1.20.4.1 arsenate + glutaredoxin - Saccharomyces cerevisiae arsenite + glutaredoxin disulfide + H2O - ? 442283 1.20.4.1 arsenate + glutaredoxin - Myxococcus xanthus arsenite + glutaredoxin disulfide + H2O - ? 442283 1.20.4.1 arsenate + glutaredoxin - Synechocystis sp. PCC 6803 arsenite + glutaredoxin disulfide + H2O - ? 442283 1.20.4.1 arsenate + glutaredoxin - Saccharomyces cerevisiae BY4741 arsenite + glutaredoxin disulfide + H2O - ? 442283 1.20.4.1 arsenate + glutaredoxin 1 - Escherichia coli arsenite + glutaredoxin 1 disulfide + H2O - r 451480 1.20.4.1 arsenate + glutaredoxin 2 - Escherichia coli arsenite + glutaredoxin 1 disulfide + H2O - r 451481 1.20.4.1 arsenate + glutaredoxin 2 - Escherichia coli arsenite + glutaredoxin 2 disulfide + H2O - r 453877 1.20.4.1 arsenate + glutaredoxin 3 - Escherichia coli arsenite + glutaredoxin 1 disulfide + H2O - r 451482 1.20.4.1 arsenate + glutaredoxin 3 - Escherichia coli arsenite + glutaredoxin 3 disulfide + H2O - r 453878 1.20.4.1 arsenate + glutaredoxin C7 - Saccharomyces cerevisiae arsenite + glutaredoxin C7 disulfide + H2O - ? 443066 1.20.4.1 arsenate + glutaredoxin C7 - Saccharomyces cerevisiae BY4741 arsenite + glutaredoxin C7 disulfide + H2O - ? 443066 1.20.4.1 arsenate + glutaredoxin C72.1 - Saccharomyces cerevisiae arsenite + glutaredoxin C72.1 disulfide + H2O - ? 443065 1.20.4.1 arsenate + glutaredoxin C72.1 - Saccharomyces cerevisiae BY4741 arsenite + glutaredoxin C72.1 disulfide + H2O - ? 443065 1.20.4.1 arsenate + glutathione - Myxococcus xanthus arsenite + glutathione disulfide + H2O - ? 443067 1.20.4.1 arsenate + reduced acceptor - Arabidopsis thaliana arsenite + acceptor - ? 375054 1.20.4.1 arsenate + reduced acceptor - Oryza sativa arsenite + acceptor - ? 375054 1.20.4.1 arsenate + reduced glutaredoxin - Pteris vittata arsenite + oxidized glutaredoxin - ? 355979 1.20.4.1 arsenate + reduced glutaredoxin - Synechocystis sp. arsenite + oxidized glutaredoxin - ? 355979 1.20.4.1 arsenate + reduced glutaredoxin - Nostoc sp. arsenite + oxidized glutaredoxin - ? 355979 1.20.4.1 arsenate + reduced glutaredoxin strong specificity for arsenate Escherichia coli arsenite + oxidized glutaredoxin - ? 355979 1.20.4.1 arsenate + reduced glutaredoxin thioredoxin is unable to support arsenate reduction. The N-terminal Cys residue is essential for arsenate reductase activity. During the catalytic cycle, Acr2p forms a mixed disulfide with GSH before being reduced vby glutaredoxin to regenerate the active Acr2p reductase Saccharomyces cerevisiae arsenite + oxidized glutaredoxin - ? 355979 1.20.4.1 arsenate + reduced glutaredoxin the first step of the reaction is the binding of arsenate, followed by the interaction of the enzyme-arsenate complex with GSH. A reaction scheme is hypothesized in which the enzyme forms a mixed disulfide between the Cys-12 thiolate of ArsC and GSH. Glutaredoxin would then be required to resolve the mixed disulfide, regenerating reduced ArsC Escherichia coli arsenite + oxidized glutaredoxin - ? 355979 1.20.4.1 arsenate + reduced glutaredoxin thioredoxin is not effective as electron donor Escherichia coli arsenite + oxidized glutaredoxin - ? 355979 1.20.4.1 arsenate + reduced glutaredoxin the enzyme uses GSH with glutaredoxin as electron donor. Glutaredoxin 2 is the most effective hydrogen donor for the reduction of arsenate. During the catalytic cycle, ArsC forms a mixed disulfide with GSH before being reduced by glutaredoxin to regenerate the active ArsC reductase Escherichia coli arsenite + oxidized glutaredoxin - ? 355979 1.20.4.1 arsenate + reduced glutaredoxin C12 is located at the active site and is required for catalysis Escherichia coli arsenite + oxidized glutaredoxin - ? 355979 1.20.4.1 arsenate + reduced glutaredoxin the enzyme is involved in bacterial arsenic resistance Escherichia coli arsenite + oxidized glutaredoxin - ? 355979 1.20.4.1 arsenate + reduced glutaredoxin enzyme catalyzes the oxidation of NADPH coupled with reduction of arsenate in the presence of glutathione reductase, glutathione and glutaredoxin Nostoc sp. arsenite + oxidized glutaredoxin - ? 355979 1.20.4.1 arsenate + reduced glutaredoxin glutaredoxin functions as the electron donor for arsenate reduction Cronobacter sakazakii arsenite + oxidized glutaredoxin - ? 355979 1.20.4.1 arsenate + reduced glutaredoxin glutaredoxin functions as the electron donor for arsenate reduction Cronobacter sakazakii ATCC BAA-894 arsenite + oxidized glutaredoxin - ? 355979 1.20.4.1 arsenate + reduced glutaredoxin - Nostoc sp. PCC 7120 arsenite + oxidized glutaredoxin - ? 355979 1.20.4.1 arsenate + reduced glutaredoxin enzyme catalyzes the oxidation of NADPH coupled with reduction of arsenate in the presence of glutathione reductase, glutathione and glutaredoxin Nostoc sp. PCC 7120 arsenite + oxidized glutaredoxin - ? 355979 1.20.4.1 arsenate + reduced glutathione - Arabidopsis thaliana arsenite + glutathione - ? 375055 1.20.4.1 arsenate + reduced glutathione - Oryza sativa arsenite + glutathione - ? 375055 1.20.4.1 arsenate + reduced glutathione - Pteris vittata arsenite + glutathione - ? 375055 1.20.4.1 arsenate + reduced glutathione enzyme plays an important role in detoxification of arsenate Pteris vittata arsenite + glutathione - ? 375055 1.20.4.1 arsenate + reduced glutathione + NAD+ + glyceraldehyde-3-phosphate - Homo sapiens arsenite + glutathione + ? - ? 387889 1.20.4.1 arsenate + reduced glutathione + NAD+ + glyceraldehyde-3-phosphate - Rattus norvegicus arsenite + glutathione + ? - ? 387889 1.20.4.1 arsenite + acceptor high activity Myxococcus xanthus arsenate + reduced acceptor - ? 375056 1.20.4.1 additional information both glutathione-SH and glutaredoxin are required for activity. No substrate: phosphate Pteris vittata ? - ? 89 1.20.4.1 additional information no substrate: phosphate, nitrate Pteris vittata ? - ? 89 1.20.4.1 additional information chemical shift assignments of 1H, 13C and 15N atoms for the reduced form the enzyme Synechocystis sp. ? - ? 89 1.20.4.1 additional information the enzyme exhibits weak phosphatase activity toward 4-nitrophenyl phosphate Myxococcus xanthus ? - ? 89 1.20.4.1 additional information the enzyme requires the glutaredoxin system for its reactivation Synechocystis sp. PCC 6803 ? - ? 89