HMOX1 dimer, HMOX2 cleave heme

Stable Identifier
R-HSA-189398
Type
Reaction [transition]
Species
Homo sapiens
Compartment
cytosol, endoplasmic reticulum membrane
Synonyms
The heme ring is cleaved by heme oxygenase
ReviewStatus
5/5
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HMOX1 dimer, HMOX2 cleave heme
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Heme oxygenases (HMOXs) cleaves the heme ring at the alpha-methene bridge to form bilverdin. This reaction forms the only endogenous source of carbon monoxide. HMOX1 is inducible and is thought to have an antioxidant role as it is activated in virtually all cell types and by many types of "oxidative stress" (Poss & Tonegawa 1997). HMOX1 forms dimers/oligomers in the endoplasmatic reticulum. This oligomerization is crucial for the stabilization and function of HMOX1 in the ER (Hwang et al. 2009). HMOX2 is non-inducible.
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Catalyst Activity

heme oxygenase (decyclizing) activity of HMOX1 dimer, HMOX2 [endoplasmic reticulum membrane]

Physical Entity
HMOX1 dimer, HMOX2 [endoplasmic reticulum membrane] (Homo sapiens)
Activity
heme oxygenase (decyclizing) activity (GO:0004392)
Orthologous Events
HMOX1 dimer, HMOX2 cleave heme (Bos taurus)
HMOX1 dimer, HMOX2 cleave heme (Canis familiaris)
HMOX1 dimer, HMOX2 cleave heme (Danio rerio)
HMOX1 dimer, HMOX2 cleave heme (Drosophila melanogaster)
HMOX1 dimer, HMOX2 cleave heme (Gallus gallus)
HMOX1 dimer, HMOX2 cleave heme (Mus musculus)
HMOX1 dimer, HMOX2 cleave heme (Rattus norvegicus)
HMOX1 dimer, HMOX2 cleave heme (Sus scrofa)
HMOX1 dimer, HMOX2 cleave heme (Xenopus tropicalis)
Authored
Jassal, B  (2006-11-20)
Reviewed
Somers, J  (2021-01-23)
Sassa, S  (2007-01-24)
Created
Jassal, B  (2006-11-20)
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