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Gene Review

npr  -  NADH peroxidase

Enterococcus faecalis V583

 
 
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Disease relevance of npr

  • Using the E. coli phage T7 expression system the npr gene has now been overexpressed in an E. coli genetic background [1].
  • Evidence for regulation of the NADH peroxidase gene (npr) from Enterococcus faecalis by OxyR [2].
  • A 34 kDa protein has been identified in crude extracts of E. faecalis that cross-reacts with polyclonal antisera to purified OxyR from E. coli and a protein(s) present in these extracts retards npr DNA fragments in gel shift assays [2].
  • More recently, however, functional Cys-SOH residues have been identified in the native oxidized forms of the FAD-containing NADH peroxidase and NADH oxidase from Streptococcus faecalis; these two proteins constitute a new class within the flavoprotein disulfide reductase family [3].
 

High impact information on npr

 

Chemical compound and disease context of npr

 

Biological context of npr

  • The NPXase gene (npr) comprises 1341 base-pairs and is preceded by a typical ribosome binding site [1].
  • Integration into the chromosome via homologous recombination was monitored using the npr gene of E. faecalis JH2-2 as a target [14].
  • Integration of this construction into the JH2-2 npr gene was selected by shift temperature, from 30 degrees C to 42 degrees C. 85% of the analysed clones showed integration into the npr gene, demonstrating the practicality of this thermosensitive replicon as a genetic integrative tool for E. faecalis [14].
  • DNA fragments encoding streptococcal NADH peroxidase (NPXase) have been amplified, cloned and sequenced from the genome of Streptococcus (Enterococcus) faecalis 10C1 (ATCC 11700) [1].
 

Associations of npr with chemical compounds

  • The non-flavin redox center of the streptococcal NADH peroxidase. I. Thiol reactivity and redox behavior in the presence of urea [15].
  • The residual quinone reductase activity of NADH peroxidase which has undergone oxidative inactivation of the active site Cys42 indicates that this residue is not involved in the reduction of the quinones [11].
  • The role of the active site cysteine 42 in NADH peroxidase has been elucidated using biochemical and crystallographic techniques [12].
  • One-electron reduction of benzoquinone accounts for about 50% of the total electron transfer catalyzed by NADH peroxidase at pH 7, with the remainder of the reduction being catalyzed by a two-electron (hydride) transfer [11].
  • While the function of participating pterin and the roles of Nox, Npx, CynD, and CA in the CNO-catalyzed scavenging of CN remain to be determined, this is the first report describing the collective involvement of these four enzymes in the metabolic detoxification and utilization of CN as a bacterial nitrogenous growth substrate [16].
 

Analytical, diagnostic and therapeutic context of npr

References

  1. Cloning, sequence and overexpression of NADH peroxidase from Streptococcus faecalis 10C1. Structural relationship with the flavoprotein disulfide reductases. Ross, R.P., Claiborne, A. J. Mol. Biol. (1991) [Pubmed]
  2. Evidence for regulation of the NADH peroxidase gene (npr) from Enterococcus faecalis by OxyR. Ross, R.P., Claiborne, A. FEMS Microbiol. Lett. (1997) [Pubmed]
  3. Protein-sulfenic acid stabilization and function in enzyme catalysis and gene regulation. Claiborne, A., Miller, H., Parsonage, D., Ross, R.P. FASEB J. (1993) [Pubmed]
  4. Flavin-linked peroxide reductases: protein-sulfenic acids and the oxidative stress response. Claiborne, A., Ross, R.P., Parsonage, D. Trends Biochem. Sci. (1992) [Pubmed]
  5. Purification and analysis of streptococcal NADH peroxidase expressed in Escherichia coli. Parsonage, D., Miller, H., Ross, R.P., Claiborne, A. J. Biol. Chem. (1993) [Pubmed]
  6. Active-site structural comparison of streptococcal NADH peroxidase and NADH oxidase. Reconstitution with artificial flavins. Ahmed, S.A., Claiborne, A. J. Biol. Chem. (1992) [Pubmed]
  7. The non-flavin redox center of the streptococcal NADH peroxidase. II. Evidence for a stabilized cysteine-sulfenic acid. Poole, L.B., Claiborne, A. J. Biol. Chem. (1989) [Pubmed]
  8. Crystallization and preliminary x-ray diffraction study of the flavoprotein NADH peroxidase from Streptococcus faecalis 10C1. Schiering, N., Stoll, V.S., Blanchard, J.S., Pai, E.F. J. Biol. Chem. (1989) [Pubmed]
  9. Interactions of pyridine nucleotides with redox forms of the flavin-containing NADH peroxidase from Streptococcus faecalis. Poole, L.B., Claiborne, A. J. Biol. Chem. (1986) [Pubmed]
  10. Staphylococcus aureus coenzyme A disulfide reductase, a new subfamily of pyridine nucleotide-disulfide oxidoreductase. Sequence, expression, and analysis of cdr. delCardayre, S.B., Davies, J.E. J. Biol. Chem. (1998) [Pubmed]
  11. Quinone reductase reaction catalyzed by Streptococcus faecalis NADH peroxidase. Marcinkeviciene, J.A., Blanchard, J.S. Biochemistry (1995) [Pubmed]
  12. Crystallographic analyses of NADH peroxidase Cys42Ala and Cys42Ser mutants: active site structures, mechanistic implications, and an unusual environment of Arg 303. Mande, S.S., Parsonage, D., Claiborne, A., Hol, W.G. Biochemistry (1995) [Pubmed]
  13. Kinetic mechanism and nucleotide specificity of NADH peroxidase. Stoll, V.S., Blanchard, J.S. Arch. Biochem. Biophys. (1988) [Pubmed]
  14. A new theta-type thermosensitive replicon from Lactococcus lactis as an integration vector for Enterococcus faecalis. Frère, J., Benachour, A., Giard, J.C., Laplace, J.M., Flahaut, S., Auffray, Y. FEMS Microbiol. Lett. (1998) [Pubmed]
  15. The non-flavin redox center of the streptococcal NADH peroxidase. I. Thiol reactivity and redox behavior in the presence of urea. Poole, L.B., Claiborne, A. J. Biol. Chem. (1989) [Pubmed]
  16. Bacterial cyanide oxygenase is a suite of enzymes catalyzing the scavenging and adventitious utilization of cyanide as a nitrogenous growth substrate. Fernandez, R.F., Kunz, D.A. J. Bacteriol. (2005) [Pubmed]
  17. Molecular cloning and analysis of the gene encoding the NADH oxidase from Streptococcus faecalis 10C1. Comparison with NADH peroxidase and the flavoprotein disulfide reductases. Ross, R.P., Claiborne, A. J. Mol. Biol. (1992) [Pubmed]
  18. Evidence for a single active-site cysteinyl residue in the streptococcal NADH peroxidase. Poole, L.B., Claiborne, A. Biochem. Biophys. Res. Commun. (1988) [Pubmed]
 
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