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Related Concept Videos

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...
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,...
Catalytically Perfect Enzymes01:07

Catalytically Perfect Enzymes

The theory of catalytically perfect enzymes was first proposed by W.J. Albery and J. R. Knowles in 1976. These enzymes catalyze biochemical reactions at high-speed. Their catalytic efficiency values range from 108-109 M-1s-1. These enzymes are also called 'diffusion-controlled' as the only rate-limiting step in the catalysis is that of the substrate diffusion into the active site. Examples include triose phosphate isomerase, fumarase, and superoxide dismutase.
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...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...

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A New Screening Method for the Directed Evolution of Thermostable Bacteriolytic Enzymes
13:30

A New Screening Method for the Directed Evolution of Thermostable Bacteriolytic Enzymes

Published on: November 7, 2012

Rational engineering of enzyme allosteric regulation through sequence evolution analysis.

Jae-Seong Yang1, Sang Woo Seo, Sungho Jang

  • 1School of Interdisciplinary Bioscience and Bioengineering, Pohang University of Science and Technology, Pohang, Gyeongbuk, Korea.

Plos Computational Biology
|July 19, 2012
PubMed
Summary

Scientists engineered enzymes to control metabolic flux by altering allosteric regulation. This method reduces enzyme inhibition without impacting catalytic efficiency, aiding metabolic engineering.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Metabolic Engineering

Background:

  • Enzyme allosteric regulation is crucial for controlling metabolic flux.
  • Rational engineering of allosteric enzymes without compromising catalytic activity remains challenging.
  • Understanding allosteric ligand-binding site characteristics is key to enzyme design.

Purpose of the Study:

  • To develop an effective strategy for deregulating enzyme allosteric inhibition.
  • To investigate the molecular evolution and physicochemical properties of allosteric ligand-binding sites.
  • To engineer fructose-1,6-bisphosphatase (FBPase) for reduced allosteric inhibition.

Main Methods:

  • Analysis of evolutionary variability and residue hydrophobicity in allosteric vs. catalytic sites.
  • Design of mutations targeting specific residues in FBPase based on site characteristics.
  • Substitution of charged amino acids with hydrophobic or neutral residues at less conserved positions.

Main Results:

  • Allosteric sites exhibit higher evolutionary variability and hydrophobicity compared to catalytic sites.
  • Engineered E. coli FBPase showed significantly diminished allosteric inhibition.
  • Catalytic efficiency of the engineered FBPase remained unaffected.

Conclusions:

  • The study presents a successful strategy for deregulating enzyme allosteric inhibition.
  • The findings facilitate the rational design of enzyme allosteric regulation.
  • This approach can aid in controlling metabolic flux for biotechnological applications.