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）』「2014/06/26 11:09:39」(JST)
[Wiki en表示]
| 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 |
|
| 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, iron, and carbon monoxide.[1]
Contents
- 1 Reaction
- 2 Isoforms
- 3 Roles in Physiology
- 4 References
- 5 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[2]
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.
Isoforms
There are three known isoforms of heme oxygenase.
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
Response to Oxidative Stress Heme Oxygenase expression is increased in the presence of increase oxidative stress and in animal models increasing this expression seems to protective. [3]
Vascular Tone Carbon monoxide released from Heme Oxygenase reactions can influence vascular tone independently or influence the function of Nitric Oxide Synthathase. [4]
Malaria protection from Sickle-Cell Anemia 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.
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.
- ^ 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.
- ^ 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
- ^ 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
|
Oxidoreductases: dioxygenases, including steroid hydroxylases (EC 1.14)
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|
| 1.14.11: 2-oxoglutarate |
- Prolyl hydroxylase
- Lysyl hydroxylase
|
|
| 1.14.13: NADH or NADPH |
- Flavin-containing monooxygenase
- Nitric oxide synthase
- Cholesterol 7 alpha-hydroxylase
- Methane monooxygenase
- 3A4
- Lanosterol 14 alpha-demethylase
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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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- B
- enzm
- 1.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 10
- 11
- 13
- 14
- 15-18
- 2.1
- 3.1
- 4.1
- 5.1
- 6.1-3
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|
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- Metabolism: amino acid metabolism
- porphyrin/heme enzymes
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| Porphyrin biosynthesis |
| early mitochondrial: |
- Aminolevulinic acid synthase
- Porphobilinogen synthase
|
|
| cytosolic: |
- Porphobilinogen deaminase
- Uroporphyrinogen III synthase
- Uroporphyrinogen III decarboxylase
- Coproporphyrinogen III oxidase
|
|
| late mitochondrial: |
- 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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mt, k, c/g/r/p/y/i, f/h/s/l/o/e, a/u, n, m
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k, cgrp/y/i, f/h/s/l/o/e, au, n, m, epon
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m (A16/C10), i (k, c/g/r/p/y/i, f/h/s/o/e, a/u, n, m)
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|
|
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cell/phys (coag, heme, immu, gran), csfs
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rbmg/mogr/tumr/hist, sysi/epon, btst
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drug (B1/2/3+5+6), btst, trns
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UpToDate Contents
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English Journal
- Heme oxygenase-1 (HO-1) mediated respiratory responses to hypoxia in the goldfish, Carassius auratus.
- Tzaneva V1, Perry SF2.
- Respiratory physiology & neurobiology.Respir Physiol Neurobiol.2014 Aug 1;199:1-8. doi: 10.1016/j.resp.2014.04.006. Epub 2014 Apr 26.
- In this study we investigated the role of heme oxygenase-1 (HO-1) in modulating the hypoxic and hyperoxic ventilatory responses of goldfish (Carassius auratus) acclimated to 7 and 25°C. HO-1 was present in the neuroepithelial cells (NECs; putative branchial O2 chemoreceptors) of fish acclimated to
- PMID 24780551
- Heme oxygenase suppresses markers of heart failure and ameliorates cardiomyopathy in L-NAME-induced hypertension.
- Ndisang JF1, Chibbar R2, Lane N3.
- European journal of pharmacology.Eur J Pharmacol.2014 Jul 5;734:23-34. doi: 10.1016/j.ejphar.2014.03.026. Epub 2014 Apr 13.
- Heart failure and related cardiac complications remains a great health challenge. We investigated the effects of upregulating heme-oxygenase (HO) on myocardial histo-pathological lesions, proinflammatory cytokines/chemokines, oxidative mediators and important markers of heart failure such as osteopo
- PMID 24726875
Japanese Journal
- 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
- Isolation, identification, and biological evaluation of Nrf2-ARE activator from the leaves of green perilla (Perilla frutescens var. crispa f. viridis)
- Izumi Yasuhiko,Matsumura Atsuko,Wakita Seiko,Akagi Ken-Ichi,Fukuda Hiroyuki,Kume Toshiaki,Irie Kazuhiro,Takada-Takatori Yuki,Sugimoto Hachiro,Hashimoto Tadashi,Akaike Akinori
- Free radical biology & medicine 53(4), 669-679, 2012-06-27
- … DDC induced the expression of antioxidant enzymes, such as γ-glutamylcysteine synthetase (γ-GCS), NAD(P)H: quinone oxidoreductase-1 (NQO1), and heme oxygenase-1. …
- NAID 120004462161
Related Links
- ヘムオキシゲナーゼ（HO） ヘムオキシゲナーゼ（heme oxygenase：HO）は、ヘム（heme）を、ビリベルジン（biriverdin）と、一酸化炭素（CO）と、遊離鉄（Fe）に分解する酵素。 HOは、ヘムのポルフィリン環を開裂し、酸素分子を ...
- Buy Heme Oxygenase antibodies from Santa Cruz. Heme Oxygenase products include 7 monoclonal antibodies, 10 polyclonal antibodies, and si/shRNA gene silencers. ... Introducing HOVERcruz , a unique system for rapid ...
Related Pictures
★リンクテーブル★
[★]
- 英
- heme oxygenase
- 関
- [[]]
[★]
ヘムオキシゲナーゼ1、ヘムオキシゲナーゼ-1
[★]
ヘム