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Literature summary extracted from

  • Wadahama, H.; Kamauchi, S.; Ishimoto, M.; Kawada, T.; Urade, R.
    Protein disulfide isomerase family proteins involved in soybean protein biogenesis (2007), FEBS J., 274, 687-703.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
5.3.4.1 additional information PDIS-1, but not PDIS-2, is induced under endoplasmic reticulum-stress conditions Glycine max

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.3.4.1 genes PDIS-1 and PDIS-2, DNA and amino acid sequence determination and anaylsis, expression in Escherichia coli as soluble folded proteins Glycine max

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
5.3.4.1 endoplasmic reticulum PDIS-1 and PDIS-2 lack the C-terminal, endoplasmic reticulum-retrieval signal, KDEL Glycine max 5783
-
5.3.4.1 additional information PDIS-1 and PDIS-2 both possess a putative N-terminal secretory signal sequence and two tandem thioredoxin-like motifs, with a CGHC active site Glycine max
-
-
5.3.4.1 vacuole protein storage vacuoles Glycine max 5773
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5.3.4.1 additional information Glycine max the enzyme plays important roles in the folding of nascent polypeptides and the formation of disulfide bonds in the endoplasmic reticulum, PDIS-1 associates with proglycinin, a precursor of the seed storage protein glycinin, in the cotyledon, seed-dependent aggregation of amyloid beta-peptide (1-40) monomers is inhibited by both PDIS-1 and PDIS-2, both are involved in seed development, overview ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
5.3.4.1 Glycine max
-
 cv. Jack, genes PDIS-1 and PDIS-2
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
5.3.4.1 cotyledon distribution to the endoplasmic reticulum and protein storage vacuoles, PDIS-1 levels, but not PDIS-2 levels, are increased in cotyledons Glycine max
-
5.3.4.1 flower
-
 Glycine max
-
5.3.4.1 leaf trifoliolate leaves Glycine max
-
5.3.4.1 root
-
 Glycine max
-
5.3.4.1 seed changes in the levels of PDIS-1 and PDIS-2 during seed development, overview Glycine max
-
5.3.4.1 stem
-
 Glycine max
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.3.4.1 additional information the enzyme plays important roles in the folding of nascent polypeptides and the formation of disulfide bonds in the endoplasmic reticulum, PDIS-1 associates with proglycinin, a precursor of the seed storage protein glycinin, in the cotyledon, seed-dependent aggregation of amyloid beta-peptide (1-40) monomers is inhibited by both PDIS-1 and PDIS-2, both are involved in seed development, overview Glycine max ?
-
 ?
5.3.4.1 additional information PDIS-1 and PDIS-2 show both an oxidative refolding activity of denatured ribonuclease A and a chaperone activity, PDIS-1 and PDIS-2 both possess a putative N-terminal secretory signal sequence and two tandem thioredoxin-like motifs, with a CGHC active site Glycine max ?
-
 ?

Subunits

EC Number Subunits Comment Organism
5.3.4.1 More the enzyme structure contains two thioredoxin-like domains, a and a', and an ERp29c domain, determination by peptide mapping with either trypsin or V8 protease, domain structures, overview Glycine max

Synonyms

EC Number Synonyms Comment Organism
5.3.4.1 PDI
-
 Glycine max
5.3.4.1 protein disulfide isomerase
-
 Glycine max