Recombinant Human PDHA1 protein

Supplementary information

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

PDHA1 also known as the pyruvate dehydrogenase E1 alpha subunit plays a mechanical role in cellular metabolism. It forms part of the larger pyruvate dehydrogenase (PDH) complex where it serves as a critical catalytic component. PDHA1 is expressed ubiquitously across different tissue types reflecting its fundamental function in energy production. The molecular weight of the PDHA1 protein is approximately 43 kDa. Alternate names for this protein include the PDH E1 component and it partners closely with other components in the PDH complex to facilitate its role.

Biological function summary

PDHA1 engages in the conversion of pyruvate into acetyl-CoA an important step in cellular respiration. This protein is part of the PDH complex which consists of multiple copies of three catalytic and two regulatory subunits. The conversion process is essential for linking glycolysis to the citric acid cycle efficiently channeling energy substrates within the cell. Furthermore the functional activity of PDHA1 is regulated through phosphorylation by the pyruvate dehydrogenase kinases (PDKs) and dephosphorylation by PDH phosphatases.

Pathways

PDHA1 is integral to the metabolic pathway of cellular respiration and energy production. It enables the transition between glycolysis and the citric acid cycle by facilitating the conversion of pyruvate to acetyl-CoA which enters the citric acid cycle. Related proteins in this pathway include PDHA2 and the regulatory PDKs that modulate PDHA1 activity. These interactions ensure energy metabolism adapts to various cellular conditions influencing energy balance and substrate utilization.

Mutations or dysfunctions in PDHA1 can lead to disorders such as pyruvate dehydrogenase deficiency and Leigh syndrome. These conditions result from impaired energy metabolism leading to severe neurological symptoms and overall energy deficits in tissues with high metabolic demands. The link between PDHA1 and diseases highlights the importance of maintaining its function. Additionally altered interaction with proteins involved in phosphorylation such as the PDKs can exacerbate pathogenic conditions by further disbalancing metabolic activities.