Synthesis and tryptic hydrolysis of p-guanidinophenyl esters derived from amino acids and peptides.
A facile synthetic method for p-guanidinophenyl esters derived from a variety of amino acids and peptides, including D-amino acids, is presented. The kinetic behavior of trypsin towards these synthetic esters, inverse substrates, was analyzed. The spatial requirement of the enzyme active site for catalytic efficiency is discussed based on the steric characteristics of the substrates.
Sekizaki
H
H
Faculty of Pharmaceutical Sciences, Health Sciences University of Hokkaido, Japan.
Itoh
K
K
Toyota
E
E
Tanizawa
K
K
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000138:chemical synthesis / Q000737:chemistry*; D004952:Esters / Q000138:chemical synthesis / Q000737:chemistry*; D006146:Guanidines / Q000138:chemical synthesis / Q000737:chemistry*; D006868:Hydrolysis; D007700:Kinetics; D008969:Molecular Sequence Data; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry*; D011487:Protein Conformation; D013237:Stereoisomerism; D014357:Trypsin / Q000737:chemistry
D000596:Amino Acids; D004952:Esters; D006146:Guanidines; D010455:Peptides; D014357:Trypsin