1.14.14.18: heme oxygenase (biliverdin-producing)
This is an abbreviated version!
For detailed information about heme oxygenase (biliverdin-producing), go to the full flat file.
Word Map on EC 1.14.14.18
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1.14.14.18
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monoxide
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cytoprotective
-
endothelial
-
necrosis
-
dismutase
-
protoporphyrin
-
erythroid
-
2-related
-
tnf
-
bilirubin
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artery
-
malondialdehyde
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lipopolysaccharide
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catalase
-
hemin
-
neuroprotective
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ischemia
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gsh
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lps
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sod
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anti-oxidant
-
mapks
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sirna
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caspase-3
-
quinone
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pulmonary
-
reperfusion
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lps-induced
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hypoxia
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cyclooxygenase-2
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cox-2
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ferritin
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erk
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nf-e2-related
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anti-apoptotic
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cobalt
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myeloperoxidase
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ischemia-reperfusion
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nrf2-mediated
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pro-oxidant
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kelch-like
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nadph:quinone
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factor-2
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lps-stimulated
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2-like
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erythroid-derived
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oxygenases
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delta-aminolevulinic
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sulforaphane
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hyperbilirubinemia
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medicine
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drug development
-
analysis
- 1.14.14.18
- monoxide
-
cytoprotective
- endothelial
- necrosis
- dismutase
- protoporphyrin
-
erythroid
-
2-related
- tnf
- bilirubin
- artery
- malondialdehyde
- lipopolysaccharide
- catalase
- hemin
-
neuroprotective
- ischemia
- gsh
- lps
- sod
-
anti-oxidant
- mapks
- sirna
- caspase-3
- quinone
- pulmonary
-
reperfusion
-
lps-induced
- hypoxia
- cyclooxygenase-2
- cox-2
- ferritin
- erk
-
nf-e2-related
-
anti-apoptotic
- cobalt
- myeloperoxidase
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ischemia-reperfusion
-
nrf2-mediated
-
pro-oxidant
-
kelch-like
-
nadph:quinone
-
factor-2
-
lps-stimulated
-
2-like
-
erythroid-derived
- oxygenases
-
delta-aminolevulinic
- sulforaphane
- hyperbilirubinemia
- medicine
- drug development
- analysis
Reaction
Synonyms
biliverdin-producing heme oxygenase, ChuS, ChuZ, EC 1.14.99.3, haem oxygenase, heme oxygenase, heme oxygenase 1, heme oxygenase 2, heme oxygenase-1, heme oxygenase-2, HemO, Hmox1, Hmox1a, Hmox1b, Hmox2, Hmox2a, Hmox2b, HmuO, Hmx1, HO, HO-1, HO-2, Ho1, Ho2, Ho3, HO4, HSP32, HugZ, HY1, inducible heme oxygenase-1, More, MsHO1, ORP33 proteins, oxygenase, heme (decyclizing), pbsA1, PigA, proteins, specific or class, ORP33 (oxygen-regulated protein 33,000-mol.-wt.), Syn HO-1, Syn HO-2
ECTree
1.14.14.18 heme oxygenase (biliverdin-producing)Advanced search results
results (
results (Substrates Products
Substrates Products on EC 1.14.14.18 - heme oxygenase (biliverdin-producing)
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
15-phenylheme + electron donor + O2
10-phenylbiliverdin IXalpha + Fe2+ + CO + oxidized eletron donor + H2O
-
-
-
?
5-phenylheme + electron donor + O2
biliverdin IXalpha + Fe2+ + CO + oxidized eletron donor + H2O + benzoic acid
-
-
-
?
alpha-meso-formylmesoheme + NADPH
? + NADP+
-
exclusively oxidized at a non-formyl substituted meso-carbon
-
?
alpha-meso-hydroxyhemin IX + reduced acceptor + O2
verdoheme IXalpha + CO + acceptor + H2O
-
-
-
-
?
alpha-meso-oxyprotoheme IX + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
r
beta-meso-hydroxyhemin IX + reduced acceptor + O2
verdoheme IXbeta + CO + acceptor + H2O
-
-
-
-
?
Co-heme + NADPH + H+ + O2
biliverdin Ixalpha + Co2+ + CO + NAD+ + H2O
-
-
-
-
r
delta-meso-hydroxyhemin IX + reduced acceptor + O2
verdoheme IXdelta + CO + acceptor + H2O
-
-
-
-
?
Fe-heme + [reduced NADPH-hemoprotein reductase] + O2
biliverdin Ixalpha + Fe2+ + CO + NAD+ + H2O
-
-
-
-
r
gamma-meso-hydroxyhemin IX + reduced acceptor + O2
verdoheme IXgamma + CO + acceptor + H2O
-
-
-
-
?
hematoheme + NADPH + H+ + O2
hematobiliverdin Fe2+ + CO + NAD+ + H2O
-
-
-
-
r
heme + 2 NADH + 2 H+ + 2 O2
biliverdin + Fe2+ + CO + 2 NAD+ + H2O
-
NADH-dependent heme degradation system may have a biological role in regulating the concentration of respiratory hemoproteins and the disposition of the aberrant forms of the mitochondrial hemoproteins
-
?
heme + ferredoxin + O2
biliverdin IXalpha + Fe2+ + CO + A + H2O
-
HY1, HO3, and HO4
-
-
?
heme + NADPH + H+ + O2
biliverdin IXdelta + biliverdin IXalpha + Fe2+ + CO + NADP+ + H2O
-
mutant R183E, yields about 20% of product biliverdin IXdelta
-
?
heme + [reduced NADPH-hemoprotein reductase] + O2
biliverdin + Fe2+ + CO + [oxidized NADPH-hemoprotein reductase] + H2O
hemin + reduced acceptor + O2
alpha-meso-hydroxyhemin IX + CO + acceptor + H2O
-
-
-
-
?
protoheme + reduced acceptor + O2 + Fe2+
biliverdin-IX-alpha + CO + Fe3+ + acceptor + H2O
-
-
-
-
?
protoheme + [reduced cytochrome P450 reductase] + O2
biliverdin + Fe2+ + CO + [oxidized cytochrome P450 reductase] + H2O
-
-
-
?
protoheme + [reduced NADPH-hemoprotein reductase] + H+ + O2
biliverdin-IX-alpha + CO + Fe2+ + [oxidized NADPH-hemoprotein reductase] + H2O
protoheme + [reduced NADPH-hemoprotein reductase] + O2
biliverdin + Fe2+ + CO + [oxidized NADPH-hemoprotein reductase] + H2O
protoheme + [reduced NADPH-hemoprotein reductase] + O2
biliverdin IXbeta + biliverdin IXdelta + Fe2+ + CO + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
gamma-CH-Fe(cor) + 3 AH2 + 3 O2
?
-
the regioisomeric iron corrole is an artificial, not-natural substrate, the enzymatic cleavage happens selectively at the unexpected bipyrrolic position and yields a biomimetic biliverdin-like product. The enzymatic corrole ring opening is selective for this corrole regioisomer and for plant-type heme oxygenase, mechanism, overview
-
-
?
gamma-CH-Fe(cor) + 3 AH2 + 3 O2
?
-
the regioisomeric iron corrole is an artificial, not-natural substrate, the enzymatic cleavage happens selectively at the unexpected bipyrrolic position and yields a biomimetic biliverdin-like product. The enzymatic corrole ring opening is selective for this corrole regioisomer and for plant-type heme oxygenase, mechanism, overview
-
-
?
heme + 2 NADPH + 2 H+ + 2 O2
biliverdin + Fe2+ + CO + 2 NADP+ + H2O
-
involved in heme metabolism
-
?
heme + 2 NADPH + 2 H+ + 2 O2
biliverdin + Fe2+ + CO + 2 NADP+ + H2O
-
involved in heme metabolism
-
?
heme + 2 NADPH + 2 H+ + 2 O2
biliverdin + Fe2+ + CO + 2 NADP+ + H2O
-
-
-
?
heme + 2 NADPH + 2 H+ + 2 O2
biliverdin + Fe2+ + CO + 2 NADP+ + H2O
-
involved in heme metabolism
-
?
heme + 2 NADPH + 2 H+ + 2 O2
biliverdin + Fe2+ + CO + 2 NADP+ + H2O
-
involved in heme metabolism
-
?
heme + 2 NADPH + 2 H+ + 2 O2
biliverdin + Fe2+ + CO + 2 NADP+ + H2O
-
-
-
-
?
heme + 2 NADPH + 2 H+ + 2 O2
biliverdin + Fe2+ + CO + 2 NADP+ + H2O
-
involved in heme metabolism
-
?
heme + 2 NADPH + 2 H+ + 2 O2
biliverdin + Fe2+ + CO + 2 NADP+ + H2O
-
involved in heme metabolism
-
?
heme + 2 NADPH + 2 H+ + 2 O2
biliverdin + Fe2+ + CO + 2 NADP+ + H2O
-
involved in heme metabolism
-
?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
-
-
-
?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
-
requires three oxidative reaction steps, via alpha-meso-hydroxy-heme and verdoheme, detailed overview
-
-
?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
reaction intermediate verdoheme and the verdoheme-enzyme complex are gradually degraded in the presence of O2
-
-
?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
-
-
-
?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
-
requires three oxidative reaction steps, via alpha-meso-hydroxy-heme and verdoheme, detailed overview
-
-
?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
reaction intermediate verdoheme and the verdoheme-enzyme complex are gradually degraded in the presence of O2
-
-
?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
-
-
-
?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
requires three oxidative reaction steps, via alpha-meso-hydroxy-heme and verdoheme, detailed overview
-
-
?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
reaction intermediate verdoheme and the verdoheme-enzyme complex are gradually degraded in the presence of O2
-
-
?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
-
-
-
?
heme + 3 AH2 + 3 O2
biliverdin IXalpha + Fe2+ + CO + 3 A + 3 H2O
-
-
-
?
heme + 3 AH2 + 3 O2
biliverdin IXalpha + Fe2+ + CO + 3 A + 3 H2O
-
-
-
-
?
heme + 3 reduced ascorbate + 3 O2
biliverdin + Fe2+ + CO + 3 oxidized ascorbate + 3 H2O
-
-
-
-
?
heme + 3 reduced ascorbate + 3 O2
biliverdin + Fe2+ + CO + 3 oxidized ascorbate + 3 H2O
-
-
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
HO-1 is a critical cell defence enzyme against oxidative stress, HO-1 participates in the protective effect afforded by neuronal nicotinic acetylcholine receptors, nAChR, activation, which activates the neuroprotective signaling cascade, overview
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
induction of HO-1 leads to a reduction of superoxide and increases levels of spermine-NoNoate, HO-1 is involved in artery vascular relaxation, overview
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
-
induction of HO-1 via the ERK-Nrf2-ARE signaling pathway is involved in protecting cells from oxidative stress, overview
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
activation of the enzyme leads to induction of the ABC transporter ABCG2, but not of ABCB6
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
biliverdin is involved in hemin degradation
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
CO plays a role in cGMP production, p38 mitogen-activated protein kinase activation, and nuclear factor-kB activation, as part of the heme oxygenase-1/carbon monoxide, HO-1/CO, system, overview, correlation of HO-1-mediated cytoprotection with a decrease in intracellular free iron amounts. Biliverdin is a third generated heme catabolite by HO-1 and is converted to bilirubin by the catalytic reaction of biliverdin reductase. Both compounds are reducing species and hence may play a role in the protective response to vascular injury by oxidative stress
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
exogenous CO activates Nrf2 through the phosphorylation of protein kinase R-like endoplasmic reticulum kinase, resulting in HO-1 expression, mechanism, overview, CO renders endothelial cells resistant to ER stress not only by downregulating C/EBP homologous protein expression via p38 mitogen-activated protein kinase activation but also by upregulating Nrf2-dependent HO-1 expression via PERK activation
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
first step in the heme degradation pathway
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
-
heat shock factor 1, HSF1, is directly involved in the transcriptional regulation of ho-1 mediated by the enzyme's cadmium-responsive element, mechanism, overview
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
heme oxygenase-1 is regulated by the Nrf2/anti-oxidant response element, ARE, pathway, which plays an important role in regulating cellular anti-oxidants
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
HO-1 exhibits cytoprotective function, enzyme induction, e.g. by dehydrocostus lactone, causes the nuclear accumulation of the nuclear factor E2-related factor 2, Nrf2, and increases the promoter activity of antioxidant response element, ARE, overview
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
HO-1 induction in vivo inhibits cytokine production in synovial tissue, while HO-1 inhibition restores it, overview
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
HO-1 is a cell-protective anti-oxidant enzyme, which is sensitively induced by oxidative stress and regulated by oxidized-1-palmitoyl-2-arachidonoyl-sn-glycerol-3-phosphocholine, i.e. Ox-PAPC, and Nrf2, overview
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
HO-1 is a key enzyme in the cellular response to tissue injury and oxidative stress. HO-1 enzymatic activity results in the formation of the cytoprotective metabolites CO and biliverdin
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
HO-1 is the chief regulatory enzyme in the oxidative degradation of heme to biliverdin. HO-1 receives the electrons necessary for catalysis from the flavoprotein NADPH cytochrome P450 reductase, CPR, releasing free iron and carbon monoxide
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
HO-1 participates in the degradation of heme, the enzyme is involved in tumor development
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
HO-1 shows vasculoprotective and anti-inflammatory activity, it is ptionally regulated by peroxisome proliferator-activated receptors PPARalpha and PPARgamma in vascular cells, inhibition of HO-1 enzymatic activity reverses PPAR ligand-mediated inhibition of cell proliferation and expression of cyclooxygenase-2 in vascular smooth muscle cells, overview
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
HO-1 transcriptional regulation system, overview
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
in aortic smooth muscle cells, induction of HO-1 confers vascular protection against cellular proliferation mainly via its up-regulation of the cyclin-dependent kinase inhibitor p21WAF1/CIP1 that is involved in negative regulation of cellular proliferation, overview
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
inhibition or selective knockdown of HO-1 has anti-inflammatory effects via bilirubin, overview
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
the enzyme catalyzes the first and rate-limiting step in the oxidative heme breakdown, physiological role of isozyme HO-1 and its reaction products, detailed overview
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
the enzyme catalyzes the first and rate-limiting step in the oxidative heme breakdown, physiological role of isozyme HO-2 and its reaction products, detailed overview
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
proper orientation of heme in HO-2 is required for the regioselective oxidation of the alpha-mesocarbon. This is accomplished by interactions within the heme binding pocket, which is made up of two helices. The iron coordinating residue, His45, resides on the proximal helix. The distal helix contains highly conserved glycine residues that allow the helix to flex and interact with the bound heme. Tyr154, Lys199, and Arg203 orient the heme through direct interactions with the heme propionates, overview
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
the C-terminal 23 amino acids are essential for maximal catalytic activity
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
endogenous HO-1 shows anti-apoptotic activity, and is overexpressed in various cancer diseases and might contribute to cancer progression
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
heme oxygenase-1 upregulation significantly inhibits TNF-alpha and Hmgb1 releasing and attenuates lipopolysaccharide-induced acute lung injury in mice, overview
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
-
HO is a microsomal enzyme and catalyzes the oxidation of the alpha-meso-carbon bridge of heme moieties resulting in the generation of ferrous iron, carbon monoxide and biliverdin. HO-1 is inducible and plays a main role in the cellular oxidant/antioxidant balance, whereas HO-2 is constitutive and involved in the physiologicalmetabolism of heme
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
HO-1 catalyzes the rate-limiting step of heme degradation and plays an important anti-inflammatory role via its enzymatic products carbon monoxide and biliverdin
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
HO-1 gene is a glia-expressing wound-responsive gene, HO-1 gene expression associated with traumatic brain injury involving the toll-like receptor 2, overview
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
HO-1 is an antioxidant and cytoprotective enzyme. Methoxychalcones, especially 5-methoxychalcone, 3,4,5-trimethoxychalcone, and 3,4,5,3',4',5'-hexamethoxychalcone, induce the enzyme expression and activity in macrophages without causing cytotoxicity, they also cause anti-inflamatory affects, overview
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
HO-1 is an inducible enzyme that catalyzes the rate-limiting step in the degradation of heme to biliverdin, CO and iron
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
-
HO-1 is the rate-limiting enzyme in heme degradation
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
HO-1 participates in the degradation of heme, the enzyme is involved in tumor development
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
HO-1 shows anti-inflammatory effect, inhibition of HO-1 or scavenging of CO significantly reverses the inhibition of LPS-stimulated nitrite accumulation by tanshinone IIA, overview
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
HO-1 shows anti-inflammatory properties
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
statin-induced heme oxygenase-1 increases NF-kappaB activation and oxygen radical production in cultured neuronal cells exposed to lipopolysaccharide, overview
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
the enzyme catalyzes the first and rate-limiting step in the oxidative heme breakdown, physiological role of isozyme HO-1 and its reaction products, detailed overview
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
the enzyme catalyzes the first and rate-limiting step in the oxidative heme breakdown, physiological role of isozyme HO-2 and its reaction products, detailed overview
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
the enzyme has anti-inflammatory activity and is involved in mediation of curcumin's inhibitory effect on inducible NO synthase expression and NO production. Treatment with HO inhibitor abolishes the inhibitory effect of curcumin on lipopolysaccharide-induced NF-kappaB activation, overview
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
the enzyme shows anti-inflammatory activity, HO-1 expression is induced via the ERK1/2 activation pathway
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
endogenous HO-1 shows anti-apoptotic activity, and is overexpressed in various cancer diseases and might contribute to cancer progression
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
HO-1 shows anti-inflammatory properties
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
HO-1 gene is a glia-expressing wound-responsive gene, HO-1 gene expression associated with traumatic brain injury involving the toll-like receptor 2, overview
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
-
685973, 686073, 686565, 686599, 686882, 687570, 688156, 688160, 688672, 688701, 690140, 690143, 690161
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
heme oxygenase is the rate-limiting enzyme in heme degradation to biliverdin, heme oxygenase-1 catalyzes the degradation of heme and forms antioxidant bile pigments as well as the signaling molecule carbon monoxide, HO-1 is inducible in response to a variety of chemical and physical stress conditions to function as a cytoprotective molecule. Catalytic inactive heme oxygenase-1 deletion mutant protein regulates its own expression in oxidative stress in a positive feedback manner, feed-forward autoregulation of HO-1 in oxidative stress, overview, HO-1 protein also plays a role in regulating cadmium chloride-mediated HO-1 gene induction
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
HO-1 acts as anti-oxidant and protects cells against injury, it regulates neutrophil O2- production and protects the intestine from damage following EtOH and burn injury, overview
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
HO-1 catalyzes the rate-limiting step of heme degradation and plays an important anti-inflammatory role via its enzymatic products carbon monoxide and biliverdin
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
HO-1 is a heat shock protein, and it provides endogenous anti-oxidant and anti-inflammatory moieties which can modulate colonic inflammation
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
HO-1 is the rate-limiting enzyme in heme degradation
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
in vascular smooth muscle cells, induction of HO-1 confers vascular protection against cellular proliferation mainly via its up-regulation of the cyclin-dependent kinase inhibitor p21WAF1/CIP1 that is involved in negative regulation of cellular proliferation, overview
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
statin-induced heme oxygenase-1 increases NF-kappaB activation and oxygen radical production in cultured neuronal cells exposed to lipopolysaccharide, overview
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
the enzyme plays a protective role against hypoxic injury, and in the vicious cycle of low-flow priapism
-
-
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
the gene encoding HO-1 is a Nrf2-regulated gene. NF-E2 related factor 2 activation and heme oxygenase-1 induction by tert-butylhydroquinone protect against deltamethrin-mediated oxidative stress in PC12 cells, e.g. by H2O2 and 6-hydroxydopamine
-
-
?
heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized electron donor + H2O
-
-
-
-
?
heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized electron donor + H2O
-
-
-
-
?
heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized electron donor + H2O
-
-
-
?
heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized electron donor + H2O
-
-
-
-
?
heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized electron donor + H2O
-
-
-
?
heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized electron donor + H2O
-
-
-
-
?
heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized electron donor + H2O
-
-
-
-
?
heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized electron donor + H2O
-
-
-
?
heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
NADH can replace NADPH at concentrations higher than 5 mM in vitro, NADH is unlikely to be an electron donor in vivo
-
-
?
heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
electron donor NADH
-
-
?
heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
iron-protoporphyrin IX is the most active substrate, lower activity with: iron-mesoporphyrin IX, iron-deuteroheme IX, iron-coproheme I, alpha and beta chain of hemoglobin, poor substrates: oxyhemoglobin, carboxyhemoglobin, myoglobin
-
-
?
heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
alpha-meso-oxyprotoheme is an intermediate of heme degradation that is converted stereospecifically into biliverdin IXa via verdoheme IXa
-
-
?
heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
NADH-dependent heme-degradation activity, 16% of NADH activity with 0.5 mM NADPH
-
-
?
heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
enzyme catalyzes oxidative cleavage of both heme b and heme c
-
-
?
heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
porphyrins without chelated iron and metalloporphyrins other than iron porphyrins are not oxidized
-
-
?
heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
cytochrome c and myoglobin are not oxidized
-
-
?
heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
electron donor NADPH
-
-
?
heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
-
-
-
?
heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
electron donor ascorbic acid
-
?
heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
electron donor NADPH, reductase: human or E. coli NADPH-cytochrome P450 reductase or putidaredoxin/putidaredoxin reductase
-
?
heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
algal heme oxygenase requires a second reductant in addition to reduced pyridine nucleotide
-
?
heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
iron-protoporphyrin IX is the most active substrate, lower activity with: iron-mesoporphyrin IX, iron-deuteroheme IX, iron-coproheme I, alpha and beta chain of hemoglobin, poor substrates: oxyhemoglobin, carboxyhemoglobin, myoglobin
-
-
?
heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
porphyrins without chelated iron and metalloporphyrins other than iron porphyrins are not oxidized
-
-
?
heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
electron donor NADPH
-
?
heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
-
-
-
?
heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
-
-
?
heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
iron-protoporphyrin IX is the most active substrate, lower activity with: iron-mesoporphyrin IX, iron-deuteroheme IX, iron-coproheme I, alpha and beta chain of hemoglobin, poor substrates: oxyhemoglobin, carboxyhemoglobin, myoglobin
-
-
?
heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
porphyrins without chelated iron and metalloporphyrins other than iron porphyrins are not oxidized
-
-
?
heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
-
-
-
?
heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
-
-
-
?
heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
iron-protoporphyrin IX is the most active substrate, lower activity with: iron-mesoporphyrin IX, iron-deuteroheme IX, iron-coproheme I, alpha and beta chain of hemoglobin, poor substrates: oxyhemoglobin, carboxyhemoglobin, myoglobin
-
-
?
heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
porphyrins without chelated iron and metalloporphyrins other than iron porphyrins are not oxidized
-
-
?
heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
-
-
?
heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
-
-
-
?
heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
-
-
?
heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
-
-
-
?
heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
-
-
?
heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
overview, substrate specificity
-
-
?
heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
electron donor NADH
-
-
?
heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
iron-protoporphyrin IX is the most active substrate, lower activity with: iron-mesoporphyrin IX, iron-deuteroheme IX, iron-coproheme I, alpha and beta chain of hemoglobin, poor substrates: oxyhemoglobin, carboxyhemoglobin, myoglobin
-
-
?
heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
Ni, Mn, and Sn protoporphyrin IX is not oxidized
-
-
?
heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
oxidation of Co-heme
-
-
?
heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
synthetic hemins XIII and III and iron porphyrin are better substrates than the natural substrate hemin IX, 83 and 86% of hemin IX activity with mesohemin IX and hematohemin IX respectively
-
-
?
heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
enzyme oxidizes protoheme, hematoheme, hematoheme dimethyl ester, dicysteinyl hematoheme, and heme undecapeptide, conversion of hematoheme to hematobilirubin requires the presence of: NADPH, NADPH-cytochrome c reductase, biliverdin reductase and O2
-
-
?
heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
testis heme oxygenase 2 oxidizes Fe-protopophyrin, ferric hematoporphyrin acetate and ferric hematoporphyrin
-
-
?
heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
enzyme catalyzes oxidative cleavage of both heme b and heme c
-
-
?
heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
porphyrins without chelated iron and metalloporphyrins other than iron porphyrins are not oxidized
-
-
?
heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
intact cytochrome c is not oxidized
-
-
?
heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
NADPH is more effective than NADH
-
-
?
heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
electron donor NADPH
-
?
heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
electron donor NADPH
-
-
?
heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
iron-protoporphyrin IX is the most active substrate, lower activity with: iron-mesoporphyrin IX, iron-deuteroheme IX, iron-coproheme I, alpha and beta chain of hemoglobin, poor substrates: oxyhemoglobin, carboxyhemoglobin, myoglobin
-
-
?
heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
porphyrins without chelated iron and metalloporphyrins other than iron porphyrins are not oxidized
-
-
?
heme + NADPH + H+ + O2
biliverdin IXalpha + Fe2+ + CO + NADP+ + H2O
-
wild-type, selective production of biliverdin IXalpha
-
?
heme + [reduced NADPH-hemoprotein reductase] + O2
biliverdin + Fe2+ + CO + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
heme + [reduced NADPH-hemoprotein reductase] + O2
biliverdin + Fe2+ + CO + [oxidized NADPH-hemoprotein reductase] + H2O
Leptospira interrogans serovar Icterohaemorrhagiae serovar Lai 56601
-
-
-
-
?
protoheme + [reduced NADPH-hemoprotein reductase] + H+ + O2
biliverdin-IX-alpha + CO + Fe2+ + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
protoheme + [reduced NADPH-hemoprotein reductase] + H+ + O2
biliverdin-IX-alpha + CO + Fe2+ + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
protoheme + [reduced NADPH-hemoprotein reductase] + H+ + O2
biliverdin-IX-alpha + CO + Fe2+ + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
protoheme + [reduced NADPH-hemoprotein reductase] + O2
biliverdin + Fe2+ + CO + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
protoheme + [reduced NADPH-hemoprotein reductase] + O2
biliverdin + Fe2+ + CO + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
protoheme + [reduced NADPH-hemoprotein reductase] + O2
biliverdin + Fe2+ + CO + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
protoheme + [reduced NADPH-hemoprotein reductase] + O2
biliverdin + Fe2+ + CO + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
additional information
?
-
screening for heme proteins with heme oxygenase activity after de novo synthesis of the heme proteins on a membrane-coupled template, overview
-
-
?
additional information
?
-
-
screening for heme proteins with heme oxygenase activity after de novo synthesis of the heme proteins on a membrane-coupled template, overview
-
-
?
additional information
?
-
-
The first HO reaction step is the regiospecific hydroxylation of the porphyrin alpha-meso-carbon atom, the second is a rapid, spontaneous autooxidation of the reactive alpha-meso-hydroxyheme in which the HO enzyme does not play a critical role. The third reaction step is a major rate-determining step of HO catalysis to regulate the enzyme activity. HO catalysis is unique in that all three O2 activations are performed by the substrate itself, analysis of structural and biochemical properties of HO catalysis, especially its first and third oxygenation steps, overview. FeOOH verdoheme is the key intermediate of the ring-opening reaction, mechanism, overview. Critical functioning of the FeOOH species in HO heme self-oxidation and catalytic importance of the distal hydrogenbonding network in its unique O2 activation
-
-
?
additional information
?
-
-
structure-function relationship and analysis, overview
-
-
?
additional information
?
-
capsaicin induces heme oxygenase-1 expression in Hep-G2 cells via activation of PI3K-Nrf2 signaling, and capsaicin protects against SIN-1-induced cytotoxicity, which is abolished by HO-1 inhibition
-
-
?
additional information
?
-
expression of Hepatitis C virus core protein sensitizes hepatocytes to toxic injury and inhibits the induction of HO-1 in response to stress, overview
-
-
?
additional information
?
-
-
expression of Hepatitis C virus core protein sensitizes hepatocytes to toxic injury and inhibits the induction of HO-1 in response to stress, overview
-
-
?
additional information
?
-
heme oxygenase-1 inhibits breast cancer invasion via suppressing the expression of matrix metalloproteinase-9, overview
-
-
?
additional information
?
-
-
heme oxygenase-1 inhibits breast cancer invasion via suppressing the expression of matrix metalloproteinase-9, overview
-
-
?
additional information
?
-
heme oxygenase-1/CO pathway is a key modulator in NO-mediated antiapoptosis and anti-inflammation, mechanisms, overview, mechanisms for the HO-1-mediated inhibition of NO production, activation of the PI3K/Akt pathway, overview
-
-
?
additional information
?
-
HO-1 gene regulation system, dynamic roles of transcriptional repressor BACH1 and transcription factor NRF2 in the transcription of the heme oxygenase-1 gene, overview
-
-
?
additional information
?
-
HO-1 is involved in the function of bax inhibitor-1, BI-1, an anti-apoptotic protein that is located in endoplasmic reticulum membranes and protects cells from endoplasmic reticulum stress-induced apoptosis. For BI-1 associated function, HO-1 expression is induced by nuclear factor erythroid 2-related factor 2, overview
-
-
?
additional information
?
-
the enzyme has anti-inflammatory function in the vascular system via production of antioxidants bilirubin and biliverdin as well as CO, the enzyme contributes to cardiovascular health
-
-
?
additional information
?
-
-
the enzyme has anti-inflammatory function in the vascular system via production of antioxidants bilirubin and biliverdin as well as CO, the enzyme contributes to cardiovascular health
-
-
?
additional information
?
-
the enzyme is involved in cancer cell response to photodynamic therapy, overview
-
-
?
additional information
?
-
-
the enzyme is involved in cancer cell response to photodynamic therapy, overview
-
-
?
additional information
?
-
-
ho-1 forms complexes with proteins from heavy metal-treated HeLa cells
-
-
?
additional information
?
-
-
a pattern of substrate methyl contact shifts that places the lone iron pi-spin in the dxz orbital, rather than the dyz orbital found in the cyanide complex. Low-spin, (dxy)2(dyz,dxz)3, ground state in both azide and cyanide complexes. Switch from singly occupied dyz for the cyanide to dxz for the azide complex of HO is consistent with the orbital hole determined by the azide pi-plane in the latter complex, which is ca. 90° in-plane rotated from that of the imidazole pi-plane
-
-
?
additional information
?
-
-
ability of uncoupled HO-1 to produce large quantities of H2O2, H2O2 generation is much more efficient with the full-length form of HO-1 than with the soluble form
-
-
?
additional information
?
-
-
The first HO reaction step is the regiospecific hydroxylation of the porphyrin alpha-meso-carbon atom, the second is a rapid, spontaneous autooxidation of the reactive alpha-meso-hydroxyheme in which the HO enzyme does not play a critical role. The third reaction step is a major rate-determining step of HO catalysis to regulate the enzyme activity. HO catalysis is unique in that all three O2 activations are performed by the substrate itself, analysis of structural and biochemical properties of HO catalysis, especially its first and third oxygenation steps, overview. FeOOH verdoheme is the key intermediate of the ring-opening reaction, mechanism, overview. Critical functioning of the FeOOH species in HO heme self-oxidation and catalytic importance of the distal hydrogen bonding network in its unique O2 activation
-
-
?
additional information
?
-
-
structure-function relationship and analysis, overview
-
-
?
additional information
?
-
-
hemoglobin neurotoxicity is attenuated by inhibitors of the protein kinase CK2 and protein kinase C independent of heme oxygenase activity
-
-
?
additional information
?
-
inhibition of heme oxygenase 1 expression by small interfering RNA decreases orthotopic tumor growth in livers of mice. Downmodulation of HO-1 by siRNA resulted in increased cellular damage and apoptosis, reduced proliferation, reduced growth of orthotopic hepatocellular carcinoma and reduced angiogenesis, mechanism, overview
-
-
?
additional information
?
-
-
inhibition of heme oxygenase 1 expression by small interfering RNA decreases orthotopic tumor growth in livers of mice. Downmodulation of HO-1 by siRNA resulted in increased cellular damage and apoptosis, reduced proliferation, reduced growth of orthotopic hepatocellular carcinoma and reduced angiogenesis, mechanism, overview
-
-
?
additional information
?
-
LPS-induced maturation of dendritic cells is dependent on STAT3 phosphorylation and independent of HO-1 activity, overview
-
-
?
additional information
?
-
-
LPS-induced maturation of dendritic cells is dependent on STAT3 phosphorylation and independent of HO-1 activity, overview
-
-
?
additional information
?
-
overexpression of HO-1 in B16F10 cells confers resistance to cisplatin treatment, overview
-
-
?
additional information
?
-
-
overexpression of HO-1 in B16F10 cells confers resistance to cisplatin treatment, overview
-
-
?
additional information
?
-
PMA-dependent activation of HO-1 is mediated via a nonclassical NF-kappaB pathway that is independent of IKK2 activity
-
-
?
additional information
?
-
the anti-inflammatory activity of Phellinus linteus is mediated through the PKCdelta/Nrf2/ARE signaling to up-regulation of heme oxygenase-1
-
-
?
additional information
?
-
inhibition of heme oxygenase 1 expression by small interfering RNA decreases orthotopic tumor growth in livers of mice. Downmodulation of HO-1 by siRNA resulted in increased cellular damage and apoptosis, reduced proliferation, reduced growth of orthotopic hepatocellular carcinoma and reduced angiogenesis, mechanism, overview
-
-
?
additional information
?
-
LPS-induced maturation of dendritic cells is dependent on STAT3 phosphorylation and independent of HO-1 activity, overview
-
-
?
additional information
?
-
-
involved in the control of wound healing
-
-
?
additional information
?
-
-
reaction proceeds via three steps, first step is alpha-regioselective hydroxylation of hemin, second degradation of meso-hydroxyhemin to verdoheme and third degradation of verdoheme to biliverdin, which again is stereoselective for verdoheme IXalpha. In the second step, enzyme would convert all four isomers of meso-hydroxyhemin
-
-
?
additional information
?
-
butylated hydroxyanisole stimulates heme oxygenase-1 gene expression and inhibits neointima formation in rat arteries involving Nrf2 activation, overview
-
-
?
additional information
?
-
expression and activity of heme oxygenase-1 is elevated in artificially induced low-flow priapism in rat penile tissues, overview
-
-
?
additional information
?
-
HO-1 and its byproduct biliverdin play major roles in the pathophysiological cascade leading to renal I/R injury
-
-
?
additional information
?
-
-
HO-1 is involved in host defense reactions against various stresses, HO-1 modulates immunocyte activation and functions and suppresses mast cell degranulation, overview
-
-
?
additional information
?
-
HO-1 is involved in host defense reactions against various stresses, HO-1 modulates immunocyte activation and functions and suppresses mast cell degranulation, overview
-
-
?
additional information
?
-
HO-1 protein delivery mediates activation of various transcription factors, nuclear localization of HO-1 has a signalling role, effect of nuclear localization of HO-1oncell viability, overview
-
-
?
additional information
?
-
HO-1 regulation, HO-1 autoregulation, and HO-1 regulatory functions, activation of MAPK pathways is not required in HO-1 self-regulation, overview
-
-
?
additional information
?
-
inhibition of heme oxygenase-1 protects against tissue injury in carbon tetrachloride exposed livers, SnPP-IX-mediated HO-1 inhibition markedly aggravates intrahepatic leukocyte-endothelial cell interaction with an almost 2fold increase of the number of adherent leukocytes when compared with solely CCl4-exposed livers, overview
-
-
?
additional information
?
-
-
NO derived from LPS-induced nitric oxide synthase, NOS, entails an increase in HO activity and this activity, in turn, is involved in the consequent inhibition of NOS, overview
-
-
?
additional information
?
-
PMA-dependent activation of HO-1 is mediated via a nonclassical NF-kappaB pathway that is independent of IKK2 activity
-
-
?
additional information
?
-
-
the enzyme activity is positively correlated with nitric oxide and cGMP levels in cavernous tissue, overview
-
-
?
additional information
?
-
The first HO reaction step is the regiospecific hydroxylation of the porphyrin alpha-meso-carbon atom, the second is a rapid, spontaneous autooxidation of the reactive alpha-meso-hydroxyheme in which the HO enzyme does not play a critical role. The third reaction step is a major rate-determining step of HO catalysis to regulate the enzyme activity. HO catalysis is unique in that all three O2 activations are performed by the substrate itself, analysis of structural and biochemical properties of HO catalysis, especially its first and third oxygenation steps, overview. FeOOH verdoheme is the key intermediate of the ring-opening reaction, mecjanism, overview. Critical functioning of the FeOOH species in HO heme self-oxidation and catalytic importance of the distal hydrogenbonding network in its unique O2 activation
-
-
?
additional information
?
-
-
heme oxygenase activity in rat spleen and brain microsomal fractions is determined by the quantitation of CO formed from the degradation of methemalbumin, i.e. heme complexed with albumin
-
-
?
additional information
?
-
structure-function relationship and analysis, overview
-
-
?
additional information
?
-
-
heme oxygenase activity in rat spleen and brain microsomal fractions is determined by the quantitation of CO formed from the degradation of methemalbumin, i.e. heme complexed with albumin
-
-
?
