Functional analysis of amino acid residues Y61, F72 and H180 in uracil-DNA glycosylase from Staphylococcus aureus
Main Article Content
Authors
A.S. Koreneva
NCJSC «S. Seifullin Kazakh Agrotechnical Research University», 010000, Republic of Kazakhstan, Astana, Zhenis avenue, 62
S.K. Abeldenov
LLP «National center for biotechnology», 010000, Republic of Kazakhstan, Astana, Korgalzhyn highway, 13/5
A.M. Turgimbayeva
LLP «National center for biotechnology», 010000, Republic of Kazakhstan, Astana, Korgalzhyn highway, 13/5
Abstract
In this study, bioinformatic and in silico structural analysis of uracil-DNA glycosylase from Staphylococcus aureus (SaUDG) was performed, leading to identification the amino acid residues Y61, F72 and H180 as potentially important for the catalytic activity of the enzyme. Based on the obtained data, SaUDG Y61S, F72N and H180Q mutant variants were constructed. The results of the enzymatic analysis revealed the absence of detectable catalytic activity in SaUDG F72N and H180Q mutants, whereas the Y61S substitution led to a significant reduction in activity.
These data indicate the key role of the F72 and H180 amino acid residues in the catalytic mechanism of SaUDG and highlight the functional importance of the Y61 residue for maintaining enzymatic activity. Overall, these results provide further insight into the structure and mechanism of action of SaUDG and are consistent with previous data on the conserved organization of the active site in first-family UDG enzymes.
Keywords
Staphylococcus aureus, DNA repair, base excision repair, uracil-DNA glycosylase, site-directed mutagenesis, mutant variant
Article Details
References
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