The Michaelis-Menten equation is derived using the steady-state assumption. This assumption states that during the initial phase of the reaction:

• A The total enzyme concentration equals the substrate concentration
• B The reverse reaction from product to substrate proceeds at the same rate as the forward reaction
• C The product concentration rises linearly until it equals the substrate concentration
• D The concentration of the enzyme-substrate complex remains constant because its rate of formation equals its rate of breakdown ✓

Explanation

Briggs and Haldane assumed that early in the reaction the ES complex accumulates rapidly and then holds nearly constant, so d[ES]/dt is approximately zero; this allows algebraic solution for [ES] and yields the Michaelis-Menten equation. Initial-rate measurements also make product concentration negligible, so the reverse reaction is ignored, ruling out option B. Option A is impossible since enzymes are catalytic and present at far lower concentrations than substrate.

Reference: Lehninger Principles of Biochemistry, 7th ed.

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