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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

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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Tairum, Carlos A. [1, 2] ; Santos, Melina Cardoso [1] ; Breyer, Carlos Alexandre [1] ; Pires de Oliveira, Ana Laura [1] ; Montanhero Cabrera, Vitoria Isabela [1] ; Toledo-Silva, Guilherme [3] ; Mori, Gustavo Maruyama [4] ; Toyama, Marcos Hikari [1] ; Soares Netto, Luis Eduardo [2] ; de Oliveira, Marcos Antonio [1]
Total Authors: 10
[1] Univ Estadual Paulista, Inst Biociencias, UNESP, BR-01049010 Sao Vicente - Brazil
[2] Univ Sao Paulo, Inst Biociencias, Dept Genet & Biol Evolut, BR-01049010 Sao Paulo - Brazil
[3] Univ Fed Santa Catarina, Dept Bioquim, Lab Biomarcadores Contaminacao Aquat & Imunoquim, BR-88040900 Florianopolis, SC - Brazil
[4] Univ Estadual Paulista, Inst Biociencias, Lab Ecol Mol, UNESP, BR-01049010 Sao Vicente - Brazil
Total Affiliations: 4
Document type: Journal article
Source: ANTIOXIDANTS; v. 10, n. 7 JUL 2021.
Web of Science Citations: 1

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 (C-P) 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. (AU)

FAPESP's process: 17/20291-0 - Characterization of the proinflammatory activity of a new serine protease (cdtsp-2) purified from the total venom of Crotalus durissus terrificus
Grantee:Marcos Hikari Toyama
Support type: Regular Research Grants
FAPESP's process: 20/02868-1 - Effects of natural compounds over the peroxidase activity of AhpCs and pathogenic bacteria survival
Grantee:Vitória Isabela Montanhero Cabrera
Support type: Scholarships in Brazil - Master
FAPESP's process: 17/06263-4 - Evaluation of bioactive molecules as inhibitors for atioxidant system of typical 2-Cys peroxiredoxins (AhpC) in baceria
Grantee:Melina Cardoso dos Santos
Support type: Scholarships in Brazil - Doctorate
FAPESP's process: 19/04054-4 - Search of inhibitors of typical 2-Cys peroxirredoxin system from eukaryotes: functional and structural evaluation
Grantee:Ana Laura Pires de Oliveira
Support type: Scholarships in Brazil - Master
FAPESP's process: 17/19942-7 - Search for inhibitors of the peroxirredoxin system from pathogens and humans
Grantee:Marcos Antonio de Oliveira
Support type: Regular Research Grants
FAPESP's process: 13/07937-8 - Redoxome - Redox Processes in Biomedicine
Grantee:Ohara Augusto
Support type: Research Grants - Research, Innovation and Dissemination Centers - RIDC
FAPESP's process: 18/12628-8 - AhpC from Salmonella typhimurium and Staphylococcus aureus: investigation of the inhibitory potential of Adenantine on bacterial peroxiredoxins
Grantee:Camila Perussi Inácio
Support type: Scholarships in Brazil - Scientific Initiation
FAPESP's process: 11/13500-6 - Investigation of the molecular determinants involved in the interaction with substrates of Tsa1 and Tsa2 of Saccharomyces cerevisiae
Grantee:Carlos Alexandre Breyer
Support type: Scholarships in Brazil - Doctorate