3gx0
From Proteopedia
(Difference between revisions)
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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=3gx0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gx0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3gx0 RCSB], [http://www.ebi.ac.uk/pdbsum/3gx0 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=3gx0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gx0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3gx0 RCSB], [http://www.ebi.ac.uk/pdbsum/3gx0 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/YFCG_ECOLI YFCG_ECOLI]] Exhibits a very robust glutathione (GSH)-dependent disulfide-bond reductase activity toward the model substrate, 2-hydroxyethyl disulfide; the actual physiological substrates are not known. Has also a low GSH-dependent hydroperoxidase activity toward cumene hydroperoxide, but does not reduce H(2)O(2), tert-butyl hydroperoxide, benzyl peroxide, or lauroyl peroxide. Exhibits little or no GSH transferase activity with most typical electrophilic substrates, and has no detectable transferase activity using glutathionylspermidine (GspSH) as the nucleophilic substrate. Is involved in defense against oxidative stress, probably via its peroxidase activity.<ref>PMID:17018556</ref> <ref>PMID:19537707</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 15:20, 25 December 2014
Crystal Structure of GSH-dependent Disulfide bond Oxidoreductase
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