4wmh: 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=4wmh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wmh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4wmh RCSB], [http://www.ebi.ac.uk/pdbsum/4wmh 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=4wmh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wmh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4wmh RCSB], [http://www.ebi.ac.uk/pdbsum/4wmh PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/HMOX2_HUMAN HMOX2_HUMAN]] 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. Heme oxygenase 2 could be implicated in the production of carbon monoxide in brain where it could act as a neurotransmitter. | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Heme oxygenase]] | [[Category: Heme oxygenase]] | ||
[[Category: Bianchetti, C M | [[Category: Bianchetti, C M]] | ||
[[Category: | [[Category: Structural genomic]] | ||
[[Category: Li, Y | [[Category: Li, Y]] | ||
[[Category: Phillips, G N | [[Category: Phillips, G N]] | ||
[[Category: Ragsdale, S W | [[Category: Ragsdale, S W]] | ||
[[Category: Cesg]] | [[Category: Cesg]] | ||
[[Category: Ho2]] | [[Category: Ho2]] | ||
[[Category: Oxygenase]] | [[Category: Oxygenase]] | ||
[[Category: Protein structure initiative | [[Category: PSI, Protein structure initiative]] | ||
Revision as of 08:13, 25 December 2014
Structure of heme oxygenase-2 containing residues 1-288 lacking the membrane spanning regionStructure of heme oxygenase-2 containing residues 1-288 lacking the membrane spanning region
Structural highlights
Function[HMOX2_HUMAN] 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. Heme oxygenase 2 could be implicated in the production of carbon monoxide in brain where it could act as a neurotransmitter. |
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