1.8.4.16: thioredoxin:protein disulfide reductase
This is an abbreviated version!
For detailed information about thioredoxin:protein disulfide reductase, go to the full flat file.
Word Map on EC 1.8.4.16
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1.8.4.16
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chaperone
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methanothermobacter
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pdi-like
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extremophiles
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thermoautotrophicum
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gssg
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testis-specific
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pdilt
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mercuric
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agrobacterium-mediated
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nipponbare
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non-protein
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phytochelatins
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non-classical
- 1.8.4.16
- chaperone
- methanothermobacter
-
pdi-like
-
extremophiles
- thermoautotrophicum
- gssg
-
testis-specific
- pdilt
-
mercuric
-
agrobacterium-mediated
-
nipponbare
-
non-protein
- phytochelatins
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non-classical
Reaction
Synonyms
CcdA, dipZ, disulfide bond reductase, disulfide isomerase-like protein, DsbD, DsbDalpha, NmDsbD
ECTree
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General Information
General Information on EC 1.8.4.16 - thioredoxin:protein disulfide reductase
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malfunction
metabolism
physiological function
additional information
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enzyme absence enhances the sensitivity of the dsbA1A2 mutant to oxidative stress
malfunction
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enzyme loss leads to hypersensitivity to dithiothreitol and benzylpenicillin
malfunction
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enzyme absence enhances the sensitivity of the dsbA1A2 mutant to oxidative stress
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cytoplasmic electrons donated by thioredoxin are transferred into the periplasm via the enzyme
metabolism
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the enzyme accepts electrons from cytoplasmic thioredoxin and shuttles these electrons via a well-defined cascade through the membrane-spanning region and into the periplasm
metabolism
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the enzyme generates a reducing source in the periplasm, which is required for maintaining proper redox conditions
metabolism
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the enzyme is a reductase that acts as an electron hub, translocating reducing equivalents from cytoplasmic thioredoxin to a number of periplasmic substrates involved in oxidative protein folding, cytochrome c maturation and oxidative stress defence
metabolism
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the enzyme is required to maintain the functional oxidation state of DsbC and DsbG
metabolism
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the enzyme mediates electron transfer from the cytoplasm across the membrane
metabolism
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the enzyme transfers reducing potential to periplasmic protein disulfide bond isomerases and to the cytochromexa0c thioreduction pathway
metabolism
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the enzyme is a reductase that acts as an electron hub, translocating reducing equivalents from cytoplasmic thioredoxin to a number of periplasmic substrates involved in oxidative protein folding, cytochrome c maturation and oxidative stress defence
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overproduction of the enzyme and protein disulfide isomerase DsbC markedly enhances periplasmic production of human nerve growth factor in Escherichia coli
physiological function
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the enzyme is essential for bacterial growth at temperatures above 42°C
physiological function
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the enzyme is essential for survival of Neisseria gonorrhoeae
physiological function
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the enzyme is required for the survival Neisseria meningitides
physiological function
NmDsbD is essential for viability. To initiate electron transport across the inner membrane, the disulfide bonded cysteine residues in t-DsbD are reduced by cytoplasmic thioredoxin. The transmebrane part, t-DsbD, in turn reduces the disulfide bond in c-DsbD, which then reduces n-DsbD. Lastly, n-DsbD transfers electrons to periplasmic substrates including the isomerases DsbC and DsbG, which reshuffle non-native disulfide bonds in multi-cysteine containing, as well as the reductases CcmG (DsbE), and CcmH which are involved in cytochrome c maturation
physiological function
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the enzyme is required for the survival Neisseria meningitides
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physiological function
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NmDsbD is essential for viability. To initiate electron transport across the inner membrane, the disulfide bonded cysteine residues in t-DsbD are reduced by cytoplasmic thioredoxin. The transmebrane part, t-DsbD, in turn reduces the disulfide bond in c-DsbD, which then reduces n-DsbD. Lastly, n-DsbD transfers electrons to periplasmic substrates including the isomerases DsbC and DsbG, which reshuffle non-native disulfide bonds in multi-cysteine containing, as well as the reductases CcmG (DsbE), and CcmH which are involved in cytochrome c maturation
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13Calpha and 13Cbeta chemical shift comparison of the two active site cysteine residues between n-NmDsbDOx and n-NmDsbDRed relative to the average BMRB shift values, overview
additional information
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13Calpha and 13Cbeta chemical shift comparison of the two active site cysteine residues between n-NmDsbDOx and n-NmDsbDRed relative to the average BMRB shift values, overview
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