Recombinant Human PCK1/PEPC protein
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Recombinant Human PCK1/PEPC protein is a Human Full Length protein, in the 1 to 622 aa range, expressed in Escherichia coli, with >85%, suitable for SDS-PAGE.
View Alternative Names
PEPCK1, PCK1, PEPCK-C, Serine-protein kinase PCK1
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Human PCK1/PEPC protein (AB119469)
SDS-PAGE analysis of ab119469.
Reactivity data
Product details
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage duration
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
PCK1 is essential for maintaining glucose homeostasis in the body. Although not part of a larger protein complex its function directly impacts the tricarboxylic acid (TCA) cycle by providing substrates for glucose synthesis. By orchestrating the conversion of oxaloacetate to PEP PCK1 contributes significantly to reducing dependency on dietary carbohydrates particularly during fasting or intensive physical activity.
Pathways
PCK1 integrates critical metabolic processes. It mainly influences the gluconeogenesis and glycolysis pathways. In the gluconeogenesis pathway PCK1 coordinates with enzymes such as glucose-6-phosphatase to facilitate the generation of glucose from lactate and amino acids. Additionally its role in glycolysis intersects with enzymes like pyruvate kinase managing energy production and consumption.
Specifications
Form
Liquid
Additional notes
ab119469 was purified using conventional chromatography.
General info
Function
Cytosolic phosphoenolpyruvate carboxykinase that catalyzes the reversible decarboxylation and phosphorylation of oxaloacetate (OAA) and acts as the rate-limiting enzyme in gluconeogenesis (PubMed : 24863970, PubMed : 26971250, PubMed : 28216384, PubMed : 30193097). Regulates cataplerosis and anaplerosis, the processes that control the levels of metabolic intermediates in the citric acid cycle (PubMed : 24863970, PubMed : 26971250, PubMed : 28216384, PubMed : 30193097). At low glucose levels, it catalyzes the cataplerotic conversion of oxaloacetate to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle (PubMed : 30193097). At high glucose levels, it catalyzes the anaplerotic conversion of phosphoenolpyruvate to oxaloacetate (PubMed : 30193097). Acts as a regulator of formation and maintenance of memory CD8(+) T-cells : up-regulated in these cells, where it generates phosphoenolpyruvate, via gluconeogenesis (By similarity). The resultant phosphoenolpyruvate flows to glycogen and pentose phosphate pathway, which is essential for memory CD8(+) T-cells homeostasis (By similarity). In addition to the phosphoenolpyruvate carboxykinase activity, also acts as a protein kinase when phosphorylated at Ser-90 : phosphorylation at Ser-90 by AKT1 reduces the binding affinity to oxaloacetate and promotes an atypical serine protein kinase activity using GTP as donor (PubMed : 32322062). The protein kinase activity regulates lipogenesis : upon phosphorylation at Ser-90, translocates to the endoplasmic reticulum and catalyzes phosphorylation of INSIG proteins (INSIG1 and INSIG2), thereby disrupting the interaction between INSIG proteins and SCAP and promoting nuclear translocation of SREBP proteins (SREBF1/SREBP1 or SREBF2/SREBP2) and subsequent transcription of downstream lipogenesis-related genes (PubMed : 32322062).
Sequence similarities
Belongs to the phosphoenolpyruvate carboxykinase [GTP] family.
Post-translational modifications
Acetylated. Lysine acetylation by p300/EP300 is increased on high glucose conditions (PubMed:20167786, PubMed:21726808, PubMed:30193097). Lysine acetylation promotes ubiquitination by UBR5 (PubMed:21726808). Acetylation is enhanced in the presence of BAG6. Deacetylated by SIRT2. Deacetylation of Lys-91 is carried out by SIRT1 and depends on PCK1 phosphorylation levels (PubMed:30193097).. Phosphorylated in a GSK3B-mediated pathway; phosphorylation affects the efficiency of SIRT1-mediated deacetylation, and regulates PCK1 ubiquitination and degradation (PubMed:30193097). Phosphorylation at Ser-90 by AKT1 reduces the binding affinity to oxaloacetate and promotes the protein kinase activity: phosphorylated PCK1 translocates to the endoplasmic reticulum, where it phosphorylates INSIG1 and INSIG2 (PubMed:32322062).. Ubiquitination by UBR5 leads to proteasomal degradation.
Target data
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Product promise
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