Effects of Inhibitors on Lactate Dehydrogenase

Very Hard Biochemistry Enzymes

Enzymatic reactions often follow specific kinetic patterns that can be affected by various factors, including substrate concentration, temperature, and pH. In a recent study investigating the enzyme lactate dehydrogenase (LDH), researchers explored its activity under physiological and pathological conditions. During the study, they noted that the enzyme displayed different V_max values at varied pH levels, with a marked reduction in activity at pH values significantly deviating from the physiological range of 7.4.

To further investigate the properties of LDH, the researchers performed experiments to ascertain the effect of inhibitors on the enzyme’s activity. They exposed LDH to both reversible and irreversible inhibitors, aiming to determine which type was more effective in reducing the enzyme’s functionality. Given this context, which of the following statements regarding the effects of inhibitors on LDH is most accurate?

Reversible inhibitors permanently alter the enzyme's active site, reducing its activity irreversibly.

Irreversible inhibitors bind temporarily to the allosteric site, allowing for a rapid recovery of enzymatic function.

Reversible inhibitors can compete with the substrate for the active site, reducing the effective concentration of the enzyme-substrate complex.

Both reversible and irreversible inhibitors increase the V<sub>max</sub> of LDH.

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