Which type of enzyme inhibitor does not alter the KM/Vmax ratio?

Uncompetitive inhibitors uniquely affect enzyme kinetics by binding to the enzyme-substrate complex, rather than the free enzyme. When an uncompetitive inhibitor binds, it effectively locks the substrate in the enzyme, preventing the conversion of substrate to product. This interaction decreases both the maximum velocity (Vmax) and the Michaelis constant (KM) because the concentration of the substrate does not lead to the same maximal rate of reaction due to the inhibition.

However, since both Vmax and KM decrease proportionally, the ratio of KM to Vmax remains unchanged. This contrasts with competitive and non-competitive inhibitors, where the KM or Vmax is altered leading to a change in that ratio. Therefore, the behavior of uncompetitive inhibitors results in a consistent KM/Vmax ratio, making option B the correct answer.