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Literature summary for 5.3.4.1 extracted from

  • Tian, G.; Xiang, S.; Noiva, R.; Lennarz, W.J.; Schindelin, H.
    The crystal structure of yeast protein disulfide isomerase suggests cooperativity between its active sites (2006), Cell, 124, 61-73.
    View publication on PubMed
Search for more literature for 5.3.4.1

Cloned(Commentary)

Cloned (Comment) Organism
expression of residues 23-522 of PDI1 Saccharomyces cerevisiae

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant residues 23-522 of PDI1, X-ray diffraction structure determination and analysis at 2.4 A resolution, modeling Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
C409A site-directed mutagenesis, mutation of the second cysteine of the active site, the mutant shows similar activity to the wild-type enzyme Saccharomyces cerevisiae
C64A site-directed mutagenesis, mutation of the second cysteine of the active site, the mutant shows similar activity to the wild-type enzyme Saccharomyces cerevisiae
additional information a domain a'-deletion mutant shows reduced activity in refolding of RNase compared to the wild-type enzyme Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Saccharomyces cerevisiae PDI plays a key role in catalyzing the folding of secretory proteins ?
-
 ?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Reaction

Reaction Comment Organism Reaction ID
catalyses the rearrangement of -S-S- bonds in proteins active site location, structure, and redox state Saccharomyces cerevisiae
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information PDI plays a key role in catalyzing the folding of secretory proteins Saccharomyces cerevisiae ?
-
 ?
additional information all 5 domains of PDI are required for full catalytic activity Saccharomyces cerevisiae ?
-
 ?
RNase refolding of RNase, renaturation of reduced and of scrambled RNase with almost equal activity Saccharomyces cerevisiae ?
-
 ?

Subunits

Subunits Comment Organism
More domain arrangement: two catalytically inactive thioredoxin domains inserted between two catalytically active thioredoxin domains and an acidic C-terminal tail, the four thioredoxin domains form the shape of a twisted U with the active sites facing each other across the long sides, the inside surface is enriched in hydrophobic residues facilitating interactions with misfolded proteins, all 5 domains of PDI are required for full catalytic activity Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
PDI
-
 Saccharomyces cerevisiae
protein disulfide isomerase
-
 Saccharomyces cerevisiae