The role of S126 in the Staphylococcus equorum MnSOD activity and stability

Retnoningrum, Debbie Soefie; Yoshida, Hiromi; Razani, M.; Muliadi, Rahmat; Meidianto, Vincencius Felix; Artarini, Anita; Ismaya, Wangsa T.

doi:10.1016/j.jsb.2021.107731

Cited by 4 publications

(3 citation statements)

References 26 publications

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“…Although the L169W mutant was dimeric like the wild-type, it had an altered monomeric form. However, enzyme activity was similar to that of the wild type [26]. Another mutant, N73F was generated, and the substitution was at the dimer interface.…”

Section: Significance Of the Mnsod Quaternary Structurementioning

confidence: 88%

“…Conservation of the N73-F124 bonding in the structure of human MnSOD further supports the importance of these residues in maintaining the dimer structure. Residue S126 is also involved in interactions at the dimer interface [26]. Another substitution in S. equorum MnSOD, S126C ( S-S bond breakage due to the neighboring tryptophan residue.…”

Section: Significance Of the Mnsod Quaternary Structurementioning

confidence: 99%

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The structure–function relationships and physiological roles of MnSOD mutants

Bonetta

2022

Bioscience Reports

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In this review, we focus on understanding the structure-function relationships of numerous manganese superoxide dismutase (MnSOD) mutants to investigate the role that various amino acids play to maintain enzyme quaternary structure or the active site structure, catalytic potential and metal homeostasis in MnSOD, which is essential to maintain enzyme activity. We also observe how polymorphisms of MnSOD are linked to pathologies and how post-translational modifications affect the antioxidant properties of MnSOD. Understanding how modified forms of MnSOD may act as tumor promoters or suppressors by altering the redox status in the body, ultimately aid in generating novel therapies that exploit the therapeutic potential of mutant MnSODs or pave the way for the development of synthetic SOD mimics.

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Section: Significance Of the Mnsod Quaternary Structurementioning

confidence: 88%

Section: Significance Of the Mnsod Quaternary Structurementioning

confidence: 99%

The structure–function relationships and physiological roles of MnSOD mutants

Bonetta

2022

Bioscience Reports

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“…Stabilization of homodimeric enzymes can be achieved through different approaches such as introducing disulfide bonds between the subunit–subunit interfaces − or stable mutations to strengthen subunit interactions and prevent homodimeric enzyme dissociation. Protein engineering techniques like directed evolution (DE), and prediction of hot spot amino acids , can also be used to rationally introduce stabilization to the interface.…”

Section: Biological Necessity Of Dimeric Enzymesmentioning

confidence: 99%

New Insights into the Cooperativity and Dynamics of Dimeric Enzymes

Chen

Sun

2023

Chem. Rev.

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A survey of protein databases indicates that the majority of enzymes exist in oligomeric forms, with about half of those found in the UniProt database being homodimeric. Understanding why many enzymes are in their dimeric form is imperative. Recent developments in experimental and computational techniques have allowed for a deeper comprehension of the cooperative interactions between the subunits of dimeric enzymes. This review aims to succinctly summarize these recent advancements by providing an overview of experimental and theoretical methods, as well as an understanding of cooperativity in substrate binding and the molecular mechanisms of cooperative catalysis within homodimeric enzymes. Focus is set upon the beneficial effects of dimerization and cooperative catalysis. These advancements not only provide essential case studies and theoretical support for comprehending dimeric enzyme catalysis but also serve as a foundation for designing highly efficient catalysts, such as dimeric organic catalysts. Moreover, these developments have significant implications for drug design, as exemplified by Paxlovid, which was designed for the homodimeric main protease of SARS-CoV-2.

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