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heme oxygenase-1 (HMOX1, heat shock protein 32, HO1)

Function: - in association with cyt P450 reductase & bilirubin reductase, cleaves heme to form bilirubin, CO & Fe+2 - electrons donated by cyt P450 reductase - biliverdin reductase rapidly reduces biliverdin to bilirubin heme oxygenase cyt P450 reductase heme[Fe+2] + O2 ------------------> biliverdin + CO + Fe+2 + NADPH + H+ + NADP+ + H2O biliverdin reductase biliverdin ------------------> bilirubin + NADP+ + NADPH + H+ Structure: belongs to the heme oxygenase family Compartment: microsome Expression: - found especially in spleen & other peripheral tissues associated with destruction of erythrocytes - highly inducible by its substrate heme & by various non-heme substances such as heavy metals, bromobenzene, endotoxin, oxidizing agents & UVA - inducible by stress, including inflammation & heat shock

Related

heme heme catabolism heme oxygenase 1 gene

General

heat shock protein heme oxygenase

Properties

SIZE: entity length = 288 aa MW = 33 kD COMPARTMENT: smooth endoplasmic reticulum CELL: macrophage WITHIN: spleen MOTIF: Iron [Fe]-binding site SITE: 25-25 active site Ser phosphorylation site {S229}

Database Correlations

OMIM 141250 UniProt P09601 Pfam PF01126 Kegg hsa/hsa00860 ENZYME 1.14.99.3

References

  1. Snyder SH. Nitric oxide: first in a new class of neurotransmitters. Science. 1992 Jul 24;257(5069):494-6. Review. PMID: 1353273
  2. Smith MA, Kutty RK, Richey PL, Yan SD, Stern D, Chader GJ, Wiggert B, Petersen RB, Perry G. Heme oxygenase-1 is associated with the neurofibrillary pathology of Alzheimer's disease. Am J Pathol. 1994 Jul;145(1):42-7. PMID: 8030754 1994
  3. Sedlak TW, Snyder SH. Messenger molecules & cell death: therapeutic implications. JAMA. 2006 Jan 4;295(1):81-9. PMID: 16391220
  4. UniProt :accession P09601

Component-of

multienzyme complex