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Literature summary for 1.8.4.2 extracted from

  • Varandani, P.T.
    Mechanistic and structural aspects of glutathione-insulin transhydogenase (protein-disulfide interchange enzyme) (1978), Dev. Biochem., 1, 29-42.
No PubMed abstract available
Search for more literature for 1.8.4.2

Activating Compound

Activating Compound Comment Organism Structure
deoxycholate activating the enzyme membrane-bound in the microsomal fraction Rattus norvegicus
Triton X-100 activating the enzyme membrane-bound in the microsomal fraction Rattus norvegicus

Inhibitors

Inhibitors Comment Organism Structure
deoxycholate
-
 Bos taurus
deoxycholate inhibitory for the solubilized enzyme Rattus norvegicus
lysolecithin
-
 Bos taurus
lysolecithin
-
 Homo sapiens
lysolecithin
-
 Rattus norvegicus
phosphatidic acid
-
 Bos taurus
phosphatidic acid
-
 Homo sapiens
phosphatidic acid
-
 Rattus norvegicus
Triton X-100 inhibitory for the solubilized enzyme Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-
Homo sapiens
-
-
-
Rattus norvegicus
-
-
-

Reaction

Reaction Comment Organism Reaction ID
2 glutathione + protein-disulfide = glutathione-disulfide + protein-dithiol random and allosteric mechanism via multiple distinct reaction sites Homo sapiens
a
2 glutathione + protein-disulfide = glutathione-disulfide + protein-dithiol random and allosteric mechanism via multiple distinct reaction sites Rattus norvegicus
a
2 glutathione + protein-disulfide = glutathione-disulfide + protein-dithiol random and allosteric mechanism via multiple distinct reaction sites Bos taurus
a

Source Tissue

Source Tissue Comment Organism Textmining
heart
-
 Homo sapiens
-
heart
-
 Rattus norvegicus
-
heart
-
 Bos taurus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
GSH + insulin proinsulin Homo sapiens GSSG + reduced insulin chain A and B
-
 ?
GSH + insulin proinsulin Rattus norvegicus GSSG + reduced insulin chain A and B
-
 ?
GSH + insulin proinsulin Bos taurus GSSG + reduced insulin chain A and B
-
 ?
GSH + oxytoxin
-
 Homo sapiens ?
-
 ?
GSH + oxytoxin
-
 Rattus norvegicus ?
-
 ?
GSH + oxytoxin
-
 Bos taurus ?
-
 ?
GSH + protein disulfide
-
 Homo sapiens GSSG + protein-dithiol
-
 ?
GSH + protein disulfide
-
 Rattus norvegicus GSSG + protein-dithiol
-
 ?
GSH + protein disulfide
-
 Bos taurus GSSG + protein-dithiol
-
 ?
GSH + vasopressin
-
 Homo sapiens ?
-
 ?
GSH + vasopressin
-
 Rattus norvegicus ?
-
 ?
GSH + vasopressin
-
 Bos taurus ?
-
 ?
additional information the two activities, cleavage and formation of protein-disulfide bonds, present alternate activities of the same enzyme Homo sapiens ?
-
 ?
additional information the two activities, cleavage and formation of protein-disulfide bonds, present alternate activities of the same enzyme Rattus norvegicus ?
-
 ?
additional information the two activities, cleavage and formation of protein-disulfide bonds, present alternate activities of the same enzyme Bos taurus ?
-
 ?
additional information immunoglobulin IgM and IgG Homo sapiens ?
-
 ?
additional information immunoglobulin IgM and IgG Rattus norvegicus ?
-
 ?
additional information immunoglobulin IgM and IgG Bos taurus ?
-
 ?
additional information scrambled lysozyme Homo sapiens ?
-
 ?
additional information scrambled lysozyme Rattus norvegicus ?
-
 ?
additional information scrambled lysozyme Bos taurus ?
-
 ?
additional information scrambled trypsin inhibitor and proinsulin Homo sapiens ?
-
 ?
additional information scrambled trypsin inhibitor and proinsulin Rattus norvegicus ?
-
 ?
additional information scrambled trypsin inhibitor and proinsulin Bos taurus ?
-
 ?
additional information thiol:protein-disulfide oxidoreductase EC 1.8.4.2 and thiol:protein-disulfide isomerase EC 5.3.4.1 are immunological identical Homo sapiens ?
-
 ?
additional information thiol:protein-disulfide oxidoreductase EC 1.8.4.2 and thiol:protein-disulfide isomerase EC 5.3.4.1 are immunological identical Rattus norvegicus ?
-
 ?
additional information thiol:protein-disulfide oxidoreductase EC 1.8.4.2 and thiol:protein-disulfide isomerase EC 5.3.4.1 are immunological identical Bos taurus ?
-
 ?
additional information enzyme also catalyzes reactivation and folding of protein containing incorrectly paired disulfide bond, e.g.: scrambled ribonuclease Homo sapiens ?
-
 ?
additional information enzyme also catalyzes reactivation and folding of protein containing incorrectly paired disulfide bond, e.g.: scrambled ribonuclease Rattus norvegicus ?
-
 ?
additional information enzyme also catalyzes reactivation and folding of protein containing incorrectly paired disulfide bond, e.g.: scrambled ribonuclease Bos taurus ?
-
 ?

Synonyms

Synonyms Comment Organism
More the two activities, cleavage and formation of protein-disulfide bonds, present alternate activities of the same enzyme Homo sapiens
More the two activities, cleavage and formation of protein-disulfide bonds, present alternate activities of the same enzyme Rattus norvegicus
More the two activities, cleavage and formation of protein-disulfide bonds, present alternate activities of the same enzyme Bos taurus
More thiol:protein-disulfide oxidoreductase EC 1.8.4.2 and thiol:protein-disulfide isomerase EC 5.3.4.1 are immunological identical Homo sapiens
More thiol:protein-disulfide oxidoreductase EC 1.8.4.2 and thiol:protein-disulfide isomerase EC 5.3.4.1 are immunological identical Rattus norvegicus
More thiol:protein-disulfide oxidoreductase EC 1.8.4.2 and thiol:protein-disulfide isomerase EC 5.3.4.1 are immunological identical Bos taurus