ArticleProtein science : a publication of the Protein Society2023
L-serine biosynthesis in the human central nervous system: Structure and function of phosphoserine aminotransferase.
Article in Protein science : a publication of the Protein Society, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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12 citing papers in PubMed, 18 citations in OpenAlex.
- Targeting PSAT1 in diabetic kidney disease: a ferroptosis-driven strategy for precision therapy.Molecular and cellular biochemistry · 2026Article
- A phosphoserine phosphatase variant present in the brain of Alzheimer's disease patients favors nuclear mistargeting.The FEBS journal · 2025Article
- Nonessential amino acid is not nonessential in geriatric patients: implications for maxillofacial wound healing and bone repair.Maxillofacial plastic and reconstructive surgery · 2025Review
- Article
- On the quaternary structure of human D-3-phosphoglycerate dehydrogenase.Protein science : a publication of the Protein Society · 2024Article
- Identification of Small Molecule Inhibitors Targeting Phosphoserine Phosphatase: A Novel Target for the Development of Antiamoebic Drugs.ACS omega · 2024Article
- Engineering and finetuning expression of SerC for balanced metabolic flux in vitamin BSynthetic and systems biotechnology · 2024Article
- L-serine deficiency: on the properties of the Asn133Ser variant of human phosphoserine phosphatase.Scientific reports · 2024Article
- One substrate many enzymes virtual screening uncovers missing genes of carnitine biosynthesis in human and mouse.Nature communications · 2024Article
- N6-methyladenosine modification of LATS2 promotes hepatoblastoma progression by inhibiting ferroptosis through the YAP1/ATF4/PSAT1 axis.International journal of biological sciences · 2024Article
- Phosphoserine Aminotransferase Pathogenetic Variants in Serine Deficiency Disorders: A Functional Characterization.Biomolecules · 2023Article
- L-serine biosynthesis in the human central nervous system: Structure and function of phosphoserine aminotransferase.Protein science : a publication of the Protein Society · 2023Article
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11 authors at 4 institutions in 2 countries.
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Abstract
Organisms from all kingdoms of life synthesize L-serine (L-Ser) from 3-phosphoglycerate through the phosphorylated pathway, a three-step diversion of glycolysis. Phosphoserine aminotransferase (PSAT) catalyzes the intermediate step, the pyridoxal 5'-phosphate-dependent transamination of 3-phosphohydroxypyruvate and L-glutamate to O-phosphoserine (OPS) and α-ketoglutarate. PSAT is particularly relevant in the central nervous system of mammals because L-Ser is the metabolic precursor of D-serine, cysteine, phospholipids, and nucleotides. Several mutations in the human psat gene have been linked to serine deficiency disorders, characterized by severe neurological symptoms. Furthermore, PSAT is overexpressed in many tumors and this overexpression has been associated with poor clinical outcomes. Here, we report the detailed functional and structural characterization of the recombinant human PSAT. The reaction catalyzed by PSAT is reversible, with an equilibrium constant of about 10, and the enzyme is very efficient, with a k
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