Impaired local hydrophobicity, structural stability and conformational flexibility due to point mutations in SULT1 family of enzymes Scientific paper

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Published: Sep 20, 2023
Updated: 20.09.2023
DOI: https://doi.org/10.2298/JSC230210022C
Keywords:
protein plasticity protein stability hydrophobicity profile mutations metabolism bioinformatics

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Silvana Ceauranu
West University of Timișoara, Faculty of Chemistry, Biology, Geography and Advanced Research Environmental Laboratories, 16 H. Pestalozzi, 300115 Timișoara, Romania
https://orcid.org/0009-0004-3995-2823
Vasile Ostafe
West University of Timisoara
https://orcid.org/0000-0003-1352-1115
Adriana Isvoran
West University of Timisoara, Timisoara, Romania
https://orcid.org/0000-0002-3068-2642

Abstract

Sulfotransferases (SULTs) are enzymes involved in phase II of the metabolism of xenobiotics. Single nucleotide polymorphisms were identified for genes encoding the SULTs leading to allozymes with modified sulfating activity. This study aims to analyse the effects of the most frequently identified amino acid mutations in the sequences of enzymes belonging to the SULT1 family on their local properties and structural stability. The outcomes reveal that single point mutations alter the local hydrophobicity and flexibility, mainly due to destabilization of the protein structures, may consequently lead to changes in the dynamic of the active site activity reducing the affinity for the substrate. Elucidation of how the single point mutations influence the activity of enzymes contributes to understanding the molecular basis of the specificity of enzymatic activity and mitigating anomalies in the metabolism of xeno­biotics.

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How to Cite
[1]
S. Ceauranu, V. Ostafe, and A. Isvoran, “Impaired local hydrophobicity, structural stability and conformational flexibility due to point mutations in SULT1 family of enzymes: Scientific paper”, J. Serb. Chem. Soc., vol. 88, no. 9, pp. 841–857, Sep. 2023.
Issue
Vol. 88 No. 9 (2023)
Section
Biochemistry & Biotechnology
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