1.20.4.4: arsenate reductase (thioredoxin)
This is an abbreviated version!
For detailed information about arsenate reductase (thioredoxin), go to the full flat file.
Reaction
Synonyms
ARS, ArsC, ArsC1, ArsC1', ArsC3, arsenate reductase, Bs_ArsC, pI258 arsenate reductase, plasmid pI258 arsenate reductase, Sa_ArsC, Strop634, thioredoxin-arsenate reductase complex, thioredoxin-coupled arsenate reductase, Trx-coupled arsenate reductase
ECTree
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Engineering
Engineering on EC 1.20.4.4 - arsenate reductase (thioredoxin)
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C10S/C15A/C82S
mutant in complex with the thioredoxin C32S mutant. Solve the structure of the Trx-ArsC complex by NMR spectroscopy
C10A
C10S/C15A
C10S/C15A/C82S
C10S/C15A/C89L
mutant, determination of the redox potential of the Cys82-Cys89 redox couple
C15A
C82A
C82S
C89A
C7S
additional information
C10A
site-directed mutagenesis, mutation of Cys 10, 82, and 89 leads to redox-inactive enzymes
mutant, determination of the redox potential of the Cys82-Cys89 redox couple, thioredoxin is unable to reduce the Cys10-Cys15 disulfide in oxidized ArsC C82S
C10S/C15A/C82S
site-directed mutagenesis, triple mutant, structure very similar to that of the reduced form of wild-type ArsC
C15A
site-directed mutagenesis, only ArsC wild type and ArsC C15A show enzymatic activity
C15A
as compared to wild-type enzyme the affinity is reduced ba a factor of 2
C82A
site-directed mutagenesis, mutation of Cys 10, 82, and 89 leads to redox-inactive enzymes
C82S
site-directed mutagenesis, mutation of Cys 10, 82, and 89 leads to redox-inactive enzymes
C89A
site-directed mutagenesis, mutation of Cys 10, 82, and 89 leads to redox-inactive enzymes
commonly occurring mutation of a histidine (H62), located about 6 A from the potassium-binding site in Sa_ArsC, to a glutamine uncouples the kinetic dependency on potassium. Mutations within the Trx-coupled family of arsenate reductases lead to subtly different ion-dependent kinetic features
additional information
-
commonly occurring mutation of a histidine (H62), located about 6 A from the potassium-binding site in Sa_ArsC, to a glutamine uncouples the kinetic dependency on potassium. Mutations within the Trx-coupled family of arsenate reductases lead to subtly different ion-dependent kinetic features
additional information
in mutant lacking N-terminal 78 amino acids, the kinetic parameters are greatly reduced
additional information
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in mutant lacking N-terminal 78 amino acids, the kinetic parameters are greatly reduced
-
additional information
ArsC triple mutants and the Trx C32S mutant formate a ArsC-TrxC32S complex
additional information
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ArsC triple mutants and the Trx C32S mutant formate a ArsC-TrxC32S complex
additional information
commonly occurring mutation of a histidine (H62), located about 6 A from the potassium-binding site in Sa_ArsC, to a glutamine uncouples the kinetic dependency on potassium. Mutations within the Trx-coupled family of arsenate reductases lead to subtly different ion-dependent kinetic features
additional information
-
commonly occurring mutation of a histidine (H62), located about 6 A from the potassium-binding site in Sa_ArsC, to a glutamine uncouples the kinetic dependency on potassium. Mutations within the Trx-coupled family of arsenate reductases lead to subtly different ion-dependent kinetic features
additional information
essential cysteinyl residues and redox couple in arsenate reductase are identified by a combination of site-specific mutagenesis and endoprotease-digest mass spectroscopy analysis