Heme Oxygenase 2 (HMOX2) Recombinant Protein

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. Alternative splice variants encoding the same protein have been identified at this locus. [provided by RefSeq, Jul 2008]

HMOX2: 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. Belongs to the heme oxygenase family.

Protein type: Oxidoreductase; EC 1.14.99.3; Cofactor and Vitamin Metabolism - porphyrin and chlorophyll

Chromosomal Location of Human Ortholog: 16p13.3

Cellular Component: endoplasmic reticulum membrane; membrane; plasma membrane

Molecular Function: protein binding; metal ion binding; heme oxygenase (decyclizing) activity

Biological Process: heme catabolic process; cellular iron ion homeostasis; porphyrin metabolic process; heme oxidation; response to hypoxia; transmembrane transport