CHM 4139 Lecture Notes - Lecture 11: Nucleophile, Covalent Bond, Ornithine Decarboxylase

• School: University of Ottawa
• Department: Chemistry
• Course: CHM 4139
• Professor: Roberto Chica

Document Summary

Irreversible inhibition: group-specific inhibition: in this type of inhibition chemical compounds that react with specific functional groups in the active site inactivate the enzyme by covalent modification of the side chain required for catalysis. These inhibitors are substrate analogues (structurally similar to the substrate) that contain a reactive electrophilic group to react with an active site nucleophile. Inhibitors react stoichiometrically with enzyme active sites. Inhibitors can also react with identical functional groups elsewhere on the protein, albeit with lower reactivity. 1: **suicide inhibition: in this type of inhibition, a substrate analogue binds to and is chemically modified by the enzyme. This reaction generates a reactive intermediate that inhibits the enzyme irreversibly. Thus, the enzyme creates the inhibitor via its catalytic activity. Criteria/conditions for suicide inhibition: inhibitor molecule is chemically inactive in the absence of the target enzyme, the inhibitor is activated specifically by its target enzyme. The goal of an enzyme assay is to detect enzymatic activity and quantify it.