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MCAT - Biochemistry - Enzyme kineticsLive tournament10 tasks

Enzyme Kinetics Tournament

Two onboarding diagrams put you inside carbohydrate metabolism. Then eight MCAT rounds: the definition of Km, a Lineweaver-Burk intercept, the E + S ⇌ ES → E + P sequence, parameter matching, hexokinase vs glucokinase curves, a half-Vmax calculation, Michaelis-Menten assumptions, and what a competitive inhibitor actually does to rate.

Step 1 of 3 - The bigger pictureEnzyme Kinetics Tournament

Where the Glucose metabolism (gluconeogenesis branch) fits in Metabolism of carbohydrates

Every carbohydrate pathway on this Reactome map is an enzyme-catalyzed rate problem. Hexokinase vs glucokinase, PFK-1 vs FBPase, and the bypasses of gluconeogenesis are the MCAT's favorite kinetic contrasts. Click the highlighted glucose-metabolism panel to enter the tournament.

Click the highlighted Glucose metabolism (gluconeogenesis branch) box to continue.

What this tournament tests

Each task maps to a distinct MCAT cognitive demand. The first two orient you in the broader topology; the next 8 test the high-yield mechanism, regulation, sequence and quantitative reasoning that consistently appear on test day.

1

The Bigger Picture

Anchor glucose-metabolizing enzymes on the live Reactome carbohydrate map.

2

Whole-Pathway Overview

Pan and zoom the WikiPathways glucose-metabolism figure before you answer.

3

Fill in the Blank

Recall that Km is [S] at one-half Vmax.

4

Disruptor

Read Km from a Lineweaver-Burk x-intercept.

5

Sequence Ordering

Order E + S ⇌ ES → E + P.

6

Match the Pairs

Pair Km, Vmax, k_cat, and both LB intercepts with their meaning.

7

Graph Reading

Read hexokinase vs glucokinase Michaelis-Menten curves.

8

Numeric Input

Compute v when [S] = Km.

9

Select All That Apply

Identify true Michaelis-Menten assumptions.

10

Odd One Out

Spot the change that lowers, not raises, unsaturated velocity.

Public leaderboard

Your score posts to a global, persistent leaderboard scored by points first, time as tiebreaker.

Enzyme kinetics in 60 seconds

Michaelis-Menten: v = Vmax [S] / (Km + [S]). Km is [S] at half Vmax — a low Km is high affinity. Vmax is the saturated rate and equals k_cat [E].

Lineweaver-Burk plots 1/v against 1/[S]. Y-intercept is 1/Vmax, x-intercept is -1/Km. The MCAT uses this plot to diagnose inhibitor type, which is the sister tournament.

Hexokinase (low Km, G6P-inhibited) traps glucose in every tissue at fasting concentrations. Glucokinase (high Km, liver and β-cell) only runs hard after a meal.

FAQ

Is Km the same as Kd?

Only when k_cat is negligible compared with k_off. In general Km = (k_off + k_cat) / k_on, so a very fast catalytic step inflates Km above the true dissociation constant.

Why does the MCAT love hexokinase vs glucokinase?

It is the cleanest tissue-specific kinetic pair on the exam. Same reaction (glucose → G6P), opposite physiologic jobs, opposite Km and regulation.

What is the Lineweaver-Burk x-intercept?

−1/Km. The y-intercept is 1/Vmax. The MCAT uses those two numbers to read affinity and capacity off a double-reciprocal plot without fitting a curve.

Do I need an account to play?

No. The tournament is fully public. You get a randomized handle and your score posts to the public leaderboard.