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Heme oxygenase information


heme oxygenase
Heme oxygenase I, homodimer, Human
Identifiers
EC no.1.14.99.3
CAS no.9059-22-7
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins
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
Identifiers
SymbolHeme_oxygenase
PfamPF01126
Pfam clanCL0230
InterProIPR016053
PROSITEPDOC00512
SCOP21qq8 / SCOPe / SUPFAM
Membranome532
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

Heme oxygenase, or haem oxygenase, (HMOX, commonly abbreviated as HO) is an enzyme that catalyzes the degradation of heme to produce biliverdin, ferrous iron, and carbon monoxide.[1]

There are many heme degrading enzymes in nature. In general, only aerobic heme degrading enzymes are referred to as HMOX-like enzymes whereas anaerobic enzymes are typically not affiliated with the HMOX family.

  1. ^ Ryter SW, Alam J, Choi AM (April 2006). "Heme oxygenase-1/carbon monoxide: from basic science to therapeutic applications". Physiological Reviews. 86 (2): 583–650. doi:10.1152/physrev.00011.2005. PMID 16601269.

and 27 Related for: Heme oxygenase information

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Heme oxygenase

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Heme oxygenase, or haem oxygenase, (HMOX, commonly abbreviated as HO) is an enzyme that catalyzes the degradation of heme to produce biliverdin, ferrous...

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Heme

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erythrocytes from the circulation. In the first step, heme is converted to biliverdin by the enzyme heme oxygenase (HO). NADPH is used as the reducing agent, molecular...

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HMOX1

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HMOX1 (heme oxygenase 1 gene) is a human gene that encodes for the enzyme heme oxygenase 1 (EC 1.14.99.3). Heme oxygenase (abbreviated HMOX or HO) mediates...

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HMOX2

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Heme oxygenase 2 is an enzyme that in humans is encoded by the HMOX2 gene. Heme oxygenase, an essential enzyme in heme catabolism, cleaves heme to form...

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Aminolevulinic acid

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first compound in the porphyrin synthesis pathway, the pathway that leads to heme in mammals, as well as chlorophyll in plants. 5ALA is used in photodynamic...

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Hemoglobin

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Retrieved 2008-10-12. Kikuchi, G.; Yoshida, T.; Noguchi, M. (2005). "Heme oxygenase and heme degradation". Biochemical and Biophysical Research Communications...

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Oxygenase

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microbial P450 monooxygenase research: peroxo-heme intermediates--the central bus station in heme oxygenase catalysis". Biochem. Biophys. Res. Commun. 338...

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Bilirubin

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mostly produced by the destruction of erythrocytes. Heme is metabolized into biliverdin (via heme oxygenase) and then into bilirubin (via biliverdin reductase)...

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Carboxyhemoglobin

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pathways. The most extensively studied pathway is the metabolism of heme by heme oxygenase which occurs throughout the body with significant activity in the...

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Protoporphyrin IX

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gamma (c15), and delta (c20). In the context of heme, metabolic biotransformation by heme oxygenase results in the selective opening of the alpha-methine...

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NFE2L2

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genes encoding cytoprotective proteins. NRF2 induces the expression of heme oxygenase 1 in vitro leading to an increase in phase II enzymes. NRF2 also inhibits...

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Cytochrome P450 reductase

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electron transfer from NADPH to cytochrome P450 and other heme proteins including heme oxygenase in the endoplasmic reticulum of the eukaryotic cell. Human...

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Hemopexin

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extracellular heme can lead to the deactivation of Bach1 repression which leads to the transcriptional activation of antioxidant heme oxygenase-1 gene. Hemoglobin...

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Carbon monoxide

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pathways, the best understood of which is the catabolic action of heme oxygenase on the heme derived from hemoproteins such as hemoglobin. Following the first...

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Zinc protoporphyrin

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investigated for cancer therapies. ZnPP is a competitive inhibitor of heme oxygenase. Heme oxygenase is a cytoprotective enzyme that copes with oxidative stress...

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Jaundice

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a sign indicating the presence of underlying diseases involving abnormal heme metabolism, liver dysfunction, or biliary-tract obstruction. The prevalence...

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Clavulanic acid

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N2-(2-carboxyethyl)-L-arginine (CEA) synthase. Clavaminate synthase is a non-heme oxygenase dependent on iron and α-keto-glutarate and is encoded by orf5 of the...

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Hemin

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the "X factor" required for the growth of Haemophilus influenzae. Heme oxygenase Heme arginate Acute intermittent porphyria Hematin Hemozoin Carbon monoxide-releasing...

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Vasodilation

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improves angiotensin II-induced vascular dysfunction via induction of heme oxygenase-1". Hypertension. 55 (4): 897–904. doi:10.1161/HYPERTENSIONAHA.109.149542...

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Hormesis

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majority of endogenous carbon monoxide is produced by heme oxygenase; the loss of heme oxygenase and subsequent loss of carbon monoxide signaling has catastrophic...

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Peripheral chemoreceptors

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channels also changes throughout the lifetime. Some studies propose that heme-oxygenase 2 is the transducer; however, since its deletion in mice does not affect...

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Hemolytic jaundice

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red blood cells are then degraded to release heme, which will be converted by microsomal heme oxygenase to iron, carbon monoxide and biliverdin, and are...

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Decarbonylation

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released in the degradation (catabolism) of heme by the action of O2, NADPH and the enzyme heme oxygenase: Heme   b + 3 O 2 + 3 2 NADPH + 3 2 H + ⟶ biliverdin...

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Immune privilege

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regulatory T-cells producing "tolerant molecules". These molecules including heme oxygenase 1 (HO-1), leukaemia inhibitory factor (LIF), transforming growth factor...

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Human iron metabolism

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to heme, it is instead transported across the apical membrane by heme carrier protein 1 (HCP1). Heme is then catabolized by microsomal heme oxygenase into...

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Tin mesoporphyrin

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consists of a group of competitive inhibitors of heme oxygenase, a rate-limiting enzyme in the heme catabolic pathway. Tin mesoporphyrin is one of the...

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BACH1

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oxidative stress in the cardiovascular system: focusing on the Bach1/heme oxygenase-1 pathway". Current Pharmaceutical Biotechnology. 7 (2): 87–93. doi:10...

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