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Quizzes > Science

Glycolysis Pathway Quiz: Test Steps, Enzymes, and ATP

Quick, free glycolysis quiz to check steps and enzymes. Instant results.

Editorial: Review CompletedCreated By: Fin PalfreymanUpdated Aug 27, 2025
Difficulty: Moderate
2-5mins
Learning OutcomesCheat Sheet
Paper art illustration for glycolysis quiz on a coral background

This glycolysis quiz helps you map each step from glucose to pyruvate, tally ATP and NADH, and spot key control points. Build your skills with an enzyme quiz, explore cellular respiration basics, and try an electron transport chain quiz. Finish in minutes and see which steps to review next.

Where in the cell does glycolysis primarily occur?
Nucleus
Mitochondria
Endoplasmic Reticulum
Cytosol
Glycolysis is a cytosolic process that breaks down glucose in the cytoplasm, not in organelles like mitochondria or the nucleus. It occurs in the cytosol in both prokaryotic and eukaryotic cells. This localization allows glycolysis to function under anaerobic conditions.
What is the net ATP gain from one molecule of glucose during glycolysis?
3 ATP
2 ATP
4 ATP
1 ATP
The net yield of ATP from glycolysis is two ATP molecules per glucose. Although four ATP are generated during the payoff phase, two ATP are consumed during the investment phase. This results in a net gain of 2 ATP molecules per glucose molecule.
Which enzyme catalyzes the first step of glycolysis?
Phosphofructokinase-1
Pyruvate kinase
Hexokinase
Aldolase
Hexokinase catalyzes the first irreversible step of glycolysis, phosphorylating glucose to glucose-6-phosphate using ATP. This traps glucose in the cell and prepares it for further metabolism. Hexokinase has a high affinity for glucose, functioning at low concentrations.
Glycolysis starts with which substrate?
Pyruvate
Glucose-1-phosphate
Fructose-6-phosphate
Glucose
Glycolysis begins with free glucose in the cytosol, which is then phosphorylated by hexokinase. Other sugars or intermediates are not the starting substrate of the glycolytic pathway. Glucose must be available for the pathway to proceed.
Which three-carbon molecules are produced when fructose-1,6-bisphosphate is cleaved by aldolase?
3-Phosphoglycerate and phosphoenolpyruvate
Dihydroxyacetone phosphate only
Glyceraldehyde 3-phosphate and dihydroxyacetone phosphate
Glyceraldehyde 3-phosphate only
Fructose-1,6-bisphosphate is cleaved by aldolase into two three-carbon sugars: glyceraldehyde 3-phosphate and dihydroxyacetone phosphate. This step is reversible and critical for splitting the molecule into triose units. Only these two triose phosphates are produced in this reaction.
Which enzyme catalyzes the rate-limiting step of glycolysis?
Hexokinase
Phosphofructokinase-1
Phosphoglucose isomerase
Pyruvate kinase
Phosphofructokinase-1 catalyzes the rate-limiting, committed step of glycolysis, converting fructose-6-phosphate to fructose-1,6-bisphosphate. It is highly regulated by allosteric effectors such as ATP and fructose-2,6-bisphosphate. This regulation ensures proper flux through the pathway.
What is the primary regulatory effect of fructose-2,6-bisphosphate on glycolysis?
Activates phosphofructokinase-1
Inhibits pyruvate kinase
Activates hexokinase
Inhibits phosphofructokinase-1
Fructose-2,6-bisphosphate is a potent activator of phosphofructokinase-1, increasing its affinity for fructose-6-phosphate. It acts as a key regulatory molecule linking glycolysis and gluconeogenesis. Elevated levels stimulate glycolytic flux under insulin signaling.
During glycolysis, which enzyme produces NADH?
Enolase
Aldolase
Triose phosphate isomerase
Glyceraldehyde 3-phosphate dehydrogenase
Glyceraldehyde 3-phosphate dehydrogenase catalyzes the oxidation of glyceraldehyde 3-phosphate, reducing NAD+ to NADH. This is the only step in glycolysis where NAD+ is reduced. NADH is then reoxidized under anaerobic or aerobic conditions.
Which enzyme catalyzes substrate-level phosphorylation to form ATP in glycolysis?
Pyruvate kinase
Phosphoglycerate kinase
Both phosphoglycerate kinase and pyruvate kinase
None of the above
Substrate-level phosphorylation in glycolysis occurs at two steps: phosphoglycerate kinase transfers a phosphate to ADP to form ATP, and pyruvate kinase produces ATP from phosphoenolpyruvate. Both enzymes catalyze ATP generation without oxygen.
Which step is reversible under physiological conditions in glycolysis?
Conversion of 3-phosphoglycerate to 2-phosphoglycerate
Conversion of fructose-6-phosphate to fructose-1,6-bisphosphate
Conversion of glucose to glucose-6-phosphate
Conversion of phosphoenolpyruvate to pyruvate
The conversion of 3-phosphoglycerate to 2-phosphoglycerate is catalyzed by phosphoglycerate mutase and is near equilibrium under physiological conditions. Other steps like phosphoenolpyruvate to pyruvate or fructose-6-phosphate to fructose-1,6-bisphosphate are highly exergonic and essentially irreversible.
Which cofactor is essential for the glyceraldehyde 3-phosphate dehydrogenase reaction?
NAD+
NADP+
Coenzyme A
FAD
Glyceraldehyde 3-phosphate dehydrogenase requires NAD+ as an electron acceptor to oxidize glyceraldehyde 3-phosphate into 1,3-bisphosphoglycerate. NAD+ is reduced to NADH in this step. FAD and CoA are not used in glycolysis.
What is the role of magnesium ions (Mg2+) in the phosphofructokinase-1 reaction?
Serves as a substrate for the kinase reaction
Acts as an allosteric inhibitor of PFK-1
Forms a complex with ATP to enable phosphoryl transfer
Coordinates with fructose-6-phosphate to facilitate isomerization
Magnesium ions form a complex with ATP (Mg-ATP) which is the true substrate for phosphofructokinase-1, stabilizing the negative charges and facilitating phosphoryl transfer. Without Mg2+, ATP would not properly bind to the enzyme active site.
In the absence of sufficient oxygen, what is the fate of pyruvate produced by glycolysis in muscle cells?
Converted to acetyl-CoA
Reduced to lactate
Carboxylated to oxaloacetate
Used to generate ethanol
Under anaerobic conditions in muscle cells, pyruvate is reduced to lactate by lactate dehydrogenase to regenerate NAD+, allowing glycolysis to continue. This prevents NADH from accumulating and ensures ATP production in the absence of oxygen.
Which enzyme interconverts dihydroxyacetone phosphate and glyceraldehyde 3-phosphate?
Aldolase
Phosphoglycerate kinase
Triose phosphate isomerase
Glyceraldehyde 3-phosphate dehydrogenase
Triose phosphate isomerase interconverts dihydroxyacetone phosphate and glyceraldehyde 3-phosphate rapidly and near equilibrium. This ensures that both triose phosphates can enter the payoff phase of glycolysis. It is one of the most efficient enzymes known.
What is the standard free energy change (?G°') of the hexokinase reaction, making it effectively irreversible?
-84.6 kJ/mol
-16.7 kJ/mol
-30.5 kJ/mol
+1.7 kJ/mol
The hexokinase reaction has a standard free energy change (?G°') of approximately -16.7 kJ/mol, making it essentially irreversible under physiological conditions. This ensures glucose is committed to metabolism once phosphorylated. Such strongly exergonic reactions drive pathway directionality.
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Study Outcomes

  1. Recall Glycolysis Steps -

    Engage with the remember steps of glycolysis quiz to accurately recall all ten enzymatic reactions from glucose to pyruvate.

  2. Identify Key Enzymes -

    Pinpoint the specific enzymes that catalyze each step and understand their roles in facilitating substrate-level phosphorylation and redox reactions.

  3. Calculate Net Energy Yield -

    Quantify the ATP and NADH produced during glycolysis and apply these calculations in our glycolysis practice test scenarios.

  4. Analyze Regulatory Mechanisms -

    Examine how feedback inhibition and allosteric control affect critical steps, reinforcing concepts in the glycolysis pathway quiz.

  5. Apply Concepts in a Game Format -

    Utilize the glycolysis game elements to test your mastery under timed conditions and boost retention through interactive challenges.

Cheat Sheet

  1. ATP Investment and Net Yield -

    Glycolysis invests 2 ATP in the energy”investment phase (steps 1 - 3) and produces 4 ATP and 2 NADH in the payoff phase (steps 7 - 10), yielding a net of 2 ATP and 2 NADH per glucose. Remember this balance when you tackle glycolysis quiz or practice questions to avoid mixing up totals. Use the equation: glucose + 2 ADP + 2 Pi + 2 NAD+ → 2 pyruvate + 2 ATP + 2 NADH + 2 H+ to solidify your understanding.

  2. Regulatory Enzymes: PFK-1, Hexokinase & Pyruvate Kinase -

    Phosphofructokinase-1 is the pathway's key rate-limiting step, allosterically inhibited by ATP and activated by AMP and fructose-2,6-bisphosphate. Hexokinase traps glucose in the cell, and pyruvate kinase catalyzes the final ATP”generating step. Mastering these control points boosts your score on any glycolysis pathway quiz or glycolysis game challenge.

  3. NADH Formation and Anaerobic Regeneration -

    During step 6, glyceraldehyde-3-phosphate dehydrogenase reduces NAD+ to NADH; under anaerobic conditions, lactate dehydrogenase regenerates NAD+ by converting pyruvate to lactate. This balance is crucial for sustained glycolytic flux and a common focus of glycolysis practice questions. Recall that 2 NADH per glucose are produced, linking energy yield to redox balance.

  4. Substrate Sequence Mnemonic -

    Use "Hungry Peter Pan And The Growling Pink Panther Ate Eight Pickles" to recall Hexokinase, Phosphoglucose isomerase, Phosphofructokinase, Aldolase, Triose phosphate isomerase, Glyceraldehyde-3-phosphate dehydrogenase, Phosphoglycerate kinase, Phosphoglycerate mutase, Enolase, Pyruvate kinase. Mnemonics like this sharpen recall in the remember steps of glycolysis quiz or during fast-paced glycolysis practice questions. Keep it handy to breeze through each enzyme and order.

  5. High-Energy Intermediates Drive ATP Synthesis -

    1,3-Bisphosphoglycerate and phosphoenolpyruvate are high-energy intermediates that donate phosphates to ADP via substrate-level phosphorylation. Recognizing these intermediates is key to understanding how glycolysis generates ATP and acing detailed items in your glycolysis quiz. Think of them as the "energy currency" coins you spend to power the cell.

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