/10/02)
Using the modified carbodiimide procedure or EEDQ as coupling reagent, N-Phenylacetyl (PhAc) amino acids are condensed in good yields with amino acid methyl, benzyl, allyl, and tert-butyl esters to give totally protected dipeptides.The PhAc group is stabl