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Literature summary for 2.7.3.3 extracted from

  • Zhang, X.C.; Wang, W.D.; Wang, J.S.; Pan, J.C.
    PPIase independent chaperone-like function of recombinant human cyclophilin A during arginine kinase refolding (2013), FEBS Lett., 587, 666-672.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of His-tagged enzyme in Escherichia coli strain Rossta Penaeus chinensis

Organism

Organism UniProt Comment Textmining
Penaeus chinensis
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-
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Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli strain Rossetta by nickel affinity chromatography Penaeus chinensis

Renatured (Commentary)

Renatured (Comment) Organism
reactivation of denatured enzyme AK: human cyclophilin A (CyPA) has a peptidyl-prolyl cis-trans isomerase (PPIase)-independent chaperone-like activity during enzyme AK folding. Recombinant rhCyPA can form dimers and trimers during the purification procedure, catalytically inactive recombinant cyclophilin A mutant variant Q63A has even more efficiency to suppress aggregation and improve reactivation yields of enzyme AK than the wild-type cyclophilin A, overview. Catalytically inactive cyclophilin A mutants R55A, F60A, and H126A can also act as chaperones in arginine kinase folding. The refolding is initiated by a 50fold dilution in 20 mM Tris-HCl buffer, pH 7.8, containing 10 mM 2-mercaptoethanol, in the presence or absence of 0.006 mM of the wild-type rhCyPA or its variants at 20°C Penaeus chinensis

Source Tissue

Source Tissue Comment Organism Textmining
muscle
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Penaeus chinensis
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