Final answer:
The phenomenon described in the question is an example of irreversible inhibition, where an inhibitor binds covalently to the active site of an enzyme.
Step-by-step explanation:
The phenomenon described in the question is an example of irreversible inhibition.
Irreversible inhibition occurs when an inhibitor binds covalently to the active site of an enzyme, rendering the enzyme permanently inactive. In the case of Phenyl-methane-sulfonyl-fluoride (PMSF), it inactivates serine proteases by covalently bonding to the catalytic serine residue at the active site, and this bond is not cleaved by the enzyme.
Examples of irreversible inhibitors include iodoacetate, which permanently inhibits aldolase, and di-isopropylflurophosphate (DFP), a component of nerve gas that permanently inhibits most digestive enzymes in humans.