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Literature summary for 1.8.4.16 extracted from

  • Kurokawa, Y.; Yanagi, H.; Yura, T.
    Overproduction of bacterial protein disulfide isomerase (DsbC) and its modulator (DsbD) markedly enhances periplasmic production of human nerve growth factor in Escherichia coli (2001), J. Biol. Chem., 276, 14393-14399 .
No PubMed abstract available
Search for more literature for 1.8.4.16

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
 Escherichia coli 16020
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
a [protein] carrying a disulfide bond + thioredoxin Escherichia coli overall reaction a [protein] with reduced L-cysteine residues + thioredoxin disulfide
-
 ?
[DsbC protein] carrying a disulfide bond + thioredoxin Escherichia coli
-
 [DsbC protein] with reduced L-cysteine residues + thioredoxin disulfide
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
a [protein] carrying a disulfide bond + thioredoxin overall reaction Escherichia coli a [protein] with reduced L-cysteine residues + thioredoxin disulfide
-
 ?
[DsbC protein] carrying a disulfide bond + thioredoxin
-
 Escherichia coli [DsbC protein] with reduced L-cysteine residues + thioredoxin disulfide
-
 ?

Synonyms

Synonyms Comment Organism
dipZ
-
 Escherichia coli
DsbD
-
 Escherichia coli

General Information

General Information Comment Organism
physiological function overproduction of the enzyme and protein disulfide isomerase DsbC markedly enhances periplasmic production of human nerve growth factor in Escherichia coli Escherichia coli