2l17
From Proteopedia
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2l17 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l17 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2l17 RCSB], [http://www.ebi.ac.uk/pdbsum/2l17 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2l17 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l17 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2l17 RCSB], [http://www.ebi.ac.uk/pdbsum/2l17 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/P74313_SYNY3 P74313_SYNY3]] Reduces arsenate [As(V)] to arsenite [As(III)] using glutathione and glutaredoxin as sources of reducing equivalents. GrxA is the most effective electron donor in vivo compared to other glutaredoxins. Constitutes the major arsenate reductase compared to ArsI1 and ArsI2. Also shows weak phosphatase activity toward p-nitrophenyl phosphate.<ref>PMID:14617642</ref> <ref>PMID:19304854</ref> <ref>PMID:22155275</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Revision as of 16:57, 25 December 2014
An arsenate reductase in the reduced state
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