Final answer:
The enzyme aldolase is inhibited by iodoacetate, which causes permanent inactivation by binding irreversibly to the enzyme's active site. Aldolase is involved in glycolysis, and its inhibition affects the breakdown of glucose for energy. Hexokinase, on the other hand, is not inhibited by iodoacetate but is affected by other inhibitors.
Step-by-step explanation:
The enzyme inhibited by iodoacetate is aldolase. Iodoacetate is known to permanently inactivate aldolase by modifying its essential thiol (–SH) groups. This reaction is an example of irreversible enzyme inhibition, as the inhibitor binds permanently to the enzyme, rendering it inactive and unable to catalyze its normal reaction.
Hexokinase is another enzyme that is affected by certain inhibitors such as para chloro-mercuric benzoate (PCMB), but it is not inhibited by iodoacetate. Hexokinase catalyzes a biologically irreversible reaction, the phosphorylation of glucose, using ATP as a phosphate donor, forming glucose-6-phosphate which cannot cross the plasma membrane easily. This is an important step in glycolysis and cell energy production.