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Saturation Kinetics

Definition

Enzyme behaviour at substrate concentrations above the Km, where the rate of metabolism is constant rather than proportional to concentration. Ethanol saturates alcohol dehydrogenase at low millimolar concentrations, which is why an ethanol infusion blocks methanol metabolism.

Condition
Substrate concentration above the Km
Effect
Metabolism rate becomes constant, not proportional
Relevant enzyme
Alcohol dehydrogenase
Clinical application
Ethanol infusion blocks methanol metabolism

Common questions

Why does ethanol infusion work as an antidote for methanol poisoning based on this kinetics principle?+

Because ethanol has a much higher affinity for alcohol dehydrogenase than methanol does, administering enough ethanol saturates the enzyme with ethanol first, effectively blocking methanol from being converted into its more toxic metabolites like formic acid while the body clears the methanol unmetabolised.

How does saturation kinetics affect the interpretation of a blood alcohol concentration over time?+

Once ethanol concentration exceeds the level needed to saturate alcohol dehydrogenase, the body eliminates it at a roughly constant rate rather than a rate proportional to how much is present, which is the basis for the near-linear elimination curves used in back-calculation estimates.

Does saturation kinetics apply equally to all toxins metabolised by the same enzyme pathway?+

Only compounds that are substrates for the same saturable enzyme, such as methanol and ethylene glycol competing with ethanol at alcohol dehydrogenase, show this competitive blocking effect; toxins cleared by different pathways are unaffected by ethanol saturation.

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