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Literature summary extracted from

  • Lambert, N.; Freedman, R.B.
    Kinetics and specificity of homogeneous protein disulphide-isomerase in protein disulphide isomerization and in thiol-protein-disulphide oxidoreduction (1983), Biochem. J., 213, 235-243.
    View publication on PubMedView publication on EuropePMC

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.8.4.2 additional information
-
 additional information
-
 Bos taurus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.8.4.2 phosphate enhances activity Bos taurus

Organism

EC Number Organism UniProt Comment Textmining
1.8.4.2 Bos taurus
-
-
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.8.4.2 additional information
-
-
 Bos taurus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.4.2 GSH + insulin
-
 Bos taurus GSSG + reduced insulin chain A and B
-
 ?
1.8.4.2 GSH + protein disulfide
-
 Bos taurus GSSG + protein-dithiol
-
 ?
1.8.4.2 additional information the two activities, cleavage and formation of protein-disulfide bonds, present alternate activities of the same enzyme Bos taurus ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.8.4.2 More the two activities, cleavage and formation of protein-disulfide bonds, present alternate activities of the same enzyme Bos taurus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.8.4.2 7.8
-
-
 Bos taurus