Pyruvate kinase PKM(PKM)


100ug, 50ug


Product type

Host Species



Product namePyruvate kinase PKM(PKM)
Uniprot IDP14618
Uniprot link
Expression systemProkaryotic expression
Molecular weight60.1kDa
Protein delivered with Tag?N-terminal His Tag
Purity estimated>90% by SDS-PAGE
BufferPBS, pH7.5
Delivery conditionDry Ice
Delivery lead time in business daysEurope: 5-7 working days
USA & Canada: 7-10 working days
Rest of the world: 5-12 working days
Storage condition4°C for short term (1 week), -20°C or -80°C for long term (avoid freezing/thawing cycles; addition of 20-40% glycerol improves cryoprotection)
Host speciesEscherichia coli (E.coli)
Fragment TypeMet1-Pro531
Protein AccessionP14618
Spec:Entrez GeneID5315
Spec:NCBI Gene AliasesPK3; TCB; p58; OIP3; PKM2; CTHBP; THBP1; HEL-S-30
NCBI ReferenceP14618
Aliases /SynonymsCytosolic thyroid hormone-binding protein,CTHBP,Opa-interacting protein 3,OIP-3,Pyruvate kinase 2/3,Pyruvate kinase muscle isozyme,Thyroid hormone-binding protein 1,THBP1,Tumor M2-PK,p58,OIP3, PK2, PK3, PKM2
NoteFor research use only

Description of Pyruvate kinase PKM(PKM)

Introduction to Pyruvate Kinase PKM

Pyruvate kinase PKM (PKM) is a key enzyme involved in the final step of glycolysis, the metabolic pathway that converts glucose into energy. It catalyzes the conversion of phosphoenolpyruvate (PEP) to pyruvate, producing adenosine triphosphate (ATP) in the process. PKM is a highly conserved protein found in all living organisms, from bacteria to humans. In this article, we will explore the structure, activity, and application of PKM, with a focus on its potential as a drug target.

Structure of this protein

PKM is a tetrameric protein composed of four identical subunits, each with a molecular weight of approximately 58 kDa. The subunits can exist in two different isoforms, PKM1 and PKM2, which differ in their amino acid sequences and enzymatic activity. PKM1 is predominantly found in tissues with high energy demand, such as muscle and brain, while PKM2 is mainly expressed in rapidly proliferating cells, such as cancer cells.

The crystal structure of PKM has been extensively studied, revealing that each subunit consists of two domains: the N-terminal domain and the C-terminal domain. The N-terminal domain is responsible for binding to PEP, while the C-terminal domain is involved in the binding of other substrates and allosteric regulators. The tetrameric structure of PKM is essential for its activity, as it allows for the efficient transfer of phosphate groups between subunits.

Activity of PKM

PKM is a key regulator of glycolysis, the process by which cells convert glucose into energy. It plays a crucial role in maintaining cellular energy homeostasis by controlling the rate of glycolysis. In its active form, PKM catalyzes the conversion of PEP to pyruvate, which is then further metabolized to produce ATP. This process is essential for providing cells with the energy they need to carry out their functions.

In addition to its role in energy production, PKM also has non-metabolic functions. It has been shown to regulate gene expression, cell proliferation, and apoptosis. PKM can also act as a protein kinase, phosphorylating other proteins and influencing their activity. These diverse functions make PKM a potential target for therapeutic intervention in various diseases.

Potential as a Drug Target

The dysregulation of PKM has been linked to various diseases, including cancer, diabetes, and neurodegenerative disorders. In cancer, PKM2 is often overexpressed, promoting the Warburg effect, a metabolic phenomenon where cancer cells rely on glycolysis for energy production even in the presence of oxygen. Targeting PKM2 has been shown to inhibit cancer cell growth and promote cell death, making it a promising target for cancer therapy.

In diabetes, PKM has been implicated in the development of insulin resistance. Inhibition of PKM activity has been shown to improve insulin sensitivity and glucose tolerance in animal models, suggesting that targeting PKM could be a potential treatment for diabetes.

In neurodegenerative disorders, PKM has been linked to the regulation of neuronal cell death. Studies have shown that inhibition of PKM activity can protect neurons from cell death, making it a potential target for the treatment of diseases such as Alzheimer’s and Parkinson’s.


In conclusion, PKM is a crucial enzyme involved in glycolysis, energy production, and various non-metabolic functions. Its structure and activity make it a potential target for therapeutic intervention in diseases such as cancer, diabetes, and neurodegenerative disorders. Further research on PKM could lead to the development of novel treatments for these diseases, making it an exciting area of study in the field of biochemistry and medicine.


There are no reviews yet.


Be the first to review “Pyruvate kinase PKM(PKM)”

Your email address will not be published. Required fields are marked *

Contact us

Send us a message from the form below

    Cart (0 Items)

    Your cart is currently empty.

    View Products