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L-serine deficiency: on the properties of the Asn133Ser variant of human phosphoserine phosphatase

Sci Rep. 2024-05; 
Loredano Pollegioni, Barbara Campanini, Jean-Marc Good, Zoraide Motta, Giulia Murtas, Valeria Buoli Comani, Despina-Christina Pavlidou, No?lle Mercier, Laureane Mittaz-Crettol, Silvia Sacchi, Francesco Marchesani
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Proteins, Expression, Isolation and Analysis … The plasmid carrying the mutation coding for the Asn133Ser substitution was prepared by GenScript. The proteins were expressed and purified using a published procedure 22 . The … Get A Quote

摘要

The non-essential amino acid L-serine is involved in a number of metabolic pathways and in the brain its level is largely due to the biosynthesis from the glycolytic intermediate D-3-phosphoglycerate by the phosphorylated pathway (PP). This cytosolic pathway is made by three enzymes proposed to generate a reversible metabolon named the "serinosome". Phosphoserine phosphatase (PSP) catalyses the last and irreversible step, representing the driving force pushing L-serine synthesis. Genetic defects of the PP enzymes result in strong neurological phenotypes. Recently, we identified the homozygous missense variant [NM_004577.4: c.398A?>?G p.(Asn133Ser)] in the PSPH, the PSP encoding gene, in two siblings with a ... More

關鍵詞

Genetic disease, Phosphorylated pathway, Serine deficiency, Structure–function relationships
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