3wkt
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=3wkt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wkt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wkt RCSB], [http://www.ebi.ac.uk/pdbsum/3wkt 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=3wkt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wkt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wkt RCSB], [http://www.ebi.ac.uk/pdbsum/3wkt PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/NCPR_RAT NCPR_RAT]] This enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome B5. [[http://www.uniprot.org/uniprot/HMOX1_RAT HMOX1_RAT]] Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 14:17, 25 December 2014
Complex structure of an open form of NADPH-cytochrome P450 reductase and heme oxygenase-1
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