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Literature summary for 3.5.1.1 extracted from

  • Ferrara, M.; Severino, N.; Valente, R.; Perales, J.; Bon, E.
    High-yield extraction of periplasmic asparaginase produced by recombinant Pichia pastoris harbouring the Saccharomyces cerevisiae ASP3 gene (2010), Enzyme Microb. Technol., 47, 71-76.
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Cloned(Commentary)

Cloned (Comment) Organism
expressed in Pichia pastoris, haboring the ASP3 gene of asparaginase from Saccharomyces cervisiae Saccharomyces cerevisiae

Localization

Localization Comment Organism GeneOntology No. Textmining
periplasm high-yield extraction of the periplasmic asparaginase produced by the recombinant Pichia pastoris strain habouring the Saccharomyes cerevisiae ASP3 gene. The use of six freeze-thaw cycles, folllowed by extraction with 20 mM potassium phosphate buffer pH 7.0 for 20 h, resulted in 85% enzyme recovery whereas the alkaline extraction using 500 mM potassium phosphate at pH 11.5 in the presence of 10 mM cysteine allows 100% enzyme recovery Saccharomyces cerevisiae
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Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
45000
-
 x * 45000, SDS-PAGE, recombinant protein Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
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 recombinant protein, using the Pichia pastoris expression system
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Storage Stability

Storage Stability Organism
the crude asparaginase preparations are stable upon storage at -18°C for several months Saccharomyces cerevisiae

Subunits

Subunits Comment Organism
? x * 45000, SDS-PAGE, recombinant protein Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
asparaginase II
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 Saccharomyces cerevisiae