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substrate inhibition

Substrate inhibition is the inhibition of an enzymic reaction at high substrate levels, usually due to a second, inhibitory, and lower-affinity binding site for the substrate in addition to the catalytic site.

Substrate inhibition is the most common deviation from Michaelis–Menten kinetics, occurring in approximately 25% of known enzymes. It is generally attributed to forming an unproductive enzyme-substrate complex after the simultaneous binding of two or more substrate molecules to the active site. Substrate concentration affects the primary rate and yield of enzymatic hydrolysis. High substrate concentrations can result in substrate inhibition, significantly lowering the hydrolysis rate. Problems relating to heat and mass transfer efficiency reduction, rheological issues, and increased inhibitor concentration have been reported associated with high solid loading. The substrate inhibits the microbial growth rate at high substrate concentrations. As in enzyme kinetics, substrate inhibition of growth may be competitive or noncompetitive. Suppose a single-substrate enzyme-catalyzed reaction is a rate-limiting step in microbial growth. In that case, the inhibition of the enzyme activity results in the inhibition of microbial growth by the same pattern.

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