4g98: 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=4g98 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g98 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4g98 RCSB], [http://www.ebi.ac.uk/pdbsum/4g98 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=4g98 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g98 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4g98 RCSB], [http://www.ebi.ac.uk/pdbsum/4g98 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[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. | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
