Aliases for HMOX1 Gene
External Ids for HMOX1 Gene
Previous GeneCards Identifiers for HMOX1 Gene
Heme oxygenase, an essential enzyme in heme catabolism, cleaves heme to form biliverdin, which is subsequently converted to bilirubin by biliverdin reductase, and carbon monoxide, a putative neurotransmitter. Heme oxygenase activity is induced by its substrate heme and by various nonheme substances. Heme oxygenase occurs as 2 isozymes, an inducible heme oxygenase-1 and a constitutive heme oxygenase-2. HMOX1 and HMOX2 belong to the heme oxygenase family. [provided by RefSeq, Jul 2008]
GeneCards Summary for HMOX1 Gene
HMOX1 (Heme Oxygenase 1) is a Protein Coding gene. Diseases associated with HMOX1 include pulmonary disease, chronic obstructive and heme oxygenase-1 deficiency. Among its related pathways are MicroRNAs in cancer and Angiogenesis (CST). GO annotations related to this gene include protein homodimerization activity and enzyme binding. An important paralog of this gene is HMOX2.
UniProtKB/Swiss-Prot for HMOX1 Gene
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. Exhibits cytoprotective effects since excess of free heme sensitizes cells to undergo apoptosis
Heme oxygenase (HO) catalyzes the degradation of heme. This membrane-bound enzyme cleaves the heme ring at the alpha-methene bridge to produce bilverdin (which is metabolized further by bilirubin reductase to form bilirubin), iron and the putative neurotransmitter, carbon monoxide. There are three isoforms of hem oxygenase; the inducible HO-1, which is active at high concentrations of heme and at times of physiological stress, the constitutively active HO-2 and the non-catalytic HO-3, which is thought to function as an oxygen sensor. Hem oxygenase is localized to microsomes and the endoplasmic reticulum, and the enzyme is found at very high concentrations in splenocytes due to their function in the degradation of senescent erythrocytes.