HMOX2: Difference between revisions

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* {{cite journal | vauthors = Bianchetti CM, Yi L, Ragsdale SW, Phillips GN | title = Comparison of Apo- and Heme-bound Crystal Structures of a Truncated Human Heme Oxygenase-2 | journal = J Biol Chem | volume = 282 | issue = 52 | pages = 37624–31 | year = 2007 | pmid = 17965015 | pmc = 2896506 | doi = 10.1074/jbc.M707396200 }}
* {{cite journal | vauthors = Bianchetti CM, Yi L, Ragsdale SW, Phillips GN | title = Comparison of Apo- and Heme-bound Crystal Structures of a Truncated Human Heme Oxygenase-2 | journal = J Biol Chem | volume = 282 | issue = 52 | pages = 37624–31 | year = 2007 | pmid = 17965015 | pmc = 2896506 | doi = 10.1074/jbc.M707396200 }}
* {{cite journal | vauthors = Wang J, Zhuang H, Doré S | title = Heme oxygenase 2 is neuroprotective against intracerebral hemorrhage. | journal = Neurobiol Dis. | volume = 22 | issue = 3 | pages = 473–6 | year = 2006 | pmid = 16459095 | doi = 10.1016/j.nbd.2005.12.009 }}
* {{cite journal | vauthors = Wang J, Zhuang H, Doré S | title = Heme oxygenase 2 is neuroprotective against intracerebral hemorrhage. | journal = Neurobiol. Dis. | volume = 22 | issue = 3 | pages = 473–6 | year = 2006 | pmid = 16459095 | doi = 10.1016/j.nbd.2005.12.009 }}
* {{cite journal | vauthors = Wang J, Doré S | title = Heme oxygenase 2 deficiency increases brain swelling and inflammation after intracerebral hemorrhage | journal = Neuroscience | volume = 155 | issue = 4 | pages = 1133–41 | year = 2008 | pmid = 18674596 | pmc = 4696610 | doi = 10.1016/j.neuroscience.2008.07.004 }}
* {{cite journal | vauthors = Wang J, Doré S | title = Heme oxygenase 2 deficiency increases brain swelling and inflammation after intracerebral hemorrhage | journal = Neuroscience | volume = 155 | issue = 4 | pages = 1133–41 | year = 2008 | pmid = 18674596 | pmc = 4696610 | doi = 10.1016/j.neuroscience.2008.07.004 }}
* {{cite journal | vauthors = Barañano DE, Snyder SH | title = Neural roles for heme oxygenase: Contrasts to nitric oxide synthase | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 98 | issue = 20 | pages = 10996–1002 | year = 2001 | pmid = 11572959 | pmc = 58673 | doi = 10.1073/pnas.191351298 | bibcode = 2001PNAS...9810996B }}
* {{cite journal | vauthors = Barañano DE, Snyder SH | title = Neural roles for heme oxygenase: Contrasts to nitric oxide synthase | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 98 | issue = 20 | pages = 10996–1002 | year = 2001 | pmid = 11572959 | pmc = 58673 | doi = 10.1073/pnas.191351298 | bibcode = 2001PNAS...9810996B }}

Revision as of 17:19, 8 December 2018

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Heme oxygenase 2 is an enzyme that in humans is encoded by the HMOX2 gene.[1][2]

Function

Heme oxygenase, an essential enzyme in heme catabolism, cleaves heme to form biliverdin, which is subsequently converted to bilirubin by biliverdin reductase, and carbon monoxide, a putative neurotransmitter. Heme oxygenase activity is induced by its substrate heme and by various nonheme substances. Heme oxygenase occurs as 2 isozymes, an inducible heme oxygenase-1 and a constitutive heme oxygenase-2. HMOX1 and HMOX2 (this enzyme) belong to the heme oxygenase family.[2]

References

  1. McCoubrey WK, Ewing JF, Maines MD (Jun 1992). "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. 295 (1): 13–20. doi:10.1016/0003-9861(92)90481-B. PMID 1575508.
  2. 2.0 2.1 "Entrez Gene: HMOX2 heme oxygenase (decycling) 2".

Further reading