Allostery, in which binding of ligands to remote sites causes a functional change in the active sites, is a fascinating phenomenon observed in enzymes. Allostery can occur either with or without significant conformational changes in the enzymes, and the molecular basis of its mechanism can be difficult to decipher using only experimental techniques. Computational tools for analyzing enzyme sequences, structures, and dynamics can provide insights into the allosteric mechanism at the atomic level. Combining computational and experimental methods offers a powerful strategy for the study of enzyme allostery. The aromatic amino acid biosynthesis pathway is essential in microorganisms and plants. Multiple enzymes involved in this pathway are sensitive to feedback regulation by pathway end products and are known to use allostery to control their activities. To date, four enzymes in the aromatic amino acid biosynthesis pathway have been computationally investigated for their allosteric mechanisms, including 3-deoxy-d-arabino-heptulosonate 7-phosphate synthase, anthranilate synthase, chorismate mutase, and tryptophan synthase. Here we review the computational studies and findings on the allosteric mechanisms of these four enzymes. Results from these studies demonstrate the capability of computational tools and encourage future computational investigations of allostery in other enzymes of this pathway.
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February 2021
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On the implications of the copper co-factor in lytic polysaccharide monooxygenase. A brief overview of structure, oxygen activation and application as bioindustrial process tools for decomposition of lignocellulose. Further information can be found in the review by Ipsen and colleagues (pages 531–540). Image provided by Katja Johansen.
Review Article|
February 05 2021
Computational investigations of allostery in aromatic amino acid biosynthetic enzymes
Wanting Jiao
1Ferrier Research Institute, Victoria University of Wellington, Wellington, New Zealand
2Maurice Wilkins Centre for Molecular Biodiscovery, Auckland, New Zealand
Correspondence: Wanting Jiao (wanting.jiao@vuw.ac.nz)
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Publisher: Portland Press Ltd
Received:
November 25 2020
Revision Received:
January 14 2021
Accepted:
January 15 2021
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© 2021 The Author(s). Published by Portland Press Limited on behalf of the Biochemical Society
2021
Biochem Soc Trans (2021) 49 (1): 415–429.
Article history
Received:
November 25 2020
Revision Received:
January 14 2021
Accepted:
January 15 2021
Citation
Wanting Jiao; Computational investigations of allostery in aromatic amino acid biosynthetic enzymes. Biochem Soc Trans 26 February 2021; 49 (1): 415–429. doi: https://doi.org/10.1042/BST20200741
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