HMOX2

血红素加氧酶2（英语：Heme oxygenase 2）是一种由人类基因 HMOX2 所编码的酶^[1][2]。

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编号	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]
查 论 编

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. 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 . 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 . 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 . 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 . 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.