Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 5.3.4.1 extracted from

  • Ruoppolo, M.; Orru, S.; Talamo, F.; Ljung, J.; Pirneskoski, A.; Kivirikko, K.I.; Marino, G.; Koivunen, P.
    Mutations in domain a' of protein disulfide isomerase affect the folding pathway of bovine pancreatic ribonuclease A (2003), Protein Sci., 12, 939-952.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 5.3.4.1

Protein Variants

Protein Variants Comment Organism
F449R mutation in the last alpha helix of domain a', 7.5-8fold reduced appearance rate of folding product RNase A Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
endoplasmic reticulum
-
 Ovis aries 5783
-

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-
Ovis aries
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
unfolded RNase A reduced and denatured bovine pancreatic RNase A, glutathione redox buffer, PDI catalyzes the entire RNase A folding by enhancing the formation and reduction of mixed disulfides with glutathione and the formation of intramolecular disulfides Homo sapiens refolded RNase A
-
 ?
unfolded RNase A tyrosine and tryptophane residues in peptides are the recognition motifs for their binding Ovis aries refolded RNase A
-
 ?

Subunits

Subunits Comment Organism
More PDI consist of 2 catalytically active domains, a and a', and two inactive ones b and b', all four domains have a thioredoxin fold, domain b' contains he primary peptide binding site Homo sapiens

Synonyms

Synonyms Comment Organism
PDI
-
 Homo sapiens
PDIp
-
 Ovis aries