3.4.22.10: streptopain

This is an abbreviated version!
For detailed information about streptopain, go to the full flat file.

Word Map on EC 3.4.22.10

Reaction

preferential cleavage with hydrophobic residues at P2, P1 and P1' =

Synonyms

More, Streptococcus peptidase A, Streptococcus protease, EC 3.4.4.18, Streptococcal cysteine proteinase, Steptococcus proteinase, proteinase, streptococcal, SCP, Spe B, streptococcal erythrogenic toxin B, streptococcal pyrogenic exotoxin B, SPP, SpeB, streptococcal proteinase, interleukin-1beta convertase, pyrogenic exotoxin B, streptococcal pyrogenic exotoxin B/cysteine protease, SPE B/SCP, SPE B protease, streptococcal cysteine protease, IdeS, IgG-degrading enzyme of Streptococcus pyogenes, SpcCEP, streptococcal pyogenic exotoxin B, streptopain

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.22 Cysteine endopeptidases
                3.4.22.10 streptopain

Purification

Purification on EC 3.4.22.10 - streptopain

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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
a combination of two successive strong cation exchange resins gives the best results for soluble, pure enzyme with the highest activity
HiTrap SP column chromatography, and G75 Sephadex gel filtration
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native mature Spe B by ammonium sulfate fractionation, dialysis, and ion exchange chromatography, recombinant His-tagged Spe B propeptide and SpeB mutant C47S from Escherichia coli
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Ni2+-chelating column chromatography
recombinant His-tagged wild-type and mutant C192S enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, the wild-type enzyme autoprocesses during purification to the mature 28 kDa protein
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recombinant pro-sequence domain and refolded mature enzyme from Escherichia coli by affinity chromatography
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recombinant wild-type and inactive mutant enzyme from Escherichia coli by affinity chromatography
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the proteins are purified by Ni2+-chelating chromatography with a gradient of 20-200 mM imidazole. The proteins are concentrated by ultrafiltration using a 10 kDa cutoff membrane and then exchanged with phosphate-buffered saline
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using Ni-NTA chromatography
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