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
-
non-classical
Reaction
Synonyms
CcdA, dipZ, disulfide bond reductase, disulfide isomerase-like protein, DsbD, DsbDalpha, NmDsbD
ECTree
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Engineering on EC 1.8.4.16 - thioredoxin:protein disulfide reductase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C103A
C103A/C109A
C163A/C282A
Echerichia coli expressing the C163A and C282A mutations is Cu2+ resistant
C163A/C285A
C282A/C285A
Echerichia coli expressing the C282A and C285A mutations is Cu2+ resistant
C461A/C464A
Echerichia coli expressing the C461A and C464A mutations is Cu2+ sensitive
C464A
D455N/E468Q
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in the double mutant of periplasmic C-terminal domain of the enzyme, the pK(a) value of Cys461 is lowered to 8.6, a value close to that expected for an unperturbed cysteine residue
P162A
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the mutation leads to less viability on copper and less susceptibility to air oxidation than wild type
P166A
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the mutation leads to less viability on copper and less susceptibility to air oxidation than wild type
P284A
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the mutation leads to less viability on copper and less susceptibility to air oxidation than wild type
P289A
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the mutation leads to less viability on copper and less susceptibility to air oxidation than wild type
C103S
C103A/C109A
Echerichia coli expressing the C103A and C109A mutations is Cu2+ sensitive and shows no enzymatic activity
C163A/C285A
Echerichia coli expressing the C163A and C285A mutations is Cu2+ sensitive and shows no enzymatic activity
