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Literature summary for 1.8.4.16 extracted from

  • Missiakas, D.; Schwager, F.; Raina, S.
    Identification and charactcerization of a new disulfide isomerase-like protein (DsbD) in Escherichia coli (1995), EMBO J., 14, 3415-3424 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) cells Escherichia coli

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] with reduced L-cysteine residues + thioredoxin disulfide Escherichia coli overall reaction a [protein] carrying a disulfide bond + thioredoxin
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
? x * 53000, calculated from amino acid sequence Escherichia coli

Synonyms

Synonyms Comment Organism
disulfide isomerase-like protein
-
Escherichia coli
DsbD
-
Escherichia coli

Expression

Organism Comment Expression
Escherichia coli transcription of the enzyme gene is decreased at 50°C, but not completely turned off down

General Information

General Information Comment Organism
malfunction enzyme loss leads to hypersensitivity to dithiothreitol and benzylpenicillin Escherichia coli
metabolism the enzyme generates a reducing source in the periplasm, which is required for maintaining proper redox conditions Escherichia coli
physiological function the enzyme is essential for bacterial growth at temperatures above 42°C Escherichia coli