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Gene Review

ECs0644  -  alkyl hydroperoxide reductase

Escherichia coli O157:H7 str. Sakai

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Disease relevance of ECs0644


High impact information on ECs0644


Chemical compound and disease context of ECs0644

  • Mycobacterium tuberculosis alkylhydroperoxidase C (AhpC) belongs to the peroxiredoxin family, but unusually contains three cysteine residues in its active site [7].
  • His-tagged tryparedoxin II expressed in E. coli exhibited ping-pong kinetics in the trypanothione:peroxiredoxin assay with kinetic parameters (KM peroxiredoxin = 4.2 microM, KM trypanothione = 33 microM, Vmax/[E] = 952 min(-1)) similar to those reported for tryparedoxin I [Gommel et al. (1997) Eur. J. Biochem. 248, 913-918] [8].

Biological context of ECs0644

  • The amino acid sequences show that Prx is related to two-cysteine peroxiredoxins from a range of organisms and that PrxR resembles NADH-dependent flavoenzymes that catalyze the reduction of peroxiredoxins in mesophilic bacteria [3].
  • Tpx contains three Cys residues, Cys(95), Cys(82), and Cys(61), and the latter residue aligns with the N-terminal active site Cys of other peroxidases in the peroxiredoxin family [9].
  • The garB gene is immediately preceded by an open reading frame encoding a novel 27.5-kDa chimeric enzyme composed of one N-terminal peroxiredoxin-like domain followed by a glutaredoxin-like C terminus [10].
  • A sequence coding for a peroxiredoxin (Prx) was isolated from a xylem/phloem cDNA library from Populus trichocarpa and subsequently inserted into an expression plasmid yielding the construction pET-Prx [11].
  • Many eubacterial genomes including those of Salmonella typhimurium, Streptococcus mutans, and Thermus aquaticus encode a dedicated flavoprotein reductase (AhpF, Nox1, or PrxR) just downstream of the structural gene for their peroxiredoxin (Prx, AhpC) homologue to reduce the latter protein during turnover [5].

Associations of ECs0644 with chemical compounds

  • All of the Ohr homologues possess two cysteine residues, one of them located in a VCP motif, which is also present in all of the proteins from the peroxiredoxin family [12].
  • Prx appears to be inactivated by cumene hydroperoxide [3].
  • Divergent light-, ascorbate-, and oxidative stress-dependent regulation of expression of the peroxiredoxin gene family in Arabidopsis [13].
  • (1)H, (13)C and (15)N NMR assignment of the homodimeric poplar phloem type II peroxiredoxin [14].
  • Hydrogen peroxide-forming NADH oxidase belonging to the peroxiredoxin oxidoreductase family: existence and physiological role in bacteria [15].

Analytical, diagnostic and therapeutic context of ECs0644

  • Southern blot analysis of the three strains probed with the A. xylanus peroxiredoxin reductase gene revealed single strong bands, which are presumably derived from the individual peroxiredoxin reductase genes [15].
  • Crystallization and preliminary X-ray data of a bifunctional peroxiredoxin from poplar [16].
  • In contrast to 2Cys-Prx, which is predominantly expressed in leaf tissue of cabbage seedlings, CPrxII is highly expressed in root tissue as revealed by Northern and Western blot analyses [17].
  • Confocal laser scanning microscopy, using polyclonal antibody against the recombinant E. moshkovskii peroxiredoxin, demonstrated that this protein was localized in the nucleus and cytoplasm of trophozoites, supporting its function as a protectant against DNA damage [18].
  • Southern blot and real-time reverse transcription PCR analyses of the E. moshkovskii peroxiredoxin gene demonstrated that it was a multi-copy gene and its expression was comparable to that of E. histolytica [18].


  1. Cloning of an organic solvent-resistance gene in Escherichia coli: the unexpected role of alkylhydroperoxide reductase. Ferrante, A.A., Augliera, J., Lewis, K., Klibanov, A.M. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  2. Crystal structure of Escherichia coli thiol peroxidase in the oxidized state: insights into intramolecular disulfide formation and substrate binding in atypical 2-Cys peroxiredoxins. Choi, J., Choi, S., Choi, J., Cha, M.K., Kim, I.H., Shin, W. J. Biol. Chem. (2003) [Pubmed]
  3. Cloning, overexpression, and characterization of peroxiredoxin and NADH peroxiredoxin reductase from Thermus aquaticus. Logan, C., Mayhew, S.G. J. Biol. Chem. (2000) [Pubmed]
  4. Anti-oxidative stress system in cyanobacteria. Significance of type II peroxiredoxin and the role of 1-Cys peroxiredoxin in Synechocystis sp. strain PCC 6803. Hosoya-Matsuda, N., Motohashi, K., Yoshimura, H., Nozaki, A., Inoue, K., Ohmori, M., Hisabori, T. J. Biol. Chem. (2005) [Pubmed]
  5. An NADH-dependent bacterial thioredoxin reductase-like protein in conjunction with a glutaredoxin homologue form a unique peroxiredoxin (AhpC) reducing system in Clostridium pasteurianum. Reynolds, C.M., Meyer, J., Poole, L.B. Biochemistry (2002) [Pubmed]
  6. Conversion of a peroxiredoxin into a disulfide reductase by a triplet repeat expansion. Ritz, D., Lim, J., Reynolds, C.M., Poole, L.B., Beckwith, J. Science (2001) [Pubmed]
  7. Site-directed mutagenesis reveals a novel catalytic mechanism of Mycobacterium tuberculosis alkylhydroperoxidase C. Chauhan, R., Mande, S.C. Biochem. J. (2002) [Pubmed]
  8. Sequence, heterologous expression and functional characterization of a novel tryparedoxin from Crithidia fasciculata. Montemartini, M., Kalisz, H.M., Kiess, M., Nogoceke, E., Singh, M., Steinert, P., Flohé, L. Biol. Chem. (1998) [Pubmed]
  9. Catalytic mechanism of thiol peroxidase from Escherichia coli. Sulfenic acid formation and overoxidation of essential CYS61. Baker, L.M., Poole, L.B. J. Biol. Chem. (2003) [Pubmed]
  10. Characterization of clutathione amide reductase from Chromatium gracile. Identification of a novel thiol peroxidase (Prx/Grx) fueled by glutathione amide redox cycling. Vergauwen, B., Pauwels, F., Jacquemotte, F., Meyer, T.E., Cusanovich, M.A., Bartsch, R.G., Van Beeumen, J.J. J. Biol. Chem. (2001) [Pubmed]
  11. Isolation and characterization of a new peroxiredoxin from poplar sieve tubes that uses either glutaredoxin or thioredoxin as a proton donor. Rouhier, N., Gelhaye, E., Sautiere, P.E., Brun, A., Laurent, P., Tagu, D., Gerard, J., de Faÿ, E., Meyer, Y., Jacquot, J.P. Plant Physiol. (2001) [Pubmed]
  12. Organic hydroperoxide resistance gene encodes a thiol-dependent peroxidase. Cussiol, J.R., Alves, S.V., de Oliveira, M.A., Netto, L.E. J. Biol. Chem. (2003) [Pubmed]
  13. Divergent light-, ascorbate-, and oxidative stress-dependent regulation of expression of the peroxiredoxin gene family in Arabidopsis. Horling, F., Lamkemeyer, P., König, J., Finkemeier, I., Kandlbinder, A., Baier, M., Dietz, K.J. Plant Physiol. (2003) [Pubmed]
  14. (1)H, (13)C and (15)N NMR assignment of the homodimeric poplar phloem type II peroxiredoxin. Bouillac, S., Rouhier, N., Tsan, P., Jacquot, J.P., Lancelin, J.M. J. Biomol. NMR (2004) [Pubmed]
  15. Hydrogen peroxide-forming NADH oxidase belonging to the peroxiredoxin oxidoreductase family: existence and physiological role in bacteria. Nishiyama, Y., Massey, V., Takeda, K., Kawasaki, S., Sato, J., Watanabe, T., Niimura, Y. J. Bacteriol. (2001) [Pubmed]
  16. Crystallization and preliminary X-ray data of a bifunctional peroxiredoxin from poplar. Echalier, A., Corbier, C., Rouhier, N., Jacquot, J.P., Aubry, A. Acta Crystallogr. D Biol. Crystallogr. (2002) [Pubmed]
  17. Cloning and expression of a new isotype of the peroxiredoxin gene of Chinese cabbage and its comparison to 2Cys-peroxiredoxin isolated from the same plant. Choi, Y.O., Cheong, N.E., Lee, K.O., Jung, B.G., Hong, C.H., Jeong, J.H., Chi, Y.H., Kim, K., Cho, M.J., Lee, S.Y. Biochem. Biophys. Res. Commun. (1999) [Pubmed]
  18. Molecular characterization of peroxiredoxin from Entamoeba moshkovskii and a comparison with Entamoeba histolytica. Cheng, X.J., Yoshihara, E., Takeuchi, T., Tachibana, H. Mol. Biochem. Parasitol. (2004) [Pubmed]
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