more
both glutathione-SH and glutaredoxin are required for activity. No substrate: phosphate
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-
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more
no substrate: phosphate, nitrate
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-
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more
chemical shift assignments of 1H, 13C and 15N atoms for the reduced form the enzyme
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-
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more
the enzyme exhibits weak phosphatase activity toward 4-nitrophenyl phosphate
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-
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more
the enzyme requires the glutaredoxin system for its reactivation
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-
?
arsenate + reduced glutaredoxin
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arsenite + oxidized glutaredoxin
-
?
arsenate + reduced glutaredoxin
-
arsenite + oxidized glutaredoxin
-
?
arsenate + reduced glutaredoxin
-
arsenite + oxidized glutaredoxin
-
?
arsenate + reduced glutaredoxin
strong specificity for arsenate
arsenite + oxidized glutaredoxin
-
?
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
arsenite + oxidized glutaredoxin
-
?
