Phosphoserine aminotransferase 1 (PSAT1)

Phosphoserine aminotransferase 1 (PSAT1) is a pyridoxal 5'-phosphate (PLP)-dependent enzyme that catalyzes the reversible transamination of 3-phosphohydroxypyruvate and L-glutamate to form O-phosphoserine and α-ketoglutarate, representing the second step of the phosphorylated pathway for L-serine biosynthesis[1][4][5][6]. This enzyme is especially important in the central nervous system, where L-serine is vital for nucleotide, phospholipid, and D-serine synthesis[4][5]. Mutations in PSAT1 can cause rare serine deficiency disorders with severe neurological manifestations[4][5]. PSAT1 is also overexpressed in several cancers, where it supports tumor cell proliferation and survival[4][2][5]. Preclinical data suggest that enhancing PSAT1 activity can promote cardiomyocyte proliferation and repair after myocardial infarction[2]. PSAT1 is thus emerging as a context-dependent therapeutic target in oncology, neurology, and regenerative medicine.

Other names

PSAT1PSAphosphoserine transaminasephosphohydroxythreonine aminotransferase

Enzyme inhibition (hypothetical/under development; reducing PSAT1 lowers serine synthesis, affecting cancer cell proliferation[2]); Enzyme augmentation (experimental: e.g., modRNA delivery to stimulate cardiac repair by promoting serine synthesis post-injury[2])