Aliases for HMOX2 Gene
External Ids for HMOX2 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. Several alternatively spliced transcript variants encoding three different isoforms have been found for this gene. [provided by RefSeq, Oct 2013]
GeneCards Summary for HMOX2 Gene
HMOX2 (Heme Oxygenase 2) is a Protein Coding gene. Diseases associated with HMOX2 include pyloric stenosis and hypertrophic pyloric stenosis. Among its related pathways are Metabolism and Glucose / Energy Metabolism. GO annotations related to this gene include heme oxygenase (decyclizing) activity. An important paralog of this gene is HMOX1.
UniProtKB/Swiss-Prot for HMOX2 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. Heme oxygenase 2 could be implicated in the production of carbon monoxide in brain where it could act as a neurotransmitter
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.