Reference on EC 1.11.1.26 - NADH-dependent peroxiredoxin
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REF. 
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Logan, C.; Mayhew, S.G.
Cloning, overexpression, and characterization of peroxiredoxin and NADH peroxiredoxin reductase from Thermus aquaticus
J. Biol. Chem.
275
30019-30028
2000
Thermus aquaticus, Thermus aquaticus YT-1
Dip, P.V.; Kamariah, N.; Subramanian Manimekalai, M.S.; Nartey, W.; Balakrishna, A.M.; Eisenhaber, F.; Eisenhaber, B.; Gruber, G.
Structure, mechanism and ensemble formation of the alkylhydroperoxide reductase subunits AhpC and AhpF from Escherichia coli
Acta Crystallogr. Sect. D
70
2848-2862
2014
Escherichia coli (P0AE08 AND P35340), Escherichia coli, Escherichia coli K12 (P0AE08 AND P35340)
Nartey, W.; Basak, S.; Kamariah, N.; Manimekalai, M.S.; Robson, S.; Wagner, G.; Eisenhaber, B.; Eisenhaber, F.; Gruber, G.
NMR studies reveal a novel grab and release mechanism for efficient catalysis of the bacterial 2-Cys peroxiredoxin machinery
FEBS J.
282
4620-4638
2015
Escherichia coli (P0AE08 AND P35340), Escherichia coli K12 (P0AE08 AND P35340)
Nelson, K.; Perkins, A.; Van Swearingen, A.; Hartman, S.; Brereton, A.; Parsonage, D.; Salsbury, F.; Karplus, P.; Poole, L.
Experimentally dissecting the origins of peroxiredoxin catalysis
Antioxid. Redox Signal.
28
521-536
2018
Salmonella enterica subsp. enterica serovar Typhimurium, Salmonella enterica subsp. enterica serovar Typhimurium (P0A251), Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720 (P0A251)
Alharbi, A.; Rabadi, S.M.; Alqahtani, M.; Marghani, D.; Worden, M.; Ma, Z.; Malik, M.; Bakshi, C.S.
Role of peroxiredoxin of the AhpC/TSA family in antioxidant defense mechanisms of Francisella tularensis
PLoS One
14
e0213699
2019
Francisella tularensis subsp. holarctica, Francisella tularensis subsp. holarctica (A0A0B3VNJ6), Francisella tularensis subsp. tularensis, Francisella tularensis subsp. tularensis (A0A0B3VNJ6), Francisella tularensis subsp. holarctica LVS, Francisella tularensis subsp. holarctica LVS (A0A0B3VNJ6), Francisella tularensis subsp. tularensis SchuS4
Hong, S.H.; Singh, S.; Tripathi, B.N.; Mondal, S.; Lee, S.; Jung, H.S.; Cho, C.; Kaur, S.; Kim, J.H.; Lee, S.; Bai, H.W.; Bae, H.J.; Lee, S.Y.; Lee, S.S.; Chung, B.Y.
Functional properties and the oligomeric state of alkyl hydroperoxide reductase subunit F (AhpF) in Pseudomonas aeruginosa
Protoplasma
257
807-817
2020
Pseudomonas aeruginosa (Q9I6Z2), Pseudomonas aeruginosa
Lou, H.; Li, X.; Guo, F.; Ding, M.; Hu, Y.; Chen, H.; Yan, J.
Evaluations of alkyl hydroperoxide reductase B cell antigen epitope as a potential epitope vaccine against Campylobacter jejuni
Saudi J. Biol. Sci.
26
1117-1122
2019
Campylobacter jejuni (Q0PBH5), Campylobacter jejuni ATCC 700819 (Q0PBH5)
Guo, S.H.; Wang, H.F.; Nian, Z.G.; Wang, Y.D.; Zeng, Q.Y.; Zhang, G.
Immunization with alkyl hydroperoxide reductase subunit C reduces Fusobacterium nucleatum load in the intestinal tract
Sci. Rep.
7
10566
2017
Fusobacterium nucleatum (Q8R6D3), Fusobacterium nucleatum ATCC 25586 (Q8R6D3)
Kamariah, N.; Eisenhaber, B.; Eisenhaber, F.; Grber, G.
Molecular mechanism of the Escherichia coli AhpC in the function of a chaperone under heat-shock conditions
Sci. Rep.
8
14151
2018
Escherichia coli
Liu, F.; Min, R.; Hong, J.; Cheng, G.; Zhang, Y.; Deng, Y.
Quantitative proteomic analysis of ahpC/F and katE and katG knockout Escherichia coli-a useful model to study endogenous oxidative stress
Appl. Microbiol. Biotechnol.
105
2399-2410
2021
Escherichia coli, Escherichia coli MG1655
Portillo-Ledesma, S.; Randall, L.; Parsonage, D.; Rizza, J.; Andrew Karplus, P.; Poole, L.; Denicola, A.; Ferrer-Sueta, G.
Differential kinetics of two-cysteine peroxiredoxin disulfide formation reveal a novel model for peroxide sensing
Biochemistry
57
3416-3424
2018
Salmonella enterica subsp. enterica serovar Typhimurium
Pan, A.; Balakrishna, A.; Nartey, W.; Kohlmeier, A.; Dip, P.; Bhushan, S.; Grueber, G.
Atomic structure and enzymatic insights into the vancomycin-resistant Enterococcus faecalis (V583) alkylhydroperoxide reductase subunit C
Free Radic. Biol. Med.
115
252-265
2018
Enterococcus faecalis (H7C7A0)
Toh, Y.K.; Shin, J.; Balakrishna, A.M.; Kamariah, N.; Grueber, A.; Eisenhaber, F.; Eisenhaber, B.; Grueber, G.
Effect of the additional cysteine 503 of vancomycin-resistant Enterococcus faecalis (V583) alkylhydroperoxide reductase subunit F (AhpF) and the mechanism of AhpF and subunit C assembling
Free Radic. Biol. Med.
138
10-22
2019
Enterococcus faecalis
Zhang, B.; Gu, H.; Yang, Y.; Bai, H.; Zhao, C.; Si, M.; Su, T.; Shen, X.
Molecular mechanisms of AhpC in resistance to oxidative stress in Burkholderia thailandensis
Front. Microbiol.
10
1483
2019
Burkholderia thailandensis (Q2SWT3)
Wan, F.; Yin, J.; Sun, W.; Gao, H.
Oxidized OxyR up-regulates AhpCF expression to suppress plating defects of oxyR- and catalase-deficient strains
Front. Microbiol.
10
439
2019
Shewanella oneidensis, Shewanella oneidensis ATCC 700550
Wan, F.; Feng, X.; Yin, J.; Gao, H.
Distinct H2O2-scavenging system in Yersinia pseudotuberculosis KatG and AhpC act together to scavenge endogenous hydrogen peroxide
Front. Microbiol.
12
626874
2021
Yersinia pseudotuberculosis, Yersinia pseudotuberculosis YPIII
Feng, X.; Guo, K.; Gao, H.
Plasticity of the peroxidase AhpC links multiple substrates to diverse disulfide-reducing pathways in Shewanella oneidensis
J. Biol. Chem.
295
11118-11130
2020
Shewanella oneidensis
Sheludko, A.; Mokeev, D.; Evstigneeva, S.; Filipecheva, Y.; Burov, A.; Petrova, L.; Katsy, E.
Suppressed biofilm formation efficiency and decreased biofilm resistance to oxidative stress and drying in an Azospirillum brasilense ahpC mutant
Microbiology
90
56-65
2021
Azospirillum brasilense, Azospirillum brasilense SP245
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Rocha, L.S.; Silva, B.P.D.; Correia, T.M.L.; Silva, R.P.D.; Meireles, D.A.; Pereira, R.; Netto, L.E.S.; Meotti, F.C.; Queiroz, R.F.
Peroxiredoxin AhpC1 protects Pseudomonas aeruginosa against the inflammatory oxidative burst and confers virulence
Redox Biol.
46
102075
2021
Pseudomonas aeruginosa (A0A072ZH89), Pseudomonas aeruginosa, Pseudomonas aeruginosa UCBPP-PA14 (A0A072ZH89)
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