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.
Heme oxygenase, an essential enzyme in heme catabolism, cleaves heme to form biliverdin, carbon monoxide, and ferrous iron.[5] 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.[6]
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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
1n45: X-RAY CRYSTAL STRUCTURE OF HUMAN HEME OXYGENASE-1 (HO-1) IN COMPLEX WITH ITS SUBSTRATE HEME
1ni6: Comparisons of the Heme-Free and-Bound Crystal Structures of Human Heme Oxygenase-1
1oyk: Crystal Structures of the Ferric, Ferrous, and Ferrous-NO Forms of the Asp140Ala Mutant of Human Heme Oxygenase-1: Catalytic Implications
1oyl: Crystal Structures of the Ferric, Ferrous, and Ferrous-NO Forms of the Asp140Ala Mutant of Human Heme Oxygenase-1: Catalytic Implications
1oze: Crystal Structures of the Ferric, Ferrous, and Ferrous-NO Forms of the Asp140Ala Mutant of Human Heme Oxygenase-1:Catalytic Implications
1ozl: Crystal Structures of the Ferric, Ferrous, and Ferrous-NO Forms of the Asp140Ala Mutant of Human Heme Oxygenase-1: Catalytic Implications
1ozr: Crystal Structures of the Ferric, Ferrous and Ferrous-NO Forms of the Asp140Ala Mutant of Human Heme Oxygenase-1: Catalytic Implications
1ozw: Crystal Structures of the Ferric, Ferrous and Ferrous-NO Forms of the Asp140Ala Mutant of Human Heme Oxygenase-1: Catalytic Implications
1s13: Human Heme Oxygenase Oxidatition of alpha- and gamma-meso-Phenylhemes
1s8c: Crystal structure of human heme oxygenase in a complex with biliverdine
1t5p: Human Heme Oxygenase Oxidation of alpha- and gamma-meso-phenylhemes
1twn: Crystal structures of ferrous and ferrous-NO forms of verdoheme in a complex with human heme oxygenase-1: catalytic implications for heme cleavage
1twr: Crystal structures of ferrous and ferrous-NO forms of verdoheme in a complex with human heme oxygenase-1: catalytic implications for heme cleavage
1xjz: Crystal Structures of the G139A, G139A-NO and G143H Mutants of Human Heme Oxygenase-1
1xk0: Crystal Structures of the G139A, G139A-NO and G143H Mutants of Human Heme Oxygenase-1
1xk1: Crystal Structures of the G139A, G139A-NO and G143H Mutants of Human Heme Oxygenase-1
1xk2: NADPH- and Ascorbate-Supported Heme Oxygenase Reactions are Distinct. Regiospecificity of Heme Cleavage by the R183E Mutant
1xk3: NADPH- and Ascorbate-Supported Heme Oxygenase Reactions are Distinct. Regiospecificity of Heme Cleavage by the R183E Mutant
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| 1.14.11: 2-oxoglutarate |
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| 1.14.13: NADHorNADPH |
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| 1.14.14: reduced flavinorflavoprotein |
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| 1.14.15: reduced iron–sulfur protein |
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| 1.14.16: reduced pteridine (BH4 dependent) |
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| 1.14.17: reduced ascorbate |
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| 1.14.18-19: other |
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| 1.14.99 - miscellaneous |
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 | This article on a gene on human chromosome 22 is a stub. You can help Wikipedia by expanding it. |
