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Literature summary for 1.11.1.24 extracted from

  • Bhattacharyya, S.; Dutta, D.; Ghosh, A.K.; Das, A.K.
    Cloning, overexpression, purification, crystallization and preliminary X-ray diffraction analysis of an atypical two-cysteine peroxiredoxin (SAOUHSC_01822) from Staphylococcus aureus NCTC 8325 (2009), Acta Crystallogr. Sect. F, 65, 1113-1115.
    View publication on PubMedView publication on EuropePMC
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Cloned(Commentary)

Cloned (Comment) Organism
expression of His-tagged enzyme in Escherichia coli Staphylococcus aureus

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant enzyme, hanging drop vapour diffusion method, 0.002 ml of 60 mg/ml protein in 10 mM Tris-HCl, pH 8.0, 50 mM NaCl, 2 mM DTT, are mixed with 0.002 ml of 2 M ammonium sulfate, 0.1 M Na HEPES, pH 7.0, 2% v/v PEG 400, 25°C, 2 days, X-ray diffraction structur determination and analysis at 2.3 A resolution Staphylococcus aureus

Organism

Organism UniProt Comment Textmining
Staphylococcus aureus Q2FXL3
-
-
Staphylococcus aureus NCTC 8325 Q2FXL3
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli by nickle affinity chromatography and gel filtration Staphylococcus aureus

Synonyms

Synonyms Comment Organism
atypical two-cysteine peroxidase
-
 Staphylococcus aureus
SAOUHSC_01822
-
 Staphylococcus aureus

General Information

General Information Comment Organism
physiological function the enzyme plays a major role in the reponse of the bacterium to oxidative stress Staphylococcus aureus