EC Number   |
BRENDA No. |
Title |
Journal |
Volume |
Pages |
Year |
Organism |
PubMed ID  |
|---|
   1.20.99.1 | 716477 |
Arsenate reductase activity in roots from the arsenic hyperaccumulator Pteris vittata utilizes both glutathione and dithiothreitol as reductants |
Plant Biosyst. |
144 |
857-859 |
2010 |
Pteris vittata |
- |
| 1.20.99.1 | 639373 |
Enzymatic reduction of arsenic compounds in mammalian systems Reduction of arsenate to arsenite by human liver arsenate reductase |
Chem. Res. Toxicol. |
200; 13 |
26-30 |
2000 |
Homo sapiens |
- |
| 1.20.99.1 | 693852 |
Reduction of arsenic oxidative toxicity by phosphate is not related to arsenate reductase activity in wheat plants |
J. Plant Nutr. |
30 |
2105-2117 |
2007 |
Triticum sp. |
- |
| 1.20.99.1 | 287859 |
Purification and characterization of the respiratory arsenate reductase of Chrysiogenes arsenatis |
Eur. J. Biochem. |
255 |
647-653 |
1998 |
Chrysiogenes arsenatis |
9738904 |
| 1.20.99.1 | 287858 |
Crystal structure of the 100 kDa arsenite oxidase from Alcaligenes faecalis in two crystal forms at 1.64 A and 2.03 A |
Structure |
9 |
125-132 |
2001 |
Alcaligenes faecalis |
11250197 |
| 1.20.99.1 | 657473 |
Preparation and crystallization of a Bacillus subtilis arsenate reductase |
Acta Crystallogr. Sect. D |
D57 |
1718-1721 |
2001 |
Bacillus subtilis |
11679756 |
| 1.20.99.1 | 660404 |
Bacillus subtilis arsenate reductase is structurally and functionally similar to low molecular weight protein tyrosine phosphatases |
Proc. Natl. Acad. Sci. USA |
98 |
13577-13582 |
2001 |
Bacillus subtilis |
11698660 |
| 1.20.99.1 | 660525 |
Insights into the structure, solvation, and mechanism of ArsC arsenate reductase, a novel arsenic detoxification enzyme |
Structure |
9 |
1071-1081 |
2001 |
Escherichia coli |
11709171 |
| 1.20.99.1 | 658961 |
The active site of arsenite oxidase from Alcaligenes faecalis |
J. Am. Chem. Soc. |
124 |
11276-11277 |
2002 |
Alcaligenes faecalis |
12236735 |
| 1.20.99.1 | 658052 |
Electrochemical studies of arsenite oxidase: an unusual example of a highly cooperative two-electron molybdenum center |
Biochemistry |
43 |
1667-1674 |
2004 |
Alcaligenes faecalis |
14769044 |
