medium · MCAT bio-biochem
An enzyme-catalyzed reaction follows Michaelis-Menten kinetics.
If a researcher adds a reversible inhibitor that increases the apparent K_M but leaves the V_max unchanged, which of the following describes the interaction between the inhibitor and the enzyme?
- The inhibitor binds to an allosteric site regardless of whether the substrate is present.
- The inhibitor binds to the active site and prevents substrate binding.
- The inhibitor covalently binds to the enzyme, permanently deactivating it.
- The inhibitor binds to an allosteric site only after the substrate has bound.
Sign up free to see the explanation and track your rank →
More MCAT bio-biochem practice
- What genetic term describes a single gene influencing multiple seemingly unrelated traits?
- In the human ear, sound waves cause fluid in the cochlea to… — Which cells are responsible
- An electrophysiologist observes a neuron at its resting memb… — Which ion is primarily res
- Which structure is most likely dysfunctional?
- Which organelle would you expect to be exceptionally well-developed in these cells?
- Which molecule acts as a 'fluidity buffer' in animal cell membranes?
- A scientist is tracking the movement of a secreted protein. If the protein has just left t
- A molecule moves into a cell against its concentration gradient using energy provided by a