Activating Compound | Comment | Organism | Structure |
---|---|---|---|
fructose 1,6-bisphosphate | FBP, FBP-mediated PKM2 activation requires the tetramerization of PKM2. The dimeric enzyme, e.g. mutant PKM2G415R, is in its tense form and cannot be activated by FBP | Homo sapiens | |
additional information | different modes of PKM2 activation by FBP and SAICAR, schematic overview | Homo sapiens | |
succinyl-5-aminoimidazole-4-carboxamide-1-ribose 5'-phosphate | SAICAR, an endogenous metabolite that correlates with an increased level of cell proliferation, it activates pyruvate kinase isoform M2 (PKM2) in its dimeric form, connection between SAICAR binding and the oligomeric state of PKM2, SAICAR stimulates the PKM2 dimer without inducing formation of a PKM2 tetramer. SAICAR binds to PKM2 mutant G415R better than it binds to wild-type PKM2 | Homo sapiens |
Protein Variants | Comment | Organism |
---|---|---|
G415R | site-directed mutagenesis, the mutant binds fructose 1,6-bisphosphate, but is not activated by it, unlike the wild-type PKM2. But the mutant is activated by succinyl-5-aminoimidazole-4-carboxamide-1-ribose 5'-phosphate (SAICAR) | Homo sapiens |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.25 | - |
ADP | mutant PKM2G415R, pH 7.6, 37°C | Homo sapiens | |
1.2 | - |
phosphoenolpyruvate | mutant PKM2G415R, pH 7.6, 37°C | Homo sapiens |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Homo sapiens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ADP + phosphoenolpyruvate | Homo sapiens | - |
ATP + pyruvate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | P14618 | - |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
carcinoma cell | prevalence of dimeric PKM2 in cancer | Homo sapiens | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ADP + phosphoenolpyruvate | - |
Homo sapiens | ATP + pyruvate | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | dimeric PKM2 is regarded as an inactive form of tetrameric pyruvate kinase, but the enzymatic activity of the PKM2 dimer is determined in presence of metabolite SAICAR | Homo sapiens |
More | although found to exist in different oligomeric forms in cells, like other pyruvate kinases, PKM2 is considered to have maximal pyruvate kinase activity as a tetramer. Prevalence of dimeric PKM2 in cancer | Homo sapiens |
tetramer | - |
Homo sapiens |
Synonyms | Comment | Organism |
---|---|---|
PKM2 | - |
Homo sapiens |
pyruvate kinase isoform M2 | - |
Homo sapiens |
pyruvate kinase M2 | - |
Homo sapiens |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Homo sapiens |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.57 | - |
phosphoenolpyruvate | mutant PKM2G415R, pH 7.6, 37°C | Homo sapiens |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.6 | - |
assay at | Homo sapiens |
General Information | Comment | Organism |
---|---|---|
physiological function | human pyruvate kinase isoform M2 (PKM2) is a glycolytic enzyme isoform implicated in cancer. Malignant cancer cells have higher levels of dimeric PKM2, which is regarded as an inactive form of tetrameric pyruvate kinase. The enzymatic activity of the PKM2 dimer likely has a key role in cancer progression. In addition to its classical role in generating ATP from ADP and the phosphate donor PEP, PKM2 also has been found to phosphorylate protein substrates | Homo sapiens |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.475 | - |
phosphoenolpyruvate | mutant PKM2G415R, pH 7.6, 37°C | Homo sapiens |