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Heme oxygenase 1 |
PDB rendering based on 1n3u.
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Available structures |
PDB |
Ortholog search: PDBe, RCSB |
List of PDB id codes |
1N3U, 1N45, 1NI6, 1OYK, 1OYL, 1OZE, 1OZL, 1OZR, 1OZW, 1S13, 1S8C, 1T5P, 1TWN, 1TWR, 1XJZ, 1XK0, 1XK1, 1XK2, 1XK3, 3CZY, 3HOK, 3K4F, 3TGM
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Symbols |
HMOX1 ; HMOX1D; HO-1; HSP32; bK286B10 |
External IDs |
OMIM: 141250 MGI: 96163 HomoloGene: 31075 ChEMBL: 2823 GeneCards: HMOX1 Gene |
EC number |
1.14.99.3 |
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More reference expression data |
Species |
Human |
Mouse |
Entrez |
3162 |
15368 |
Ensembl |
ENSG00000100292 |
ENSMUSG00000005413 |
UniProt |
P09601 |
P14901 |
RefSeq (mRNA) |
NM_002133 |
NM_010442 |
RefSeq (protein) |
NP_002124 |
NP_034572 |
Location (UCSC) |
Chr 22:
35.38 – 35.39 Mb |
Chr 8:
75.09 – 75.1 Mb |
PubMed search |
[1] |
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HMOX1 (heme oxygenase (decycling) 1) is a human gene that encodes for the enzyme heme oxygenase 1 (EC 1.14.99.3). Heme oxygenase is an essential enzyme in heme catabolism, it cleaves heme to form biliverdin.
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.[1]
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
Anti-inflammatory effect
The ability of oxygenase 1 to catabolize free heme and produce carbon monoxide (CO) gives its antiinflammatory properties by up-regulation of IL-10 and IL-1R antagonist expression.[2]
See also
References
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Further reading
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PDB gallery
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1n3u: Crystal structure of human heme oxygenase 1 (HO-1) in complex with its substrate heme, crystal form B
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1n45: X-RAY CRYSTAL STRUCTURE OF HUMAN HEME OXYGENASE-1 (HO-1) IN COMPLEX WITH ITS SUBSTRATE HEME
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1ni6: Comparisons of the Heme-Free and-Bound Crystal Structures of Human Heme Oxygenase-1
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1oyk: Crystal Structures of the Ferric, Ferrous, and Ferrous-NO Forms of the Asp140Ala Mutant of Human Heme Oxygenase-1: Catalytic Implications
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1oyl: Crystal Structures of the Ferric, Ferrous, and Ferrous-NO Forms of the Asp140Ala Mutant of Human Heme Oxygenase-1: Catalytic Implications
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1oze: Crystal Structures of the Ferric, Ferrous, and Ferrous-NO Forms of the Asp140Ala Mutant of Human Heme Oxygenase-1:Catalytic Implications
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1ozl: Crystal Structures of the Ferric, Ferrous, and Ferrous-NO Forms of the Asp140Ala Mutant of Human Heme Oxygenase-1: Catalytic Implications
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1ozr: Crystal Structures of the Ferric, Ferrous and Ferrous-NO Forms of the Asp140Ala Mutant of Human Heme Oxygenase-1: Catalytic Implications
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1ozw: Crystal Structures of the Ferric, Ferrous and Ferrous-NO Forms of the Asp140Ala Mutant of Human Heme Oxygenase-1: Catalytic Implications
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1s13: Human Heme Oxygenase Oxidatition of alpha- and gamma-meso-Phenylhemes
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1s8c: Crystal structure of human heme oxygenase in a complex with biliverdine
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1t5p: Human Heme Oxygenase Oxidation of alpha- and gamma-meso-phenylhemes
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1twn: Crystal structures of ferrous and ferrous-NO forms of verdoheme in a complex with human heme oxygenase-1: catalytic implications for heme cleavage
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1twr: Crystal structures of ferrous and ferrous-NO forms of verdoheme in a complex with human heme oxygenase-1: catalytic implications for heme cleavage
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1xjz: Crystal Structures of the G139A, G139A-NO and G143H Mutants of Human Heme Oxygenase-1
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1xk0: Crystal Structures of the G139A, G139A-NO and G143H Mutants of Human Heme Oxygenase-1
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1xk1: Crystal Structures of the G139A, G139A-NO and G143H Mutants of Human Heme Oxygenase-1
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1xk2: NADPH- and Ascorbate-Supported Heme Oxygenase Reactions are Distinct. Regiospecificity of Heme Cleavage by the R183E Mutant
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1xk3: NADPH- and Ascorbate-Supported Heme Oxygenase Reactions are Distinct. Regiospecificity of Heme Cleavage by the R183E Mutant
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Regulation |
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Classification |
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