HMOX2

Heme oxygenase (decycling) 2
血红素加氧酶2（脱环）
PDB rendering based on 2q32.
有效结构
PDB 直系同源检索：PDBe, RCSB
PDB查询代码列表

2Q32, 2QPP, 2RGZ

标识
代号 HMOX2; HO-2
扩展标识 遗传学：141251 鼠基因：109373 同源基因：1611 ChEMBL: 2546 GeneCards: HMOX2 Gene
EC編號 1.14.99.3
基因本体论描述
分子功能 · heme oxygenase (decyclizing) activity

· protein binding

· metal ion binding
细胞成分 · endoplasmic reticulum membrane
· plasma membrane
生物过程 · response to hypoxia

· porphyrin-containing compound metabolic process
· heme oxidation
· cellular iron ion homeostasis
· response to oxidative stress
· heme catabolic process
· small molecule metabolic process

· transmembrane transport
Sources: Amigo / QuickGO
RNA表达模式
更多表达数据
直系同源体
物种 人类 小鼠
Entrez 3163 15369
Ensembl ENSG00000103415 ENSMUSG00000004070
UniProt P30519 O70252
mRNA序列 NM_001127204 NM_001136066
蛋白序列 NP_001120676 NP_001129538
基因位置 Chr 16:
4.52 – 4.56 Mb		 Chr 16:
4.73 – 4.77 Mb
PubMed查询 [1] [2]
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血红素加氧酶2（英語：Heme oxygenase 2）是一种由人类基因 HMOX2 所编码的酶[1][2]。

功能

血红素加氧酶是血红素代谢过程中的必需酶，将血红素转化为胆绿素，随后被胆绿素还原酶（英语：biliverdin reductase）转化为胆红素和一氧化碳（在机体中可能起神经递质作用）。血红素加氧酶的活性受其底物血红素和其它物质介导。血红素加氧酶存在两种同工酶，一种是诱导型的血红素加氧酶1——HMOX1，另一种就是组成型的血红素加氧酶2——HMOX2[2]。

参考文献

  1. ^ McCoubrey WK Jr, Ewing JF, Maines MD. Human heme oxygenase-2: characterization and expression of a full-length cDNA and evidence suggesting that the two HO-2 transcripts may differ by choice of polyadenylation signal. Arch Biochem Biophys. Jun 1992, 295 (1): 13–20. PMID 1575508. doi:10.1016/0003-9861(92)90481-B. 
  2. ^ 2.0 2.1 Entrez Gene: HMOX2 heme oxygenase (decycling) 2. 

延伸阅读

  • Bianchetti CM, Yi L, Ragsdale SW, Phillips GN Jr. Comparison of Apo- and Heme-bound Crystal Structures of a Truncated Human Heme Oxygenase-2. J Biol Chem. 2007, 282 (52): 37624–31. PMC 2896506 可免费查阅. PMID 17965015. doi:10.1074/jbc.M707396200. 
  • Wang J, Zhuang H, Doré S. Heme oxygenase 2 is neuroprotective against intracerebral hemorrhage.. Neurobiol Dis. 2006, 22 (3): 473–6. PMID 16459095. doi:10.1016/j.nbd.2005.12.009. 
  • Wang J, Doré S. Heme oxygenase 2 deficiency increases brain swelling and inflammation after intracerebral hemorrhage.. Neuroscience. 2008, 155 (4): 1133–41. PMID 18674596. doi:10.1016/j.neuroscience.2008.07.004. 
  • Barañano DE, Snyder SH. Neural roles for heme oxygenase: Contrasts to nitric oxide synthase. Proc. Natl. Acad. Sci. U.S.A. 2001, 98 (20): 10996–1002. PMC 58673 可免费查阅. PMID 11572959. doi:10.1073/pnas.191351298. 
  • Doré S. Decreased activity of the antioxidant heme oxygenase enzyme: implications in ischemia and in Alzheimer's disease. Free Radic. Biol. Med. 2002, 32 (12): 1276–82. PMID 12057765. doi:10.1016/S0891-5849(02)00805-5. 
  • Kemp PJ. Hemeoxygenase-2 as an O2 sensor in K+ channel-dependent chemotransduction. Biochem. Biophys. Res. Commun. 2005, 338 (1): 648–52. PMID 16137652. doi:10.1016/j.bbrc.2005.08.110. 
  • Ishikawa K; Takeuchi N; Takahashi S; et al. Heme oxygenase-2. Properties of the heme complex of the purified tryptic fragment of recombinant human heme oxygenase-2. J. Biol. Chem. 1995, 270 (11): 6345–50. PMID 7890772. doi:10.1074/jbc.270.11.6345. 
  • Kutty RK; Kutty G; Rodriguez IR; et al. Chromosomal localization of the human heme oxygenase genes: heme oxygenase-1 (HMOX1) maps to chromosome 22q12 and heme oxygenase-2 (HMOX2) maps to chromosome 16p13.3. Genomics. 1994, 20 (3): 513–6. PMID 8034330. doi:10.1006/geno.1994.1213. 
  • Maruyama K, Sugano S. Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. Gene. 1994, 138 (1–2): 171–4. PMID 8125298. doi:10.1016/0378-1119(94)90802-8. 
  • Takahashi K; Hara E; Suzuki H; et al. Expression of heme oxygenase isozyme mRNAs in the human brain and induction of heme oxygenase-1 by nitric oxide donors. J. Neurochem. 1996, 67 (2): 482–9. PMID 8764571. doi:10.1046/j.1471-4159.1996.67020482.x. 
  • Saito-Ohara F, Ikeuchi T, Matsumoto M, Kurata S. Assignment of the mouse heme oxygenase genes: heme oxygenase-1 (Hmox1) to chromosome 10 band C1 and heme oxygenase-2 (Hmox2) to chromosome 16 band B1. Cytogenet. Cell Genet. 1997, 77 (3–4): 180–1. PMID 9284910. doi:10.1159/000134570. 
  • Suzuki Y; Yoshitomo-Nakagawa K; Maruyama K; et al. Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. Gene. 1997, 200 (1–2): 149–56. PMID 9373149. doi:10.1016/S0378-1119(97)00411-3. 
  • Yoshiki N, Kubota T, Aso T. Expression and localization of heme oxygenase in human placental villi. Biochem. Biophys. Res. Commun. 2000, 276 (3): 1136–42. PMID 11027601. doi:10.1006/bbrc.2000.3551. 
  • Hanselmann C, Mauch C, Werner S. Haem oxygenase-1: a novel player in cutaneous wound repair and psoriasis?. Biochem. J. 2001, 353 (Pt 3): 459–66. PMC 1221590 可免费查阅. PMID 11171041. doi:10.1042/0264-6021:3530459. 
  • Strausberg RL; Feingold EA; Grouse LH; et al. Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc. Natl. Acad. Sci. U.S.A. 2003, 99 (26): 16899–903. PMC 139241 可免费查阅. PMID 12477932. doi:10.1073/pnas.242603899. 
  • Appleton SD; Marks GS; Nakatsu K; et al. Effects of hypoxia on heme oxygenase expression in human chorionic villi explants and immortalized trophoblast cells. Am. J. Physiol. Heart Circ. Physiol. 2003, 284 (3): H853–8. PMID 12578814. doi:10.1152/ajpheart.00655.2002. 
  • Galey D; Becker K; Haughey N; et al. Differential transcriptional regulation by human immunodeficiency virus type 1 and gp120 in human astrocytes. J. Neurovirol. 2003, 9 (3): 358–71. PMID 12775419. doi:10.1080/13550280390201119. 
  • Zenclussen AC; Lim E; Knoeller S; et al. Heme oxygenases in pregnancy II: HO-2 is downregulated in human pathologic pregnancies. Am. J. Reprod. Immunol. 2004, 50 (1): 66–76. PMID 14506930. doi:10.1034/j.1600-0897.2003.00047.x. 
  • Boehning D; Moon C; Sharma S; et al. Carbon monoxide neurotransmission activated by CK2 phosphorylation of heme oxygenase-2. Neuron. 2003, 40 (1): 129–37. PMID 14527438. doi:10.1016/S0896-6273(03)00596-8. 
  • Appleton SD; Lash GE; Marks GS; et al. Effect of glucose and oxygen deprivation on heme oxygenase expression in human chorionic villi explants and immortalized trophoblast cells. Am. J. Physiol. Regul. Integr. Comp. Physiol. 2004, 285 (6): R1453–60. PMID 14615405. doi:10.1152/ajpregu.00234.2003. 
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双加氧酶（英语：Oxidoreductase）类，包括类固醇羟化酶（英语：steroid hydroxylases）（EC 1.14）
1.14.11（英语：List of EC numbers (EC 1)#EC 1.14.11 With 2-oxoglutarate as one donor.2C and incorporation of one atom each of oxygen into both donors）：以α-酮戊二酸为供体
1.14.11：以NADH或NADPH为供体
  • 苯1,2-双加氧酶
  • 5-吡哆酸双加氧酶
  • 邻苯二甲酸1,2-双加氧酶
  • 苯甲酸1,2-双加氧酶
  • 甲苯双加氧酶
  • 萘1,2-双加氧酶
  • 对苯二酸1,2-双加氧酶
  • 一氧化氮双加氧酶
  • 脱镁叶绿酸a加氧酶
  • 苯甲酰辅酶A双加氧酶
  • 咔唑1,9a-双加氧酶
1.14.13（英语：List of EC numbers (EC 1)#EC 1.14.13 With NADH or NADPH as one donor.2C and incorporation of one atom of oxygen）：以NADH或NADPH为供体
  • 含黄素单加氧酶（英语：Flavin-containing monooxygenase）（FMO1（英语：FMO1）、FMO2（英语：FMO2）、FMO3（英语：FMO3）、FMO4（英语：FMO4）、FMO5（英语：FMP5））
  • 一氧化氮合酶（NOS1（英语：NOS1）、NOS2（英语：NOS2）、NOS3（英语：NOS3））
  • 胆固醇7α-羟化酶
  • 甲烷单加氧酶
  • CYP3A4
  • 羊毛固醇14α-脱甲基酶
1.14.14：以还原型黄素黄素或黄素蛋白为供体
1.14.15：以还原型铁硫蛋白为供体
1.14.16：以还原型蝶啶为受体
1.14.17：以还原型抗坏血酸为受体
1.14.18
1.14.19
  • 硬脂酰辅酶A脱饱和酶1
1.14.20：以α-酮戊二酸为受体
1.14.99：杂项
EC 1.1/2/3/4/5/6/7/8/9/10/11/12/13/14/15/16/17/18/19/20/21/22 · 2.1/2/3/4/5/6/7(2.7.10/11-12)/8/9 · 3.1/2/3/4(3.4.21/22/23/24)/5/6/7/8/9/10/11/12/13 · 4.1/2/3/4/5/6 · 5.1/2/3/4/5/99 · 6.1-3（英语：Template:Ligases CO CS and CN）/4/5-6