Answer
Some membrane proteins are anchored to the membrane by the attachment of hydrophobic parts such as myristic acid (a 14-carbon saturated fatty acid) to the N terminal Gly of proteins. These proteins play important roles in a wide variety of functions and cellular signal transduction pathways. Cleavage of the polypeptide backbones next to the N-terminal Gly by the Shigella enzyme would disrupt the interaction of the myristoylated protein with the membrane, thus altering its function.
Work Step by Step
Some membrane proteins are anchored to the membrane by the attachment of hydrophobic parts such as myristic acid (a 14-carbon saturated fatty acid) to the N terminal Gly of proteins. These proteins play important roles in a wide variety of functions and cellular signal transduction pathways. Cleavage of the polypeptide backbones next to the N-terminal Gly by the Shigella enzyme would disrupt the interaction of the myristoylated protein with the membrane, thus altering its function.
