1ozl: Difference between revisions
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{{STRUCTURE_1ozl| PDB=1ozl | SCENE= }} | {{STRUCTURE_1ozl| PDB=1ozl | SCENE= }} | ||
===Crystal Structures of the Ferric, Ferrous, and Ferrous-NO Forms of the Asp140Ala Mutant of Human Heme Oxygenase-1: Catalytic Implications=== | |||
{{ABSTRACT_PUBMED_12842469}} | |||
=== | ==Disease== | ||
[[http://www.uniprot.org/uniprot/HMOX1_HUMAN HMOX1_HUMAN]] Defects in HMOX1 are the cause of heme oxygenase 1 deficiency (HMOX1D) [MIM:[http://omim.org/entry/614034 614034]]. A disease characterized by impaired stress hematopoiesis, resulting in marked erythrocyte fragmentation and intravascular hemolysis, coagulation abnormalities, endothelial damage, and iron deposition in renal and hepatic tissues. Clinical features include persistent hemolytic anemia, asplenia, nephritis, generalized erythematous rash, growth retardation and hepatomegaly.<ref>PMID:9884342</ref> | |||
==Function== | |||
[[http://www.uniprot.org/uniprot/HMOX1_HUMAN HMOX1_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. | |||
==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
<ref group="xtra">PMID:012842469</ref><references group="xtra"/> | <ref group="xtra">PMID:012842469</ref><references group="xtra"/><references/> | ||
[[Category: Heme oxygenase]] | [[Category: Heme oxygenase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||