Anti-PSPH antibody [EPR26995-51] - BSA and Azide free (Capture)

Supplementary info

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

Activity summary

Phosphoserine phosphatase (PSPH) also known as O-phosphoserine phosphohydrolase plays an essential role in serine biosynthesis by catalyzing the conversion of O-phospho-L-serine to L-serine. PSPH is a protein with a molecular weight of approximately 25 kDa. It is expressed across a wide range of tissues with notable expression in the liver kidney and brain. The enzyme activity of PSPH ensures the availability of serine a non-essential amino acid involved in multiple biochemical processes.

Biological function summary

Phosphoserine phosphatase contributes significantly to cellular metabolism and growth by its involvement in the serine biosynthesis pathway. This pathway is important for providing serine which acts as a precursor for proteins nucleotides and other biologically important molecules. PSPH does not function as part of a larger complex; however its enzymatic action is critical for maintaining levels of serine when dietary intake is low. In addition to its role in metabolism PSPH influences cell proliferation and differentiation through providing the necessary serine reserves.

Pathways

Phosphoserine phosphatase integrates into the serine biosynthesis pathway and shows a connection to the glycolytic pathway. The enzyme catalyzes one of the final steps in the phosphorylated serine synthesis process that branches from glycolysis. This pathway features interactions with enzymes like 3-phosphoglycerate dehydrogenase (PHGDH) and phosphoserine aminotransferase 1 (PSAT1) which work sequentially to produce 3-phosphoserine from 3-phosphoglycerate. PSPH follows these enzymes completing the conversion to serine and connects the serine biosynthesis cycle to broader metabolic activities.

Associated diseases and disorders

Altered expression or function of phosphoserine phosphatase associates with conditions such as cancer and neurodegenerative diseases. Within oncogenesis elevated activity of PSPH can supply cancer cells with serine needed for rapid proliferation and this enzyme interplays with other metabolic proteins like PHGDH in cancer metabolism. In neurodegenerative disorders deficient PSPH activity disrupts serine availability leading to harmful effects on the nervous system. Understanding PSPH's role in these conditions can provide insights into therapeutic strategies targeting serine metabolism.