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Details on Person Heme oxygenases (HMOXs) cleaves the heme ring at the alpha-m...
| Class:Id | Summation:189394 |
|---|---|
| _displayName | Heme oxygenases (HMOXs) cleaves the heme ring at the alpha-m... |
| _timestamp | 2020-11-09 11:04:14 |
| created | [InstanceEdit:189383] Jassal, Bijay, 2006-11-20 |
| literatureReference | [LiteratureReference:189399] Reduced stress defense in heme oxygenase 1-deficient cells [LiteratureReference:9706822] Oligomerization is crucial for the stability and function of heme oxygenase-1 in the endoplasmic reticulum |
| modified | [InstanceEdit:9706820] Stephan, Ralf, 2020-11-09 [InstanceEdit:9706829] Stephan, Ralf, 2020-11-09 |
| text | 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. |
| (summation) | [Reaction:189398] HMOX1 dimer, HMOX2 cleave heme [Homo sapiens] |
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No pathways have been reviewed or authored by Heme oxygenases (HMOXs) cleaves the heme ring at the alpha-m... (189394)
