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Literature summary extracted from

  • Rouhier, N.; Jacquot, J.P.
    Molecular and catalytic properties of a peroxiredoxin-glutaredoxin hybrid from Neisseria meningitidis (2003), FEBS Lett., 554, 149-153.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.11.1.27 1. full-length protein with 345 amino acids, 2. a construction which stretches from the N-terminus to the end of the peroxiredoxin domain, contains 165 amino acids, 3. the grx module, that starts with MAQESVA and ends with the C-terminus of the fusion with 77 amino acids overall, expression in Escherichia coli Neisseria meningitidis

Protein Variants

EC Number Protein Variants Comment Organism
1.11.1.27 C185S inactive mutant enzyme Neisseria meningitidis

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.11.1.27 soluble when expressed in Escherichia coli Neisseria meningitidis
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Organism

EC Number Organism UniProt Comment Textmining
1.11.1.27 Neisseria meningitidis
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 natural hybrid protein which contains both a peroxiredoxin and a glutaredoxin domain
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Purification (Commentary)

EC Number Purification (Comment) Organism
1.11.1.27
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 Neisseria meningitidis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.11.1.27 H2O2 + NADPH reaction is driven by glutathione which is maintained reduced via NADPH and glutathione reductase. Both the peroxiredoxin and glutaredoxin domains are biochemically active in the natural hybrid protein which contains both a peroxiredoxin and a glutaredoxin domain. When expressed separately, the glutaredoxin domain is catalytically active and the peroxiredoxin domain posseses a weak activity when supplemented with expoenous glutaredoxin Neisseria meningitidis H2O + NADP+
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