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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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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...
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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...
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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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Updated: Mar 19, 2026

A Customizable Approach for the Enzymatic Production and Purification of Diterpenoid Natural Products
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Engineering Distant Allosteric Networks To Remodel the Substrate Access Channel for Efficient β-Arbutin Biosynthesis.

Xinyue Zhang1, Hanwen Fan1, Jie Zheng1

  • 1School of Food Science and Pharmaceutical Engineering, Nanjing Normal University, Nanjing 210023, China.

Journal of Agricultural and Food Chemistry
|March 17, 2026
PubMed
Summary

Researchers enhanced beta-arbutin production using a novel biocatalyst design. By targeting distant enzyme residues, they significantly improved glycosyltransferase performance and yield.

Keywords:
enzyme engineeringglycosyltransferasesemirational designβ-arbutin

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Area of Science:

  • Biocatalysis and Enzyme Engineering
  • Metabolic Engineering
  • Synthetic Biology

Background:

  • Efficient production of beta-arbutin (a skin-lightening agent) is limited by the low catalytic efficiency of glycosyltransferases.
  • Conventional enzyme engineering strategies often focus on active-site modifications, which have limitations.

Purpose of the Study:

  • To develop a novel global dynamic design strategy for improving glycosyltransferase performance in whole-cell biocatalysis.
  • To enhance the catalytic efficiency and stability of enzymes for beta-arbutin production.

Main Methods:

  • Integrated dynamic cross-correlation matrix analysis with computational screening to identify key distal flexible residues.
  • Employed principal component analysis, free energy landscapes, and double mutant cycles for mechanistic elucidation.
  • Engineered a variant (G35L) by targeting a distal residue.

Main Results:

  • The G35L variant showed significantly improved enzyme kinetics and thermal stability compared to the wild type.
  • Mechanistic studies revealed functional coupling between the distal mutation and the active site, stabilizing the transition state and optimizing the substrate tunnel.
  • Optimized whole-cell biocatalysis with the G35L variant achieved a beta-arbutin titer of 8.99 g/L, a 4.14-fold improvement.

Conclusions:

  • Distal dynamic network targeting is a powerful and effective paradigm for optimizing biocatalyst performance.
  • This strategy offers a promising approach for enhancing the production of valuable compounds like beta-arbutin.