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Literature summary extracted from

  • Pandhare, J.; Deshpande, V.
    Both chaperone and isomerase functions of protein disulfide isomerase are essential for acceleration of the oxidative refolding and reactivation of dimeric alkaline protease inhibitor (2004), Protein Sci., 13, 2493-2501.
    View publication on PubMedView publication on EuropePMC

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
5.3.4.1 endoplasmic reticulum lumen Streptomyces sp. 5783
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
5.3.4.1 55000
-
 x * 55000 Streptomyces sp.

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5.3.4.1 alkaline protease inhibitor Streptomyces sp. folding and rearrangement of alkaline protease inhibitor ?
-
 ?
5.3.4.1 alkaline protease inhibitor Streptomyces sp. NCIM 5127 folding and rearrangement of alkaline protease inhibitor ?
-
 ?
5.3.4.1 additional information Streptomyces sp. both chaperone and isomerase functions of PDI are essential for acceleration of the oxidative refolding and reactivation of dimeric alkaline protease inhibitor API, PDI acts as isomerase/chaperone for a few monomeric proteins assisting in disulfide bond formation and rearrangement of secreted proteins ?
-
 ?
5.3.4.1 additional information Streptomyces sp. NCIM 5127 both chaperone and isomerase functions of PDI are essential for acceleration of the oxidative refolding and reactivation of dimeric alkaline protease inhibitor API, PDI acts as isomerase/chaperone for a few monomeric proteins assisting in disulfide bond formation and rearrangement of secreted proteins ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
5.3.4.1 Streptomyces sp.
-
 NCIM 5127
-
5.3.4.1 Streptomyces sp. NCIM 5127
-
 NCIM 5127
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
5.3.4.1 additional information
-
-
 Streptomyces sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.3.4.1 alkaline protease inhibitor folding and rearrangement of alkaline protease inhibitor Streptomyces sp. ?
-
 ?
5.3.4.1 alkaline protease inhibitor folding and rearrangement of alkaline protease inhibitor, PDI contains 2 cysteine residues in the active site which are involved in rearrangement of disulfide bonds by function in thiol/disulfide exchange Streptomyces sp. ?
-
 ?
5.3.4.1 alkaline protease inhibitor folding and rearrangement of alkaline protease inhibitor Streptomyces sp. NCIM 5127 ?
-
 ?
5.3.4.1 alkaline protease inhibitor folding and rearrangement of alkaline protease inhibitor, PDI contains 2 cysteine residues in the active site which are involved in rearrangement of disulfide bonds by function in thiol/disulfide exchange Streptomyces sp. NCIM 5127 ?
-
 ?
5.3.4.1 additional information both chaperone and isomerase functions of PDI are essential for acceleration of the oxidative refolding and reactivation of dimeric alkaline protease inhibitor API, PDI acts as isomerase/chaperone for a few monomeric proteins assisting in disulfide bond formation and rearrangement of secreted proteins Streptomyces sp. ?
-
 ?
5.3.4.1 additional information both chaperone and isomerase functions of PDI are essential for acceleration of the oxidative refolding and reactivation of dimeric alkaline protease inhibitor API, PDI acts as isomerase/chaperone for a few monomeric proteins assisting in disulfide bond formation and rearrangement of secreted proteins Streptomyces sp. NCIM 5127 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
5.3.4.1 ? x * 55000 Streptomyces sp.

Synonyms

EC Number Synonyms Comment Organism
5.3.4.1 PDI
-
 Streptomyces sp.
5.3.4.1 protein disulfide isomerase
-
 Streptomyces sp.