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Literature summary for 2.7.1.40 extracted from

  • Verma, K.; Patel, A.
    Pyruvate kinase M2 serves as blockade for nucleosome repositioning and abrogates Chd7 remodeling activity (2019), PLoS ONE, 14, e0211515 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.1.40

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) Rosetta Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
K+ required Homo sapiens
Mg2+ required Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ADP + phosphoenolpyruvate Homo sapiens
-
 ATP + pyruvate
-
 ?
additional information Homo sapiens PKM2 during in vitro reconstitution potentially interacts with histone H3 of the 5'-FAM labelled nucleosome octamer core and forms a stable complex. PKM2 phosphorylates histone H3 at T11 ?
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-

Organism

Organism UniProt Comment Textmining
Homo sapiens P14618
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) Rosetta by nickel affinity chromatography, dialysis, and gel filtration Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ADP + phosphoenolpyruvate
-
 Homo sapiens ATP + pyruvate
-
 ?
additional information PKM2 during in vitro reconstitution potentially interacts with histone H3 of the 5'-FAM labelled nucleosome octamer core and forms a stable complex. PKM2 phosphorylates histone H3 at T11 Homo sapiens ?
-
-

Synonyms

Synonyms Comment Organism
PKM2
-
 Homo sapiens
pyruvate kinase M2
-
 Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
23
-
 assay at Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.6
-
 assay at Homo sapiens

General Information

General Information Comment Organism
metabolism mode of cancer metabolism to potentially modulate the gene expression and sustain incessant proliferation by tweaking the chromatin topography, overview Homo sapiens
physiological function pyruvate kinase enzyme catalyzes the last rate-limiting step of glycolysis converting phosphoenolpyruvate to pyruvate with the subsequent production of ATP. Pyruvate kinase M2 (PKM2) is an oncofetal isoform generated as a result of alternative splicing of the PKM mRNA transcript exhibit low basal activity and thus is a key player in regulating the glycolytic flux contributing to cancer progression. It results in the build-up of glycolytic intermediates which are directed towards the biosynthetic processes. PKM2 mediates metabolic reshuffling and is ubiquitously upregulated in several cancer types. The non-metabolic function of PKM2 as key nuclear kinase and modulator of gene expression is instrumental in cancer progression and tumorigenesis. The non-canonical function of PKM2 is an epigenetic modulator. Enzyme PKM2 interacts with the reconstituted mononucleosome complex through histone H3 and possibly obstructs the access to DNA binding factors. The interaction negatively impacts the ATP-dependent remodeling activity of chromodomain helicase DNA binding protein-7 (Chd7). Chd7 remodeling activity is required to ameliorate DNA damage and is crucial to genome stability. PKM2 blocks the Chd7 mediated sliding of nucleosome. It can be conjectured that stalling Chd7 may lead to impaired DNA damage and increased genomic instability. PKM2 negatively regulates nucleosome repositioning in chromatin and may exacerbate cancer by altering the nucleosome architecture, mechanism, overview. The nucleosome digestion activity of the PKM2-nucleosome complex is remarkably impaired as can be inferred from the digestion profile. Pyruvate kinase M2 can potentially disrupt the ChD7-mediated remodeling of nucleosome Homo sapiens