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Literature summary for 5.3.4.1 extracted from

  • Wang, L.; Shimizu, Y.; Mizunaga, T.; Matsumoto, S.; Otsuka, Y.
    Expression, purification and characterization of yeast protein disulfide isomerase produced by a recombinant baculovirus-mediated silkworm, Bombyx mori, pupae expression system (2008), Biotechnol. Lett., 30, 625-630.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Bombyx mori pupae Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
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Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein expression in Bombyx mori results in production of mostly non-N-glycosylated and some N-glycosylated recombinant protein Saccharomyces cerevisiae

Purification (Commentary)

Purification (Comment) Organism
recombinant protein Saccharomyces cerevisiae

Source Tissue

Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information protein disulfide isomerase has a concentration-dependent chaperone-activity and inhibits the aggregation of rhodanese, which has no disulfide bonds Saccharomyces cerevisiae ?
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