Chemical and Pharmaceutical Bulletin · 1996 · 33 citations · 0 references
Natural SciencesBiochemistryChemistryCatalysisEnzymologyOrganic ChemistryAmino Acid ChemistryCatalytic MechanismsEnzyme KineticsPeptide ChemistryProtein ChemistryProteolytic EnzymesAmino Acid EstersAmino AcidsCatalytic EfficiencyCatalytic SpecificityEnzyme Active Site DesignEnzyme Active Site MappingHydrolysisOrganic Substrates
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.