Anti-PGK1 antibody

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

PGK1 also known as phosphoglycerate kinase-1 is an enzyme involved in glycolysis with a mass of approximately 45 kDa. PGK1 catalyzes the reversible transfer of a phosphate group from 13-bisphosphoglycerate to ADP forming 3-phosphoglycerate and ATP. This enzyme is expressed ubiquitously across various tissues with significant roles in energy metabolism. In yeast it is referred to simply as phosphoglycerate kinase where its function in cellular respiration is widely studied.

Biological function summary

The PGK1 protein plays an essential role in energy production by participating in the glycolytic pathway. This enzyme functions independently and is not part of any complex. By converting 13-bisphosphoglycerate to 3-phosphoglycerate it supports cellular processes that require ATP. Such activity facilitates the high energy needs of cells ensuring proper cellular function and homeostasis.

Pathways

The enzyme PGK1 operates predominantly within the glycolytic and gluconeogenesis pathways. Throughout glycolysis it partners with enzymes like phosphofructokinase and pyruvate kinase facilitating the breakdown of glucose into pyruvate while generating ATP. In gluconeogenesis PGK1 aids in glucose formation which helps balance energy dynamics particularly in tissues like the liver and kidney.

Associated diseases and disorders

PGK1 has associations with tumor growth and proliferation in various cancers. Its elevated expression is often found in tumors linking it to oncogenesis due to the increased demand for glycolytic activity. Additionally mutations in PGK1 can result in phosphoglycerate kinase deficiency a disorder affecting red blood cell metabolism. This links it to related proteins involved in managing metabolic pathways of energy production in affected tissues.