ヘムオキシゲナーゼ1、ヘムオキシゲナーゼ-1
WordNet
- utter `hem or `ahem
- the edge of a piece of cloth; especially the finished edge that has been doubled under and stitched down; "the hem of her dress was stained"; "let down the hem"; "he stitched weights into the curtains hem"; "it seeped along the hem of his jacket"
- the utterance of a sound similar to clearing the throat; intended to get attention, express hesitancy, fill a pause, hide embarrassment, warn a friend, etc. (同)ahem
- fold over and sew together to provide with a hem; "hem my skirt"
- the 5th letter of the Hebrew alphabet
- a complex red organic pigment containing iron and other atoms to which oxygen binds (同)haem, hematin, haemitin, protoheme
- an oxidoreductase that catalyzes the incorporation of molecular oxygen
PrepTutorEJDIC
- (折り返して縫った衣類や布の)へり,縁 / (一般に)へり,縁 / 〈布・着物〉‘の'へりを折り返して縫う;…‘の'縁どりをする
- へん!えへん!(注意・疑い・ちゅうちょ・当惑などを表するための発声) / へん(えへん)と言う,せき払いをする
- 彼は,彼が / 《指す人の性別が分からないか,または分かる必要のない場合に》その人,あの人,自分 / 《he who(that)の形で》《文》…するものはだれでも / (動物の)おす(雄)
- 鬼ごっこ(tag,tick,tig)
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2016/08/01 01:44:51」(JST)
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heme oxygenase |
Identifiers |
EC number |
1.14.99.3 |
CAS number |
9059-22-7 |
Databases |
IntEnz |
IntEnz view |
BRENDA |
BRENDA entry |
ExPASy |
NiceZyme view |
KEGG |
KEGG entry |
MetaCyc |
metabolic pathway |
PRIAM |
profile |
PDB structures |
RCSB PDB PDBe PDBsum |
Gene Ontology |
AmiGO / EGO |
Search |
PMC |
articles |
PubMed |
articles |
NCBI |
proteins |
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Heme oxygenase |
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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Identifiers |
Symbol |
Heme_oxygenase |
Pfam |
PF01126 |
Pfam clan |
CL0230 |
InterPro |
IPR016053 |
PROSITE |
PDOC00512 |
SCOP |
1qq8 |
SUPERFAMILY |
1qq8 |
Available protein structures: |
Pfam |
structures |
PDB |
RCSB PDB; PDBe; PDBj |
PDBsum |
structure summary |
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Heme oxygenase or haem oxygenase (HO) is an enzyme that catalyzes the degradation of heme. This produces biliverdin, ferrous iron, and carbon monoxide.[1][2] There is limited evidence that levels of heme oxygenase are positive predictors of metabolic disease, insulin resistance, and metaflammation.[3]
Contents
- 1 Reaction
- 2 Roles in physiology
- 3 References
- 4 External links
Reaction
Heme oxygenase cleaves the heme ring at the alpha-methene bridge to form either biliverdin or, if the heme is still attached to a globin, verdoglobin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase.
The reaction occurs as follows:
-
- Heme b + 3O2 + 3½NADPH + 3½H+ → biliverdin + Fe2+ + CO + 3½NADP+ + 3H2O[4]
This reaction can occur in virtually every cell; the classic example is the formation of a bruise, which goes through different colors as it gradually heals: red heme to green biliverdin to yellow bilirubin. Under normal physiological conditions, the activity of heme oxygenase is highest in the spleen, where old erythrocytes are sequestrated and destroyed. In terms of molecular mechanisms, the enzyme facilitates the intramolecular hydroxylation of one meso carbon centre in the heme.[5]
Isoforms
Three isoforms of heme oxygenase are known. Heme oxygenase 1 (HO-1) is an inducible isoform in response to stress such as oxidative stress, hypoxia, heavy metals, cytokines, etc. Heme oxygenase 2 (HO-2) is a constitutive isoform that is expressed under homeostatic conditions. Both HO-1 and HO-2 are ubiquitously expressed and catalytically active.
A third heme oxygenase (HO-3) is not catalytically active, but is thought to work in oxygen sensing.
Roles in physiology
Heme oxygenase expression is induced by oxidative stress, and in animal models increasing this expression seems to be protective. Carbon monoxide released from heme oxygenase reactions can influence vascular tone independently or influence the function of nitric oxide synthase. Carbon monoxide released from the reaction of free heme in the bloodstream of someone with the sickle-cell trait is believed to lessen the effects of cerebral malaria.[6]
References
- ^ 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.
- ^ Ryter, Stefan W.; Alam, Jawed; Choi, Augustine M. K. "Heme oxygenase-1/carbon monoxide: from basic science to therapeutic applications" Physiological Reviews (2006), 86(2), 583-650. doi:10.1152/physrev.00011.2005
- ^ Jais, Alexander (2014). "Heme Oxygenase-1 Drives Metaflammation and Insulin Resistance in Mouse and Man". Cell 158 (1): 25–40. Retrieved 10 May 2016.
- ^ 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. PMID 18487208.
- ^ Tadashi Yoshida, Catharina Taiko Migita "Focused Review Mechanism of heme degradation by heme oxygenase" Journal of Inorganic Biochemistry 2000, Volume 82, Issues 1–4, pages 33–41. doi:10.1016/S0162-0134(00)00156-2
- ^ Danielle Morse and Augustine M. K. Choi "Heme Oxygenase-1", American Journal of Respiratory and Critical Care Medicine, Vol. 172, No. 6 (2005), pp. 660-670. doi:10.1164/rccm.200404-465SO
External links
- Heme Oxygenase at the US National Library of Medicine Medical Subject Headings (MeSH)
- EC 1.14.99.3
Enzymes involved in the metabolism of heme and porphyrin
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Porphyrin biosynthesis |
early mitochondrial: |
- Aminolevulinic acid synthase
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cytosolic: |
- Porphobilinogen synthase
- Porphobilinogen deaminase
- Uroporphyrinogen III synthase
- Uroporphyrinogen III decarboxylase
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late mitochondrial: |
- Coproporphyrinogen III oxidase
- Protoporphyrinogen oxidase
- Ferrochelatase
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Heme degradation
to bile |
spleen: |
- Heme oxygenase
- Biliverdin reductase
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liver: |
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Oxidoreductases: dioxygenases, including steroid hydroxylases (EC 1.14)
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1.14.11: 2-oxoglutarate |
- Prolyl hydroxylase
- Lysyl hydroxylase
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1.14.13: NADH or NADPH |
- Flavin-containing monooxygenase
- Nitric oxide synthase
- Cholesterol 7 alpha-hydroxylase
- Methane monooxygenase
- 3A4
- Lanosterol 14 alpha-demethylase
- 24-hydroxycholesterol 7α-hydroxylase
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1.14.14: reduced flavin or flavoprotein |
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1.14.15: reduced iron-sulfur protein |
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1.14.16: reduced pteridine (BH4 dependent) |
- Phenylalanine hydroxylase
- Tyrosine hydroxylase
- Tryptophan hydroxylase
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1.14.17: reduced ascorbate |
- Dopamine beta-hydroxylase
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1.14.18-19: other |
- Tyrosinase
- Stearoyl-CoA desaturase-1
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1.14.99 - miscellaneous |
- Cyclooxygenase
- Heme oxygenase (HMOX1)
- Squalene monooxygenase
- 17A1
- 21A2
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Enzymes
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Activity |
- Active site
- Binding site
- Catalytic triad
- Oxyanion hole
- Enzyme promiscuity
- Catalytically perfect enzyme
- Coenzyme
- Cofactor
- Enzyme catalysis
- Enzyme kinetics
- Lineweaver–Burk plot
- Michaelis–Menten kinetics
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Regulation |
- Allosteric regulation
- Cooperativity
- Enzyme inhibitor
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Classification |
- EC number
- Enzyme superfamily
- Enzyme family
- List of enzymes
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Types |
- EC1 Oxidoreductases(list)
- EC2 Transferases(list)
- EC3 Hydrolases(list)
- EC4 Lyases(list)
- EC5 Isomerases(list)
- EC6 Ligases(list)
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UpToDate Contents
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English Journal
- Styrene-maleic acid-copolymer conjugated zinc protoporphyrin as a candidate drug for tumor-targeted therapy and imaging.
- Fang J1,2, Tsukigawa K1,2, Liao L1,3, Yin H1, Eguchi K2, Maeda H1.
- Journal of drug targeting.J Drug Target.2016 Jun;24(5):399-407. doi: 10.3109/1061186X.2015.1077851. Epub 2015 Aug 24.
- Previous studies indicated the potential of zinc protoporphyrin (ZnPP) as an antitumor agent targeting to the tumor survival factor heme oxygenase-1, and/or for photodynamic therapy (PDT). In this study, to achieve tumor-targeted delivery, styrene-maleic acid-copolymer conjugated ZnPP (SMA-ZnPP) was
- PMID 26302870
- Protective effects of monomethyl fumarate at the inflamed blood-brain barrier.
- Lim JL1, van der Pol SM2, Di Dio F3, van Het Hof B4, Kooij G5, de Vries HE6, van Horssen J7.
- Microvascular research.Microvasc Res.2016 May;105:61-9. doi: 10.1016/j.mvr.2015.12.003. Epub 2015 Dec 8.
- BACKGROUND: Reactive oxygen species play a key role in the pathogenesis of multiple sclerosis as they induce blood-brain barrier disruption and enhance transendothelial leukocyte migration. Thus, therapeutic compounds with antioxidant and anti-inflammatory potential could have clinical value in mult
- PMID 26679389
- 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.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
Japanese Journal
- Protection of Cultured Cortical Neurons by Luteolin against Oxidative Damage through Inhibition of Apoptosis and Induction of Heme Oxygenase-1
- Protective effects of tyrosol against LPS-induced acute lung injury via inhibiting NF-κB and AP-1 activation and activating the HO-1/Nrf2 Pathways
- Albumin-Based Nitric Oxide Traffic System for the Treatment of Intractable Cancers
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- heme oxygenase-1
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[★]
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- heme oxygenase-1
- 関
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