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.
No PubMed abstract available
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 |
- |
- |
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 |
- |
recombinant protein, using the Pichia pastoris expression system |
- |
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 |
- |
Saccharomyces cerevisiae |