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PKM

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Anti-PKM Recombinant Antibody Products

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For Research Use Only. Not For Clinical Use.


PKM (Pyruvate Kinase Muscle) encodes an enzyme that catalyzes the final step of glycolysis, converting phosphoenolpyruvate to pyruvate while generating ATP. PKM exists in several isoforms, with the muscle isoform (PKM2) playing a significant role in cellular energy metabolism. Alterations in PKM activity are associated with cancer metabolism, as tumor cells often exhibit increased glycolytic activity (Warburg effect).
Protein class

Cancer-related genes, Enzymes, Metabolic proteins, Plasma proteins

Predicted location

Intracellular

Single cell type specificity

Cell type enhanced (Basal respiratory cells, Late spermatids)

Immune cell specificity

Low immune cell specificity

Cell line specificity

Low cell line specificity

Interaction

[Isoform M2]: Monomer and homotetramer; exists as a monomer in the absence of D-fructose 1,6-bisphosphate (FBP), and reversibly associates to form a homotetramer in the presence of FBP (PubMed:15996096, 18298799, 18337815, 1854723, 23064226, 2813362). The monomeric form binds 3,3',5-triiodo-L-thyronine (T3) (PubMed:15996096). Tetramer formation induces pyruvate kinase activity (PubMed:15996096, 18298799, 18337815, 1854723, 23064226, 2813362). The tetrameric form has high affinity for the substrate and is associated within the glycolytic enzyme complex (PubMed:15996096, 18298799, 18337815, 1854723, 23064226, 2813362). FBP stimulates the formation of tetramers from dimers (PubMed:15996096, 18298799, 18337815, 1854723, 23064226, 2813362). Homodimer; exists in a dimeric form in tumor cells and the dimeric form has less affinity for the phosphoenolpyruvate substrate (PubMed:22306293, 24120661). The homodimer converts into a protein kinase (PubMed:22306293, 24120661). Interacts with HERC1, POU5F1 and PML (PubMed:12650930, 18191611). Interacts with EGLN3; the interaction hydroxylates PKM under hypoxia and enhances binding to HIF1A (PubMed:21620138, 21483450). Interacts with HIF1A; the interaction is enhanced by binding of EGLN3, promoting enhanced transcription activity under hypoxia (PubMed:21620138). Interacts with TRIM35; this interaction prevents FGFR1-dependent tyrosine phosphorylation (PubMed:25263439). Interacts with JMJD8 (PubMed:27199445). Interacts with TRAF4 (PubMed:32268273). Interacts with (phosphorylated) CTNNB1; leading to activate transcription (PubMed:22056988). (Microbial infection) Binding to certain oncoproteins such as HPV-16 E7 oncoprotein promotes homodimerization.

Molecular function

Allosteric enzyme, Kinase, Transferase

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