Heme oxygenase
| Heme oxygenase heme oxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 | |||||||||
| Identifier | |||||||||
| EC number | 1.14.99.3 | ||||||||
| CAS registration number | 9059-22-7 | ||||||||
| Database | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA () | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structure | RCSB PDB PDBe PDBj PDBsum | ||||||||
| Gene オントロジー | AmiGO / EGO | ||||||||
| |||||||||
Heme oxygenase (heme さんそてんかこうそ, Heme oxygenase) is an enzyme catalyzing the resolution of heme. This enzyme produces biliverdin, iron, carbon monoxide [1].
Reaction
Open ring, and generate biliverdin, and, as for the heme oxygenase, heme is connected in globin cutting by the α-methylene bridging of the heme ring; when remain it, generate ベルドグロビン. The biliverdin is converted into bilirubin sequentially by biliverdin reductase.
The reactions are as follows.
- Heme + NADPH + H+ +3 O2 → biliverdin + Fe2+ + CO + NADP+ + H2O[2]
This reaction is possible with all cells virtually. This typical example is the formation of the bruise. The bruise changes to red heme, green biliverdin, yellow bilirubin as cured. Under the normal menstruation condition, the activity of the heme oxygenase is active in spleen most lively and captures an old red blood cell and destroys it.
Three kinds of isomodels of the isomodel heme oxygenase are known.
In heme oxygenase 1(HO-1), an isomodel is derived in response to oxidation stress, hypoxia, heavy metal, stress such as cytokine. Heme oxygenase 2(HO-2) is an isomodel expressed under a homeostatic condition. Both heme oxygenase 1 and 2 exist universally and carry out a catalytic activity.
In third heme oxygenase (HO-3), it is not done catalytic activity, but it is thought that it functions in perception of oxygen.
Footnote
- ^ Kikuchi G, Yoshida T, Noguchi M (December 2005). "Heme oxygenase and heme degradation." Biochem. Biophys. Res. Commun. 338 (1): 558–67. doi: 10.1016/j.bbrc.2005.08.020. PMID 16115609.
- ^ Evans JP, Niemevz F, Buldain G, de Montellano PO (July 2008). "Isoporphyrin intermediate in heme oxygenase catalysis. Oxidation of alpha-meso-phenylheme". J. Biol. Chem. 283 (28): 19530–9. doi: 10.1074/jbc.M709685200. PMC 2443647. It is . PMID 18487208
Allied item
This article is taken from the Japanese Wikipedia Heme oxygenase
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