Biology:HMOX1
 Generic protein structure example |
HMOX1 (heme oxygenase 1 gene) is a human gene that encodes for the enzyme heme oxygenase 1 (EC 1.14.99.3). Heme oxygenase (abbreviated HMOX or HO) mediates the first step of heme catabolism, it cleaves heme to form biliverdin.
The HMOX gene is located on the long (q) arm of chromosome 22 at position 12.3, from base pair 34,101,636 to base pair 34,114,748.
Related conditions
- Heme oxygenase-1 deficiency
Heme oxygenase
Heme oxygenase, an essential enzyme in heme catabolism, cleaves heme to form biliverdin, carbon monoxide, and ferrous iron.[1] The biliverdin is subsequently converted to bilirubin by biliverdin reductase. 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.[2]
See also
References
- ↑ Lehninger's Principles of Biochemistry, 5th Edition. New York: W.H. Freeman and Company. 2008. pp. 876. ISBN 978-0-7167-7108-1. https://archive.org/details/lehningerprincip00lehn_1/page/876.
- ↑ "Entrez Gene: HMOX1 heme oxygenase (decycling) 1". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3162.
Further reading
- "Oxidative stress causes enhanced endothelial cell injury in human heme oxygenase-1 deficiency". J Clin Invest 103 (1): 129–35. 1999. doi:10.1172/JCI4165. PMID 9884342.
- "Distinct role of heme oxygenase-1 in early- and late-stage intracerebral hemorrhage in 12-month-old mice". J Cereb Blood Flow Metab 37 (1): 25–38. 2016. doi:10.1177/0271678X16655814. PMID 27317654.
- "Heme oxygenase-1 exacerbates early brain injury after intracerebral haemorrhage.". Brain 130 (6): 1643–52. 2007. doi:10.1093/brain/awm095. PMID 17525142.
- "Heme oxygenase-1, a protective gene that prevents the rejection of transplanted organs". Immunol. Rev. 184: 275–85. 2002. doi:10.1034/j.1600-065x.2001.1840124.x. PMID 12086318.
- "Heme oxygenase-1: the "emerging molecule" has arrived". Am. J. Respir. Cell Mol. Biol. 27 (1): 8–16. 2002. doi:10.1165/ajrcmb.27.1.4862. PMID 12091240.
- "Protection of grafts by hemoxygenase-1 and its toxic product carbon monoxide". Am. J. Transplant. 1 (4): 313–5. 2002. doi:10.1034/j.1600-6143.2001.10404.x. PMID 12099373.
- Ishikawa K (2003). "Heme oxygenase-1 against vascular insufficiency: roles of atherosclerotic disorders". Curr. Pharm. Des. 9 (30): 2489–97. doi:10.2174/1381612033453767. PMID 14529548.
- "The role of heme oxygenase-1 promoter polymorphisms in human disease". Free Radic. Biol. Med. 37 (8): 1097–104. 2005. doi:10.1016/j.freeradbiomed.2004.07.008. PMID 15451051.
- Ozono R (2006). "New biotechnological methods to reduce oxidative stress in the cardiovascular system: focusing on the Bach1/heme oxygenase-1 pathway". Current Pharmaceutical Biotechnology 7 (2): 87–93. doi:10.2174/138920106776597630. PMID 16724942.
- "Physiology and pathophysiology of heme: implications for kidney disease". J. Am. Soc. Nephrol. 18 (2): 414–20. 2007. doi:10.1681/ASN.2006080894. PMID 17229906.
- "(-)-Epicatechin protects hemorrhagic brain via synergistic Nrf2 pathways". Annals of Clinical and Translational Neurology 1 (4): 258–271. 2014. doi:10.1002/acn3.54. PMID 24741667.
- "Haem oxygenase-1--a culprit in vascular and renal damage?". Nephrol. Dial. Transplant. 22 (6): 1495–9. 2007. doi:10.1093/ndt/gfm093. PMID 17389623.
External links
- Overview of all the structural information available in the PDB for UniProt: P09601 (Heme oxygenase 1) at the PDBe-KB.
PDB gallery | |
|---|---|
|
 |  |
