Key regulatory steps in glycolysis: Which enzymes collectively regulate the pathway by serving as major control points responsive to cellular energy status?

Introduction / Context:
Glycolysis includes several irreversible steps that act as control points. Recognizing the regulatory enzymes clarifies how flux adjusts to ATP demand, substrate supply, and hormonal cues.

Given Data / Assumptions:

• Hexokinase/glucokinase catalyze glucose phosphorylation.
• PFK-1 commits fructose-6-phosphate to glycolysis.
• Pyruvate kinase finishes glycolysis by making pyruvate and ATP.

Concept / Approach:
Each of these steps is regulated allosterically and/or by covalent modification. Together they determine the overall throughput of glycolysis in different tissues and metabolic states.

Step-by-Step Solution:
Hexokinase: feedback inhibited by glucose-6-phosphate; hepatic glucokinase regulated by sequestration and transcription. PFK-1: inhibited by ATP/citrate; activated by ADP/AMP and fructose-2,6-bisphosphate. Pyruvate kinase: activated by fructose-1,6-bisphosphate; inhibited by ATP and alanine; subject to phosphorylation in liver. Since all three influence flux, choose “All of these.”

Verification / Alternative check:
Metabolic control analysis and classic enzyme studies identify these steps as rate-determining under common physiological conditions.

Why Other Options Are Wrong:
Picking any single enzyme ignores distributed control; aconitase is a TCA enzyme, not glycolytic.

Common Pitfalls:
Assuming one “rate-limiting” step explains all regulation; neglecting tissue-specific differences.

Final Answer:
All of these enzymes participate in glycolytic regulation.