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Related Concept Videos

Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

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 pathway,...
Ligand Binding and Linkage00:49

Ligand Binding and Linkage

Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence the...
ATP Yield01:31

ATP Yield

Cellular respiration produces 30 - 32 ATP per glucose molecule. Although most of the ATP results from oxidative phosphorylation and the electron transport chain (ETC), 4 ATP are gained beforehand (2 from glycolysis and 2 from the citric acid cycle).
The ETC is embedded in the inner mitochondrial membrane and is comprised of four main protein complexes and an ATP synthase. NADH and FADH2 pass electrons to these complexes, which pump protons into the intermembrane space. This distribution of...
Allosteric Regulation01:08

Allosteric Regulation

Allosteric regulation of enzymes occurs when the binding of an effector molecule to a site that is different from the active site causes a change in the enzymatic activity. This alternate site is called an allosteric site, and an enzyme can contain more than one of these sites. Allosteric regulation can either be positive or negative, resulting in an increase or decrease in enzyme activity. Most enzymes that display allosteric regulation are metabolic enzymes involved in the degradation or...
Allosteric Regulation01:08

Allosteric Regulation

Allosteric regulation of enzymes occurs when the binding of an effector molecule to a site that is different from the active site causes a change in the enzymatic activity. This alternate site is called an allosteric site, and an enzyme can contain more than one of these sites. Allosteric regulation can either be positive or negative, resulting in an increase or decrease in enzyme activity. Most enzymes that display allosteric regulation are metabolic enzymes involved in the degradation or...
ATP and Macromolecule Synthesis01:28

ATP and Macromolecule Synthesis

Biological macromolecules are organic compounds, predominantly composed of carbon atoms. The carbon atoms are covalently bonded with hydrogen, oxygen, nitrogen, and other minor elements. There are four major biological macromolecule classes: carbohydrates, lipids, proteins, and nucleic acids.
Most macromolecules are composed of single subunits, or building blocks, called monomers. The monomers combine with each other using covalent bonds to form larger molecules known as polymers.
Conversion of...

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Related Experiment Video

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Studying DNA Looping by Single-Molecule FRET
11:27

Studying DNA Looping by Single-Molecule FRET

Published on: June 28, 2014

A loop matters for FTO substrate selection.

Zhifu Han1, Ning Huang, Tianhui Niu

  • 1National Institute of Biological Sciences, No. 7 Science Park Road, Beijing, 102206, China.

Protein & Cell
|January 5, 2011
PubMed
Summary
This summary is machine-generated.

The fat mass and obesity-associated gene (FTO) is linked to obesity and functions as a DNA/RNA demethylase. Structural and biochemical studies reveal FTO

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Last Updated: Jun 5, 2026

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Area of Science:

  • Biochemistry
  • Genetics
  • Molecular Biology

Background:

  • Recent studies confirm a strong association between the FTO gene and obesity.
  • FTO is identified as a member of the AlkB-like family of DNA/RNA demethylases.
  • FTO exhibits unique substrate specificity and possesses an extended C-terminus with currently unknown functions compared to other AlkB family members.

Purpose of the Study:

  • To elucidate the substrate selection mechanism of FTO.
  • To gain functional insights into the role of FTO's extended C-terminus.
  • To provide a basis for designing FTO-specific inhibitors for obesity treatment.

Main Methods:

  • Structural biology techniques (e.g., X-ray crystallography) to determine FTO's 3D structure.
  • Biochemical assays to investigate FTO's enzymatic activity and substrate interactions.
  • Structure-function relationship analyses.

Main Results:

  • Detailed structural insights into how FTO selects its substrates have been obtained.
  • The extended C-terminus of FTO has been investigated, providing clues to its function.
  • Understanding of FTO's unique biochemical properties has been enhanced.

Conclusions:

  • Recent structural and biochemical studies have significantly advanced our understanding of FTO.
  • These findings are crucial for developing targeted inhibitors for FTO.
  • The potential for therapeutic agents targeting FTO in obesity and related diseases is highlighted.