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ATP Synthase: Structure01:18

ATP Synthase: Structure

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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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Allosteric Proteins-ATCase01:19

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Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to  N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...
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ATP Synthase: Mechanism01:48

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In animals, the mitochondrial F1F0 ATP synthase is the key protein that synthesizes ATP molecules through a complex catalytic mechanism. While the nuclear genome encodes the majority of ATP synthase subunits, the mitochondrial genome encodes some of the enzyme's most critical components. The formation of this multi-subunit enzyme is a complex multi-step process regulated at the level of transcription, translation, and assembly. Defects in one or more of these steps can result in decreased...
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Amino Acid Biosynthetic Pathways01:29

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Amino acid biosynthesis is essential for cell growth, protein synthesis, and metabolic regulation. Cells generate essential and non-essential amino acids from metabolic intermediates to sustain vital biological functions. These intermediates originate from key metabolic pathways: glycolysis, the tricarboxylic acid (TCA) cycle, and the pentose phosphate pathway. Important precursors include α-ketoglutarate, pyruvate, oxaloacetate, phosphoenolpyruvate, and erythrose-4-phosphate, which...
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Protein and Protein Structure02:15

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Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
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Enzymes02:34

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Inside living organisms, enzymes act as catalysts for many biochemical reactions involved in cellular metabolism. The role of enzymes is to reduce the activation energies of biochemical reactions by forming complexes with its substrates. The lowering of activation energies favor an increase in the rates of biochemical reactions.
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Combining Double Fluorescence In Situ Hybridization with Immunolabelling for Detection of the Expression of Three Genes in Mouse Brain Sections
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Asparagine synthetase: Function, structure, and role in disease.

Carrie L Lomelino1, Jacob T Andring1, Robert McKenna1

  • 1Department of Biochemistry and Molecular Biology, Shands Cancer Center, College of Medicine, University of Florida, Gainesville, Florida 32610.

The Journal of Biological Chemistry
|November 1, 2017
PubMed
Summary

Asparagine synthetase (ASNS) is crucial for cell growth and is linked to cancer therapy resistance. Mutations in the ASNS gene cause asparagine synthetase deficiency (ASD), leading to severe developmental issues.

Keywords:
acute lymphoblastic leukemiaamino acidamino acid metabolismasparaginase resistancebrain developmentbrain metabolismgenetic diseaseinborn error of metabolismneurological diseaseprotein structure

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Area of Science:

  • Biochemistry
  • Genetics
  • Molecular Biology

Background:

  • Asparagine synthetase (ASNS) catalyzes an ATP-dependent reaction converting aspartate and glutamine to asparagine and glutamate.
  • ASNS expression varies across mammalian organs and is responsive to cellular stress, primarily via transcriptional regulation.
  • Elevated ASNS expression is linked to asparaginase therapy resistance in childhood acute lymphoblastic leukemia and potentially in solid tumors.

Purpose of the Study:

  • To investigate the role of ASNS in cellular metabolism and its clinical implications.
  • To understand the genetic basis and phenotypic consequences of asparagine synthetase deficiency (ASD).
  • To explore the structural impact of ASD-associated mutations on ASNS function.

Main Methods:

  • Analysis of ASNS expression and activity in various tissues and under cellular stress.
  • Genetic analysis of patients with suspected ASD, including mutation identification in the ASNS gene.
  • Molecular modeling of ASNS protein structure using homology with E. coli ASNS-B.
  • Cell culture studies (fibroblast) to assess protein and mRNA synthesis/stability in ASD patients.

Main Results:

  • Fifteen unique mutations in the ASNS gene have been identified and associated with ASD.
  • ASD is characterized by developmental delays, intellectual disability, microcephaly, intractable seizures, and progressive brain atrophy.
  • Molecular modeling suggests ASD mutations are often located near catalytic sites or conserved regions, potentially impairing protein function.

Conclusions:

  • ASNS is vital for normal development, and its deficiency leads to severe neurological disorders.
  • Mutations in ASNS significantly impact protein structure and function, underlying the pathogenesis of ASD.
  • Further research into ASNS function and ASD pathogenesis is warranted for potential therapeutic strategies.