Succinylcholine ine is structurally almost identical to acetylcholine, but if combined with the enzyme that normally hydrolyzes acetylcholine,the enzyme is no longer able to hydrolyze acetylcholine. This suppests that __ succinylcholine must be a noncompetitive inhibitor succinylcholine must be a competitive inhibitor of acetylcholine succinylcholine must regulate the activity of this enzyme by negative feedback the active site must have the wrong configuration to permit succinylcholine binding

## Step 1<br />The problem involves understanding the concept of enzyme inhibition, specifically competitive inhibition. In competitive inhibition, a substance (in this case, succinylcholine) competes with the normal substrate (acetylcholine) for the active site of the enzyme. <br /><br />## Step 2<br />The fact that succinylcholine is structurally almost identical to acetylcholine suggests that it can bind to the active site of the enzyme, preventing acetylcholine from binding. This is a characteristic of competitive inhibition.<br /><br />## Step 3<br />The fact that the enzyme is no longer able to hydrolyze acetylcholine when succinylcholine is present further supports the idea of competitive inhibition. This is because the presence of succinylcholine is blocking the active site, preventing acetylcholine from being hydrolyzed.