Anti-Phosphoserine Aminotransferase antibody

Supplementary info

Activity summary

Phosphoserine Aminotransferase (PSAT1) is an enzyme that actively participates in amino acid metabolism. It is also known by alternate names like O-phospho-L-serine:2-oxoglutarate aminotransferase. With a molecular mass of approximately 39 kDa PSAT1 facilitates the conversion of 3-phosphohydroxypyruvate to phosphoserine. You can find its expression across various tissues including liver brain and kidney. This widespread presence suggests its essential role in cellular functions and metabolism.

Biological function summary

PSAT1 plays an important role in the biosynthesis of the amino acid serine. It is part of a multi-step serine biosynthesis complex involving other enzymes like 3-phosphoglycerate dehydrogenase and phosphoserine phosphatase. PSAT1 works in conjunction with these enzymes to ensure the proper synthesis of serine which is vital for nucleotide synthesis and cell proliferation. This function establishes PSAT1 as an important regulator of cellular growth and division.

Pathways

PSAT1 is a significant component of the serine biosynthesis pathway which is linked to the folate cycle. This metabolic pathway is important for one-carbon metabolism affecting thymidine and purine synthesis. PSAT1 interacts with proteins such as 3-phosphoglycerate dehydrogenase highlighting its involvement in these interconnected metabolic processes. This connection indicates the critical position that PSAT1 holds in facilitating the production of biomolecules essential for cell survival and function.

Associated diseases and disorders

PSAT1 has been associated with conditions such as Neu-Laxova syndrome and certain cancer types. Neu-Laxova syndrome linked to defects in serine biosynthesis involves abnormal neurological and physical development. Additionally PSAT1's role in cell proliferation pathways associates it with oncogenic processes where its altered expression can lead to tumor growth. Dysregulation of related proteins like phosphoserine phosphatase further ties PSAT1 to the pathogenesis of these conditions making it a target of interest in therapeutic research.