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Related Experiment Video

Updated: Jun 8, 2026

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

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Published on: May 13, 2020

Human pyruvate kinase M2: a multifunctional protein.

Vibhor Gupta¹, Rameshwar N K Bamezai

¹National Centre of Applied Human Genetics, School of Life Sciences, Jawaharlal Nehru University, New Delhi 110067, India. vibhor27@gmail.com

Protein Science : a Publication of the Protein Society

|September 22, 2010

Summary

Pyruvate kinase M2 (PKM2) is a key enzyme in glycolysis that regulates cellular metabolism. Its unique structure allows it to support cell growth by providing building blocks for biosynthesis.

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Area of Science:

Biochemistry
Cell Biology
Metabolic Regulation

Background:

Glycolysis is a fundamental metabolic pathway crucial for cellular energy production.
Pyruvate kinase (PK) catalyzes the final, rate-limiting step of glycolysis.
The M2 isoform (PKM2) is specifically expressed in proliferating cells, including embryonic and tumor cells.

Purpose of the Study:

To review the multifaceted roles of Pyruvate kinase M2 (PKM2) beyond its canonical glycolytic function.
To explore the non-glycolytic functions and potential implications of PKM2 in various cellular processes.
To highlight the significance of PKM2 in cellular metabolism and its involvement in diverse pathways.

Main Methods:

Literature review of studies on PKM2.
Analysis of PKM2's structural properties and allosteric regulation.
Examination of PKM2's interactions with other proteins and its role in nuclear transport.

Main Results:

PKM2 exists as a tetramer and can reversibly dissociate into dimers, modulating its enzymatic activity.
Downregulation of PKM2 activity leads to the accumulation of glycolytic intermediates, fueling anabolic biosynthesis.
PKM2 participates in protein-protein interactions and nuclear transport, suggesting non-metabolic functions.

Conclusions:

PKM2's unique regulatory mechanism supports the metabolic demands of proliferating cells.
The enzyme's involvement in non-glycolytic pathways indicates a broader role in cellular physiology.
Further research is needed to fully elucidate the diverse functions and implications of PKM2.