Disease relevance of ECs0644

• The ahpC mutant was sensitive to the more hydrophilic solvents xylene and toluene, suggesting that there are additional mechanisms of solvent toxicity [1].
• E. coli Tpx (EcTpx) shows substrate specificity toward alkyl hydroperoxides over H2O2 and is the most potent reductant of alkyl hydroperoxides surpassing AhpC and BCP, the other E. coli Prx members [2].
• Cloning, overexpression, and characterization of peroxiredoxin and NADH peroxiredoxin reductase from Thermus aquaticus [3].
• Anti-oxidative stress system in cyanobacteria. Significance of type II peroxiredoxin and the role of 1-Cys peroxiredoxin in Synechocystis sp. strain PCC 6803 [4].
• In contrast, the obligate anaerobe Clostridium pasteurianum codes for a two-component reducing system upstream of the ahpC homologue [5].

High impact information on ECs0644

• Conversion of a peroxiredoxin into a disulfide reductase by a triplet repeat expansion [6].
• The ahpC mutant was found to have an activity that was three times that of the wild type in reducing tetralin hydroperoxide to 1,2,3,4-tetrahydro-1-naphthol [1].
• Mutants resistant to a mixture of xylene and tetralin were isolated from the ahpC mutant but not from the wild-type strain [1].
• The mutation was localized to a substitution of valine for glycine at position 142 in the coding region of ahpC, which is the gene encoding the catalytic subunit of the enzyme [1].
• Based on sequence homology analysis SLL1621 and SLR1198 are categorized into type II peroxiredoxin and 1-Cys type peroxiredoxin, respectively [4].

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].

References