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In silico approaches to study the human asparagine synthetase: An insight of the interaction between the enzyme active sites and its substrates
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In silico approaches to study the human asparagine synthetase: An insight of the interaction between the enzyme active sites and its substrates
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Journal Article
In silico approaches to study the human asparagine synthetase: An insight of the interaction between the enzyme active sites and its substrates
2024
Overview
Cancer is a leading concern and important cause of death worldwide. Cancer is a non-communicable illness defined as uncontrolled division of cells. It can develop into metastatic cancer when tumor cells migrate to other organs. In recent years evidence has emerged that the bioavailability of Asn play a crucial role in cancer metastasis. Asn is a non-essential amino acid formed from an ATP dependent catalyzed reaction by the enzyme asparagine synthetase (ASNS), where Asp and Gln are converted to Asn and Glu, respectively. The human ASNS enzyme consist of 561 amino acids, with a molecular weight of 64 KDa. ASNS governs the activation of transcriptional factors that regulate the process of metastasis. In this work the 3D model of ASNS in
E
.
coli
(AS-B) and the human ASNS docked with its different ligands have been used to study the 3D mechanism of the conversion of Asp and Gln to Asn and Glu, in human ASNS. The stability evaluation of the docked complexes was checked by molecular dynamic simulation through the bioinformatic tool Desmond. The binding residues and their interactions can be exploited for the development of inhibitors, as well as for finding new drug molecules against ASNS and prevention of metastatic cancer.
Publisher
Public Library of Science,Public Library of Science (PLoS)
Subject
/ Aspartate-Ammonia Ligase - chemistry
/ Aspartate-Ammonia Ligase - genetics
/ Aspartate-Ammonia Ligase - metabolism
/ Cancer
/ Carbon-Nitrogen Ligases with Glutamine as Amide-N-Donor
/ E coli
/ Enzymes
/ Escherichia coli - enzymology
/ Escherichia coli - metabolism
/ Humans
/ Ligands
/ Ligases
/ Molecular Docking Simulation
/ Molecular Dynamics Simulation
/ Proteins
/ Software
