**Core Concept**
Competitive inhibition is a type of enzyme inhibition where the inhibitor structurally resembles the substrate and competes with it for binding to the active site of the enzyme. This prevents the substrate from binding and being converted into product, thereby reducing the overall enzyme activity.

**Why the Correct Answer is Right**
The correct answer is related to the mechanism of competitive inhibition, where the inhibitor and substrate compete for the same binding site on the enzyme. This is due to the structural similarity between the inhibitor and substrate, which allows the inhibitor to occupy the active site and prevent the substrate from binding. As a result, the enzyme's ability to convert the substrate into product is reduced, leading to a decrease in enzyme activity.

**Why Each Wrong Option is Incorrect**
**Option A:** This option is incorrect because non-competitive inhibition does not involve competition for the active site. Instead, the inhibitor binds to a different site on the enzyme, altering its shape and reducing its ability to convert the substrate into product.

**Option B:** This option is incorrect because uncompetitive inhibition involves the inhibitor binding to the enzyme-substrate complex, reducing the enzyme's activity by altering its shape.

**Option C:** This option is incorrect because allosteric inhibition involves the inhibitor binding to a site other than the active site, altering the enzyme's shape and reducing its activity.

**Clinical Pearl / High-Yield Fact**
It's essential to remember that competitive inhibition can be overcome by increasing the concentration of the substrate, as this allows more substrate molecules to outcompete the inhibitor for the active site.

**Correct Answer: C. Competitive inhibition can be overcome by increasing the concentration of the substrate.**