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Literature summary for 3.4.22.68 extracted from

  • Eckhoff, J.; Dohmen, R.J.
    In vitro studies reveal a sequential mode of chain processing by the yeast SUMO-specific protease Ulp2 (2015), J. Biol. Chem., 19, 12268-12281.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.22.68

Cloned(Commentary)

Cloned (Comment) Organism
isozyme Ulp1, expression of recombinant FLAG-tagged and maltosse-binding protein-fused isozyme Ulp1, containing a TEV protease recognition site, in Escherichia coli strain BL21, recombinant expression of GST-tagged isozyme Ulp1 Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
additional information immobilization of isozyme Ulp1 via its C-terminal FLAG tag Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae Q02724
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-

Purification (Commentary)

Purification (Comment) Organism
recombinant FLAG-tagged and maltose-binding protein-fused isozyme Ulp1, containing a TEV protease recognition site, from Escherichia coli strain BL21 by affinity chromatography Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information Ulp1 liberates poly-Smt3 from a substrate chain. In vitro, Ulp1 is highly active even in very low concentrations. Substrate specificity analysis of immobilized recombinant enzyme, overview Saccharomyces cerevisiae ?
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 ?

Synonyms

Synonyms Comment Organism
SUMO(Smt3)-specific protease
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 Saccharomyces cerevisiae
SUMO-specific protease
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 Saccharomyces cerevisiae
Ulp1
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 Saccharomyces cerevisiae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Saccharomyces cerevisiae