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The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
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Phenylketonuria (PKU) is a protein metabolism disorder characterized by high blood levels of the amino acid phenylalanine. This results from a mutation in the gene responsible for phenylalanine hydroxylase, an enzyme that converts phenylalanine into tyrosine. When this enzyme is deficient, phenylalanine builds up in the blood, leading to symptoms such as vomiting, rashes, seizures, growth deficiency, and severe mental retardation. An early diagnosis and a diet restricting phenylalanine intake...
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Lesson: Translation
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ATP synthase or ATPase is among the most conserved proteins found in bacteria, mammals, and plants. This enzyme can catalyze a forward reaction in response to the electrochemical gradient, producing ATP from ADP and inorganic phosphate. ATP synthase can also work in a reverse direction by hydrolyzing ATP and generating an electrochemical gradient. Different forms of ATP synthases have evolved special features to meet the specific demands of the cell. Based on their specific feature, ATP...
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Phosphoserine Aminotransferase Pathogenetic Variants in Serine Deficiency Disorders: A Functional Characterization.

Francesco Marchesani1, Annalisa Michielon2, Elisabetta Viale3

  • 1Department of Medicine and Surgery, University of Parma, 43124 Parma, Italy.

Biomolecules
|August 26, 2023
PubMed
Summary

Serine deficiency disorders (SDDs) stem from defects in the phosphorylated pathway (PP). This study reveals diverse PSAT enzyme dysfunctions, including altered affinity, stability, and activity, confirming their role in causing SDDs.

Keywords:
Neu–Laxova syndromeneurometabolic disordersphosphorylated pathwayphosphoserine aminotransferaseserine deficiency disorders

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Area of Science:

  • Biochemistry
  • Neuroscience
  • Metabolic Disorders

Background:

  • The phosphorylated pathway (PP) converts D-3-phosphoglycerate to L-serine.
  • Genetic defects in PP enzymes cause serine deficiency disorders (SDDs), particularly affecting the brain.
  • Phosphoserine aminotransferase (PSAT) is a key enzyme in the PP.

Purpose of the Study:

  • To investigate the pathogenetic mechanisms of PSAT variants associated with SDDs.
  • To characterize the functional impact of specific PSAT mutations.
  • To confirm the role of PSAT dysfunction in the etiology of SDDs.

Main Methods:

  • Recombinant expression and characterization of eight SDD-associated and two non-SDD PSAT variants.
  • Assessing cofactor affinity, thermal stability, aggregation, and kinetic parameters (Km, kcat).
  • In vitro reconstruction of the PP to measure flux sensitivity to PSAT variant properties.

Main Results:

  • SDD-associated PSAT variants exhibit diverse defects: altered pyridoxal 5'-phosphate affinity, thermal instability, holo-form activity loss, aggregation, and modified substrate kinetics.
  • Specific mutations like S179L and G79W caused cofactor affinity issues and instability.
  • R342W led to loss of holo-form activity, D100A caused aggregation, S43R showed increased Km, and C245R had combined kinetic impairments.

Conclusions:

  • Pathogenetic mechanisms in SDDs are highly diverse, involving multiple functional impairments of PSAT.
  • PSAT dysfunctions significantly impact flux through the phosphorylated pathway.
  • These findings confirm that PSAT alterations are a direct cause of serine deficiency disorders.