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an oxidoreductase that catalyzes the incorporation of molecular oxygen

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2014/10/03 19:03:26」(JST)

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An oxygenase is any enzyme that oxidizes a substrate by transferring the oxygen from molecular oxygen O₂ (as in air) to it. The oxygenases form a class of oxidoreductases; their EC number is EC 1.13 or EC 1.14.

Oxygenases were discovered in 1955 simultaneously by two groups, Osamu Hayaishi from Japan^[1]^[2]^[3] and Howard S. Mason from the US.^[4]^[5] Hayaishi was awarded the 1986 Wolf Prize in Medicine "for the discovery of the oxygenase enzymes and elucidation of their structure and biological importance."^[6]

There are two types of oxygenases:

Monooxygenases, or mixed function oxidase, transfer one oxygen atom to the substrate, and reduce the other oxygen atom to water.
Dioxygenases, or oxygen transferases, incorporate both atoms of molecular oxygen (O₂) into the product(s) of the reaction.^[7]

Among the most important monooxygenases are the cytochrome P450 oxidases, responsible for breaking down numerous chemicals in the body.

References

^ Hayaishi et al. (1955) Mechanism of the pyrocatechase reaction, J. Am. Chem. Soc. 77 (1955) 5450-5451
^ Sligar SG, Makris TM, Denisov IG (2005). "Thirty years of microbial P450 monooxygenase research: peroxo-heme intermediates--the central bus station in heme oxygenase catalysis". Biochem. Biophys. Res. Commun. 338 (1): 346–54. doi:10.1016/j.bbrc.2005.08.094. PMID 16139790.
^ Hayaishi O (2005). "An odyssey with oxygen". Biochem. Biophys. Res. Commun. 338 (1): 2–6. doi:10.1016/j.bbrc.2005.09.019. PMID 16185652.
^ Mason HS, Fowlks WK, and Peterson E. (1955) Oxygen transfer and electron transport by the phenolase complex. J. Am. Chem. Soc.; 77(10) pp 2914 - 2915
^ Waterman MR (2005). "Professor Howard Mason and oxygen activation". Biochem. Biophys. Res. Commun. 338 (1): 7–11. doi:10.1016/j.bbrc.2005.08.120. PMID 16153596.
^ "The Medicine Prize Committee unanimously decided that the Wolf Prize in Medicine for 1986 be awarded to Osamu Hayaishi". Wolf Foundation. Retrieved May 12, 2014.
^ Bugg TDH (2003). "Dioxygenase enzymes: catalytic mechanisms and chemical models". Tetrahedron 59 (36): 7075–7101. doi:10.1016/S0040-4020(03)00944-X.

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English Journal

Targeting of heme oxygenase-1 as a novel immune regulator of neuroblastoma.

Fest S1,2, Soldati R1,3, Christiansen NM2, Zenclussen ML3, Kilz J1,3, Berger E1,3, Starke S2, Lode HN4, Engel C5, Zenclussen AC3, Christiansen H2.
International journal of cancer. Journal international du cancer.Int J Cancer.2016 Apr 15;138(8):2030-42. doi: 10.1002/ijc.29933. Epub 2015 Dec 12.
Heme oxygenase (HO)-1 catalyzes the degradation of cytotoxic heme into biliverdin and blocks antitumor immune responses, thus protecting cancer against host defense. Whether this scenario also applies to neuroblastoma (NB), the most common extracranial solid childhood tumor, is not known. Here, we d
PMID 26595750

Effect of heme oxygenase-1 gene promoter polymorphism on cancer risk by histological subtype: A prospective study in arseniasis-endemic areas in Taiwan.

Wu MM1,2, Lee CH3, Hsu LI4, Cheng WF2, Lee TC5, Wang YH6,7, Chiou HY1, Chen CJ4.
International journal of cancer. Journal international du cancer.Int J Cancer.2016 Apr 15;138(8):1875-86. doi: 10.1002/ijc.29926. Epub 2015 Nov 28.
Heme oxygenase (HO)-1 is upregulated by many stressful stimuli, including arsenic. A GT-repeat ((GT)n) polymorphism in the HO-1 gene promoter inversely modulates the levels of HO-1 induction. Previous HO-1 (GT)n polymorphism studies in relation to cancer risk have shown disparate results. We prospec
PMID 26566708

Heme oxygenase-1 alleviates cigarette smoke-induced restenosis after vascular angioplasty by attenuating inflammation in rat model.

Ni L1, Wang Z1, Yang G1, Li T1, Liu X1, Liu C2.
Toxicology letters.Toxicol Lett.2016 Mar 14;245:99-105. doi: 10.1016/j.toxlet.2016.01.017. Epub 2016 Jan 22.
Cigarette smoke is not only a profound independent risk factor of atherosclerosis, but also aggravates restenosis after vascular angioplasty. Heme oxygenase-1 (HO-1) is an endogenous antioxidant and cytoprotective enzyme. In this study, we investigated whether HO-1 upregulating by hemin, a potent HO
PMID 26809138

Japanese Journal

Ferrous Ferric Chloride Downregulates the Inflammatory Response to Rhodococcus aurantiacus Infection in Mice

Yimin,Tao Huirong,Kohanawa Masashi,Zhao Songji,Kuge Yuji,Tamaki Nagara
Biological and Pharmaceutical Bulletin 35(12), 2214-2223, 2012-12
… aurantiacus also induced the expression of heme oxygenase-1 mRNA in the cells from F1 mice. …
NAID 120005108194

Protective action of nipradilol mediated through S-nitrosylation of Keap1 and HO-1 induction in retinal ganglion cells

Koriyama Yoshiki,Kamiya Marie,Takadera Tsuneo,Arai Kunizo,Sugitani Kayo,Ogai Kazuhiro,Kato Satoru
Neurochemistry International 61(7), 1242-1253, 2012-12
… We also demonstrated that Nip induced the expression of the NO-dependent antioxidant enzyme, heme oxygenase-1 (HO-1). …
NAID 120004966623