The enzyme catalyzes the reduction of arsenate (HAsO) to arsenite (H3AsO3) and participates in the arsenic detoxification systems of prokaryotes and eukaryotes PMID12072565. The enzyme from Staphylococcus aureus binds a potassium ion that is involved in stabilizing the structure of the active site and increases the activity of the enzyme PMID16797027.
CATALYTIC METAL(S)
| Metal/Site Information | |||||
| Residue in MACiE* | Atom in MACiE* | Residue Type in MACiE | Physiological Metal |
Site Type |
Function(s) |
| K 133 _ | K | potassium | potassium | mononuclear | Structural (in the active site) |
*It refers to the MACiE reference pdb: 1ljl
| Metal/s Properties in Resting State | ||||||
| K 133 _ | Resting state enzyme (1ljl) | |||||
| Oxidation State | 1 | |||||
| Coordination Geometry | cappedOctahedron | |||||
| Coordination Number | 7 | |||||
| Notes | - | |||||
| References |
| -Roos G, Buts L, Van Belle K, Brosens E, Geerlings P, Loris R, Wyns L, Messens J Interplay between ion binding and catalysis in the thioredoxin-coupled arsenate reductase family. J Mol Biol. 2006 Jul 21;360(4):826-38. Epub 2006 Jun 6.(MEDLINE:16797027) |