Effects of serine or threonine in the active site of typical 2-cys prx on hyperoxidation susceptibility and on chaperone activity
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Data
2021-07-01
Autores
Tairum, Carlos A. [UNESP]
Santos, Melina Cardoso [UNESP]
Breyer, Carlos Alexandre [UNESP]
de Oliveira, Ana Laura Pires [UNESP]
Cabrera, Vitoria Isabela Montanhero [UNESP]
Toledo-Silva, Guilherme
Mori, Gustavo Maruyama [UNESP]
Toyama, Marcos Hikari [UNESP]
Netto, Luis Eduardo Soares
de Oliveira, Marcos Antonio [UNESP]
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Resumo
Typical 2-Cys peroxiredoxins (2-Cys Prx) are ubiquitous Cys-based peroxidases, which are stable as decamers in the reduced state, and may dissociate into dimers upon disulfide bond formation. A peroxidatic Cys (CP) takes part of a catalytic triad, together with a Thr/Ser and an Arg. Previously, we described that the presence of Ser (instead of Thr) in the active site stabilizes yeast 2-Cys Prx as decamers. Here, we compared the hyperoxidation susceptibilities of yeast 2-Cys Prx. Notably, 2-Cys Prx containing Ser (named here Ser-Prx) were more resistant to hyperoxidation than enzymes containing Thr (Thr-Prx). In silico analysis revealed that Thr-Prx are more frequent in all domains of life, while Ser-Prx are more abundant in bacteria. As yeast 2-Cys Prx, bacterial Ser-Prx are more stable as decamers than Thr-Prx. However, bacterial Ser-Prx were only slightly more resistant to hyperoxidation than Thr-Prx. Furthermore, in all cases, organic hydroperoxide inhibited more the peroxidase activities of 2-Cys Prx than hydrogen peroxide. Moreover, bacterial Ser-Prx displayed increased thermal resistance and chaperone activity, which may be related with its enhanced stability as decamers compared to Thr-Prx. Therefore, the single substitution of Thr by Ser in the catalytic triad results in profound biochemical and structural differences in 2-Cys Prx.
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Palavras-chave
2-Cys Prx, Catalytic triad, Chaperone, Hyperoxidation, Oligomerization, Organic hydroperoxides
Como citar
Antioxidants, v. 10, n. 7, 2021.