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Literature summary for 5.3.4.1 extracted from

  • Kimura, T.; Hosoda, Y.; Kitamura, Y.; Nakamura, H.; Horibe, T.; Kikuchi, M.
    Functional differences between human and yeast protein disulfide isomerase family proteins (2004), Biochem. Biophys. Res. Commun., 320, 359-365.
    View publication on PubMed
Search for more literature for 5.3.4.1

Cloned(Commentary)

Cloned (Comment) Organism
expression of His-tagged enzyme in Escherichia coli strain AD494(DE3) Homo sapiens
expression of His-tagged enzyme in Escherichia coli strain AD494(DE3) Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
additional information chromosomal insertion of the human PDI gene into the Saccharomyces cerevisiae PDI1 disruption mutant strain cannot rescue the mutant, the human enzyme is functionally not equivalent to the yeast enzyme, tetrad analysis, overview Homo sapiens
additional information the PDI1 disruption mutant strain cannot be rescued by chromosomal insertion of the human PDI gene, the human enzyme is not functionally equivalent to the yeast enzyme, tetrad analysis, overview Saccharomyces cerevisiae

Localization

Localization Comment Organism GeneOntology No. Textmining
endoplasmic reticulum lumen Homo sapiens 5783
-
endoplasmic reticulum lumen Saccharomyces cerevisiae 5783
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Saccharomyces cerevisiae the organism is completely dependent on PDI activity for growth ?
-
 ?
additional information Saccharomyces cerevisiae trg1/TRG1 the organism is completely dependent on PDI activity for growth ?
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-
Saccharomyces cerevisiae
-
-
-
Saccharomyces cerevisiae trg1/TRG1
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein the enzyme has 5 N-glycosylation sites all modified in vivo Saccharomyces cerevisiae
no glycoprotein
-
 Homo sapiens

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli strain AD494(DE3) by nickel affinity chromatography Homo sapiens
recombinant His-tagged enzyme from Escherichia coli strain AD494(DE3) by nickel affinity chromatography Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the organism is completely dependent on PDI activity for growth Saccharomyces cerevisiae ?
-
 ?
additional information isomerase activity is assayed using the insulin/glutathione coupled assay Homo sapiens ?
-
 ?
additional information the yPDI enzyme family members Mpd1p, Mpd2p, and Eug1p show high chaperone activity, but low isomerase activity compared to PDI, isomerase activity is assayed using the insulin/glutathione coupled assay, chaperone activity is also measured utilizing mastoparan as substrate Saccharomyces cerevisiae ?
-
 ?
additional information the organism is completely dependent on PDI activity for growth Saccharomyces cerevisiae trg1/TRG1 ?
-
 ?
additional information the yPDI enzyme family members Mpd1p, Mpd2p, and Eug1p show high chaperone activity, but low isomerase activity compared to PDI, isomerase activity is assayed using the insulin/glutathione coupled assay, chaperone activity is also measured utilizing mastoparan as substrate Saccharomyces cerevisiae trg1/TRG1 ?
-
 ?
rhodanese chaperone activity Homo sapiens ?
-
 ?
rhodanese prevention of rhodanese degeneration, chaperone activity Saccharomyces cerevisiae ?
-
 ?
rhodanese prevention of rhodanese degeneration, chaperone activity Saccharomyces cerevisiae trg1/TRG1 ?
-
 ?

Synonyms

Synonyms Comment Organism
More the enzyme belongs to the yeast hPDI enzyme family Homo sapiens
More the enzymes yPDI, Mpd1p, Mpd2p, and Eug1p belong to the yeast yPDI enzyme family Saccharomyces cerevisiae
PDI
-
 Homo sapiens
PDI
-
 Saccharomyces cerevisiae
protein disulfide isomerase
-
 Homo sapiens
protein disulfide isomerase
-
 Saccharomyces cerevisiae