Step 1: Concept
Competitive inhibition occurs when an inhibitor competes with the substrate for the active site of an enzyme.
Step 2: Meaning
Kinetic parameters $V_{max}$ (maximum velocity) and $K_{m}$ (Michaelis constant) describe enzyme performance.
Step 3: Analysis
In competitive inhibition, the $V_{max}$ remains unchanged because high substrate concentrations can overcome the inhibitor. However, the apparent $K_{m}$ increases because more substrate is needed to achieve half-maximum velocity.
Step 4: Conclusion
An increase in $K_{m}$ with a constant $V_{max}$ is the hallmark of competitive inhibition.
Final Answer: (D)