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Information on EC 1.14.14.18 - heme oxygenase (biliverdin-producing)
for references in articles please use BRENDA:EC1.14.14.18
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EC Tree 1 Oxidoreductases
1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
1.14.14 With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor
1.14.14.18 heme oxygenase (biliverdin-producing)
IUBMB Comments
This mammalian enzyme participates in the degradation of heme. The terminal oxygen atoms that are incorporated into the carbonyl groups of pyrrole rings A and B of biliverdin are derived from two separate oxygen molecules . The third oxygen molecule provides the oxygen atom that converts the α-carbon to CO. The enzyme requires NAD(P)H and EC 1.6.2.4, NADPH—hemoprotein reductase. cf. EC 1.14.15.20, heme oxygenase (biliverdin-producing, ferredoxin).
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
- 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
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nrf2-mediated
-
pro-oxidant
-
kelch-like
-
nadph:quinone
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factor-2
-
lps-stimulated
-
2-like
-
erythroid-derived
- oxygenases
-
delta-aminolevulinic
- sulforaphane
- hyperbilirubinemia
- medicine
- drug development
- analysis
Reaction Schemes
showSynonyms
heme oxygenase-1, heme oxygenase, hmox1, heme oxygenase 1, haem oxygenase, hsp32, heme oxygenase-2, hmox2, heme oxygenase 2, hmox1a, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
abHemO
canonical heme oxygenase
EC 1.14.99.3
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formerly
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haem oxygenase
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heme oxygenase
heme oxygenase 1
heme oxygenase 2
heme oxygenase-1
heme oxygenase-2
Hmox1
HmuO
HO-1
HO-2
Ho1
Ho2
ORP33 proteins
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oxygenase, heme (decyclizing)
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proteins, specific or class, ORP33 (oxygen-regulated protein 33,000-mol.-wt.)
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additional information
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HugZ belongs to a distinct heme-binding protein family with a split-barrel fold
heme oxygenase-1
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heme oxygenase-1
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heme oxygenase-1
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-
heme oxygenase-1
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heme oxygenase-1
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heme oxygenase-1
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HO-1
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HO-1
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HO-1
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HO-1
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HO-1
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HO-1
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 = biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O
protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 = biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O
a ferric hydroperoxide species must be an active intermediate in the first oxygenation step
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protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 = biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O
determination of single turnover rate constants and reaction intermediates for heme oxygenase-1
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protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 = biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O
mechanism
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protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 = biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O
hydroperoxoferri-heme oxygenase-1 is the reactive species directly forming the alpha-meso-hydroxyheme product by attack of the distal OH of the hydroperoxo moiety at the heme alpha-carbon
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protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 = biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O
model of activation mechanism of Fe-OOH
protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 = biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O
electrophilic oxidation mechanism, stereochemical control of the reaction regiospecificity
protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 = biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O
binding of heme stabilizes the solvent H-bonded network in the active site required for proper catalysis
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protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 = biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O
docking model of heme and ferredoxin, indirect electron transfer from an iron-sulfur cluster in ferredoxin to the heme iron
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protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 = biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O
rate-limiting step of reaction is biliverdin release
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protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 = biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O
selective oxygenation at the alpha-meso carbon, model of active site
protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 = biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O
opened conformation of the heme pocket facilitates sequential product release, first iron, then biliverdin, iron triggers slow dissociation of biliverdin
protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 = biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O
model of active site
protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 = biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O
a three-step mechanism, mechanism of the the third step, heme oxygenase enzymatic ring-opening mechanism of verdoheme, a process which maintains iron homeostasis, overview. Reaction mechanism for the FeOOH pathway and the FeHOOH pathway, and complete triplet-state mechanism, overview
protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 = biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O
heme degradation by heme oxygenase proceeds through three successive steps of O2 activation. The first step is formation of alpha-meso-hydroxyheme from heme, second formation of verdoheme from alpha-meso-hydroxyheme, the third step is the ring opening of verdoheme. Only alpha-verdoheme with the O atom in its alpha position, and not beta-, gamma-, or delta-verdoheme, is converted to biliverdin. The third step, like the first, shows regiospecificity, the distal Asp plays an important role in this step, similar to the first. The substrate heme is sandwiched between two helices, termed the proximal and distal helices. Reaction mechanism, overview
protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 = biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O
heme degradation by heme oxygenase proceeds through three successive steps of O2 activation. The first step is formation of alpha-meso-hydroxyheme from heme, second formation of verdoheme from alpha-meso-hydroxyheme, the third step is the ring opening of verdoheme. Only alpha-verdoheme with the O atom in its alpha position, and not beta-, gamma-, or delta-verdoheme, is converted to biliverdin. The third step, like the first, shows regiospecificity, the distal Asp plays an important role in this step, similar to the first. The substrate heme is sandwiched between two helices, termed the proximal and distal helices. Reaction mechanism, overview
protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 = biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O
heme degradation by heme oxygenase proceeds through three successive steps of O2 activation. The first step is formation of alpha-meso-hydroxyheme from heme, second formation of verdoheme from alpha-meso-hydroxyheme, the third step is the ring opening of verdoheme. Only alpha-verdoheme with the O atom in its alpha position, and not beta-, gamma-, or delta-verdoheme, is converted to biliverdin. The third step, like the first, shows regiospecificity, the distal Asp plays an important role in this step, similar to the first. The substrate heme is sandwiched between two helices, termed the proximal and distal helices. Reaction mechanism, overview
protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 = biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O
heme degradation by heme oxygenase proceeds through three successive steps of O2 activation. The first step is formation of alpha-meso-hydroxyheme from from heme, second formation of verdoheme from alpha-meso-hydroxyheme, the third step is the ring opening of alpha-verdoheme to alpha-biliverdin, overview
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protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 = biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
heme degradation I
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SYSTEMATIC NAME
IUBMB Comments
protoheme,NADPH-hemoprotein reductase:oxygen oxidoreductase (alpha-methene-oxidizing, hydroxylating)
This mammalian enzyme participates in the degradation of heme. The terminal oxygen atoms that are incorporated into the carbonyl groups of pyrrole rings A and B of biliverdin are derived from two separate oxygen molecules [4]. The third oxygen molecule provides the oxygen atom that converts the alpha-carbon to CO. The enzyme requires NAD(P)H and EC 1.6.2.4, NADPH---hemoprotein reductase. cf. EC 1.14.15.20, heme oxygenase (biliverdin-producing, ferredoxin).
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CAS REGISTRY NUMBER
COMMENTARY
9059-22-7
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
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
Substrates: -
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5-phenylheme + electron donor + O2
biliverdin IXalpha + Fe2+ + CO + oxidized eletron donor + H2O + benzoic acid
Substrates: -
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?
alpha-meso-formylmesoheme + NADPH
? + NADP+
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Substrates: exclusively oxidized at a non-formyl substituted meso-carbon
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?
alpha-meso-hydroxyhemin IX + reduced acceptor + O2
verdoheme IXalpha + CO + acceptor + H2O
-
Substrates: -
Products: -
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?
alpha-meso-oxyprotoheme IX + [reduced NADPH-hemoprotein reductase] + O2
?
-
Substrates: -
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r
beta-meso-hydroxyhemin IX + reduced acceptor + O2
verdoheme IXbeta + CO + acceptor + H2O
-
Substrates: -
Products: -
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?
Co-heme + NADPH + H+ + O2
biliverdin Ixalpha + Co2+ + CO + NAD+ + H2O
-
Substrates: -
Products: -
Products: -
r
delta-meso-hydroxyhemin IX + reduced acceptor + O2
verdoheme IXdelta + CO + acceptor + H2O
-
Substrates: -
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Products: -
?
Fe-heme + [reduced NADPH-hemoprotein reductase] + O2
biliverdin Ixalpha + Fe2+ + CO + NAD+ + H2O
-
Substrates: -
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r
gamma-meso-hydroxyhemin IX + reduced acceptor + O2
verdoheme IXgamma + CO + acceptor + H2O
-
Substrates: -
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?
hematoheme + NADPH + H+ + O2
hematobiliverdin Fe2+ + CO + NAD+ + H2O
-
Substrates: -
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Products: -
r
heme + 2 NADH + 2 H+ + 2 O2
biliverdin + Fe2+ + CO + 2 NAD+ + H2O
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Substrates: 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
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?
heme + ferredoxin + O2
biliverdin IXalpha + Fe2+ + CO + A + H2O
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Substrates: HY1, HO3, and HO4
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?
heme + NADPH + H+ + O2
biliverdin IXdelta + biliverdin IXalpha + Fe2+ + CO + NADP+ + H2O
Substrates: -
Products: mutant R183E, yields about 20% of product biliverdin IXdelta
Products: mutant R183E, yields about 20% of product biliverdin IXdelta
?
heme + [reduced NADPH-hemoprotein reductase] + O2
biliverdin + Fe2+ + CO + [oxidized NADPH-hemoprotein reductase] + H2O
heme c + NADPH + H+ + O2
biliverdin c + Fe2+ + CO + NAD+ + H2O
-
Substrates: -
Products: -
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r
hemin + reduced acceptor + O2
alpha-meso-hydroxyhemin IX + CO + acceptor + H2O
-
Substrates: -
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?
protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2
biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O
protoheme + reduced acceptor + O2 + Fe2+
biliverdin-IX-alpha + CO + Fe3+ + acceptor + H2O
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Substrates: -
Products: -
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?
protoheme + [reduced cytochrome P450 reductase] + O2
biliverdin + Fe2+ + CO + [oxidized cytochrome P450 reductase] + H2O
Substrates: -
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?
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
Substrates: -
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?
verdoheme IXalpha + H2O
biliverdin IXalpha + Fe2+
-
Substrates: -
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?
gamma-CH-Fe(cor) + 3 AH2 + 3 O2
?
-
Substrates: 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
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?
gamma-CH-Fe(cor) + 3 AH2 + 3 O2
?
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Substrates: 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
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?
heme + 2 NADPH + 2 H+ + 2 O2
biliverdin + Fe2+ + CO + 2 NADP+ + H2O
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Substrates: involved in heme metabolism
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?
heme + 2 NADPH + 2 H+ + 2 O2
biliverdin + Fe2+ + CO + 2 NADP+ + H2O
-
Substrates: -
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?
heme + 2 NADPH + 2 H+ + 2 O2
biliverdin + Fe2+ + CO + 2 NADP+ + H2O
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Substrates: involved in heme metabolism
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?
heme + 2 NADPH + 2 H+ + 2 O2
biliverdin + Fe2+ + CO + 2 NADP+ + H2O
-
Substrates: -
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?
heme + 2 NADPH + 2 H+ + 2 O2
biliverdin + Fe2+ + CO + 2 NADP+ + H2O
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Substrates: involved in heme metabolism
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?
heme + 2 NADPH + 2 H+ + 2 O2
biliverdin + Fe2+ + CO + 2 NADP+ + H2O
Substrates: -
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?
heme + 2 NADPH + 2 H+ + 2 O2
biliverdin + Fe2+ + CO + 2 NADP+ + H2O
-
Substrates: -
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?
heme + 2 NADPH + 2 H+ + 2 O2
biliverdin + Fe2+ + CO + 2 NADP+ + H2O
Substrates: -
Products: -
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?
heme + 2 NADPH + 2 H+ + 2 O2
biliverdin + Fe2+ + CO + 2 NADP+ + H2O
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Substrates: involved in heme metabolism
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?
heme + 2 NADPH + 2 H+ + 2 O2
biliverdin + Fe2+ + CO + 2 NADP+ + H2O
-
Substrates: involved in heme metabolism
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?
heme + 2 NADPH + 2 H+ + 2 O2
biliverdin + Fe2+ + CO + 2 NADP+ + H2O
-
Substrates: -
Products: -
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?
heme + 2 NADPH + 2 H+ + 2 O2
biliverdin + Fe2+ + CO + 2 NADP+ + H2O
-
Substrates: involved in heme metabolism
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?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
-
Substrates: -
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?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
-
Substrates: requires three oxidative reaction steps, via alpha-meso-hydroxy-heme and verdoheme, detailed overview
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?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
Substrates: -
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?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
Substrates: reaction intermediate verdoheme and the verdoheme-enzyme complex are gradually degraded in the presence of O2
Products: -
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?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
-
Substrates: -
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?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
-
Substrates: requires three oxidative reaction steps, via alpha-meso-hydroxy-heme and verdoheme, detailed overview
Products: -
Products: -
?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
Substrates: -
Products: -
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?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
Substrates: -
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?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
Substrates: -
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?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
Substrates: reaction intermediate verdoheme and the verdoheme-enzyme complex are gradually degraded in the presence of O2
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?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
Substrates: -
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?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
-
Substrates: -
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?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
Substrates: requires three oxidative reaction steps, via alpha-meso-hydroxy-heme and verdoheme, detailed overview
Products: -
Products: -
?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
Substrates: -
Products: -
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?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
Substrates: -
Products: -
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?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
Substrates: -
Products: -
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?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
Substrates: reaction intermediate verdoheme and the verdoheme-enzyme complex are gradually degraded in the presence of O2
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Products: -
?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
Substrates: -
Products: -
Products: -
?
heme + 3 AH2 + 3 O2
biliverdin IXalpha + Fe2+ + CO + 3 A + 3 H2O
Substrates: -
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?
heme + 3 AH2 + 3 O2
biliverdin IXalpha + Fe2+ + CO + 3 A + 3 H2O
-
Substrates: -
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?
heme + 3 reduced ascorbate + 3 O2
biliverdin + Fe2+ + CO + 3 oxidized ascorbate + 3 H2O
-
Substrates: -
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heme + 3 reduced ascorbate + 3 O2
biliverdin + Fe2+ + CO + 3 oxidized ascorbate + 3 H2O
-
Substrates: -
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: 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
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?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: 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
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?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: -
Products: -
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?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
-
Substrates: induction of HO-1 via the ERK-Nrf2-ARE signaling pathway is involved in protecting cells from oxidative stress, overview
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?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
-
Substrates: -
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: HO-1 induction in vivo inhibits cytokine production in synovial tissue, while HO-1 inhibition restores it, overview
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: -
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: 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
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: HO-1 participates in the degradation of heme, the enzyme is involved in tumor development
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: heme oxygenase-1 is regulated by the Nrf2/anti-oxidant response element, ARE, pathway, which plays an important role in regulating cellular anti-oxidants
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: 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
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: 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
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: -
Products: -
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: 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
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: 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
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: 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
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: 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
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: first step in the heme degradation pathway
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
-
Substrates: 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
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: 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
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Products: -
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: 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
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: HO-1 transcriptional regulation system, overview
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: -
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: biliverdin is involved in hemin degradation
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: 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
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: inhibition or selective knockdown of HO-1 has anti-inflammatory effects via bilirubin, overview
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: activation of the enzyme leads to induction of the ABC transporter ABCG2, but not of ABCB6
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: -
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: -
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: the C-terminal 23 amino acids are essential for maximal catalytic activity
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: -
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: -
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?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: -
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: 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
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: -
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: -
Products: -
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: -
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: HO-1 participates in the degradation of heme, the enzyme is involved in tumor development
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: the enzyme shows anti-inflammatory activity, HO-1 expression is induced via the ERK1/2 activation pathway
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: 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
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: 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
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: 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
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: heme oxygenase-1 upregulation significantly inhibits TNF-alpha and Hmgb1 releasing and attenuates lipopolysaccharide-induced acute lung injury in mice, overview
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: endogenous HO-1 shows anti-apoptotic activity, and is overexpressed in various cancer diseases and might contribute to cancer progression
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
-
Substrates: HO-1 is the rate-limiting enzyme in heme degradation
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: -
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: HO-1 shows anti-inflammatory properties
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: 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
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: -
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: 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
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
-
Substrates: 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
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: 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
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: HO-1 is an inducible enzyme that catalyzes the rate-limiting step in the degradation of heme to biliverdin, CO and iron
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: statin-induced heme oxygenase-1 increases NF-kappaB activation and oxygen radical production in cultured neuronal cells exposed to lipopolysaccharide, overview
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: 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
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: -
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?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: -
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: -
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?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
-
Substrates: -
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?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: -
Products: -
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?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: -
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: -
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: endogenous HO-1 shows anti-apoptotic activity, and is overexpressed in various cancer diseases and might contribute to cancer progression
Products: -
Products: -
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: -
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: HO-1 shows anti-inflammatory properties
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: -
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: 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
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?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: -
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?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
-
Substrates: -
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?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
-
Substrates: -
Products: -
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?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: -
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: 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
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: the enzyme plays a protective role against hypoxic injury, and in the vicious cycle of low-flow priapism
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: HO-1 is a heat shock protein, and it provides endogenous anti-oxidant and anti-inflammatory moieties which can modulate colonic inflammation
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: 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
Products: -
Products: -
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: 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
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: HO-1 is the rate-limiting enzyme in heme degradation
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
-
Substrates: heme degradation
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: 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
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: 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
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: -
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: statin-induced heme oxygenase-1 increases NF-kappaB activation and oxygen radical production in cultured neuronal cells exposed to lipopolysaccharide, overview
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: -
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
-
Substrates: -
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: -
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heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized electron donor + H2O
-
Substrates: -
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heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized electron donor + H2O
Substrates: -
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heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized electron donor + H2O
-
Substrates: -
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heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized electron donor + H2O
Substrates: -
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heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized electron donor + H2O
-
Substrates: -
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heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized electron donor + H2O
Substrates: -
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heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized electron donor + H2O
-
Substrates: -
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heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized electron donor + H2O
-
Substrates: -
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heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized electron donor + H2O
Substrates: -
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heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized electron donor + H2O
-
Substrates: -
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heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
Substrates: NADH can replace NADPH at concentrations higher than 5 mM in vitro, NADH is unlikely to be an electron donor in vivo
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heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
Substrates: electron donor NADH
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heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
Substrates: 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
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heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
Substrates: alpha-meso-oxyprotoheme is an intermediate of heme degradation that is converted stereospecifically into biliverdin IXa via verdoheme IXa
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heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
Substrates: NADH-dependent heme-degradation activity, 16% of NADH activity with 0.5 mM NADPH
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heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
Substrates: enzyme catalyzes oxidative cleavage of both heme b and heme c
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heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
Substrates: porphyrins without chelated iron and metalloporphyrins other than iron porphyrins are not oxidized
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heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
Substrates: cytochrome c and myoglobin are not oxidized
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heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
Substrates: electron donor NADPH
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heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
Substrates: -
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heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
Substrates: electron donor ascorbic acid
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heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
Substrates: electron donor NADPH, reductase: human or E. coli NADPH-cytochrome P450 reductase or putidaredoxin/putidaredoxin reductase
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heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
Substrates: algal heme oxygenase requires a second reductant in addition to reduced pyridine nucleotide
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heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
Substrates: electron donor NADPH
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heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
Substrates: 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
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heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
Substrates: porphyrins without chelated iron and metalloporphyrins other than iron porphyrins are not oxidized
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heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
Substrates: -
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heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
Substrates: -
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heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
Substrates: 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
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heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
Substrates: porphyrins without chelated iron and metalloporphyrins other than iron porphyrins are not oxidized
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heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
Substrates: -
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heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
Substrates: -
Products: -
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heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
Substrates: 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
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heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
Substrates: porphyrins without chelated iron and metalloporphyrins other than iron porphyrins are not oxidized
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heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
Substrates: -
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heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
Substrates: electron donor NADPH
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heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
Substrates: overview, substrate specificity
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heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
Substrates: electron donor NADH
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heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
Substrates: 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
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heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
Substrates: Ni, Mn, and Sn protoporphyrin IX is not oxidized
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heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
Substrates: oxidation of Co-heme
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heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
Substrates: 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
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heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
Substrates: 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
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heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
Substrates: testis heme oxygenase 2 oxidizes Fe-protopophyrin, ferric hematoporphyrin acetate and ferric hematoporphyrin
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heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
Substrates: enzyme catalyzes oxidative cleavage of both heme b and heme c
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heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
Substrates: porphyrins without chelated iron and metalloporphyrins other than iron porphyrins are not oxidized
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?
heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
Substrates: intact cytochrome c is not oxidized
Products: -
Products: -
?
heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
Substrates: NADPH is more effective than NADH
Products: -
Products: -
?
heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
Substrates: electron donor NADPH
Products: -
Products: -
?
heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
Substrates: -
Products: -
Products: -
?
heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
Substrates: -
Products: -
Products: -
?
heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
Substrates: -
Products: -
Products: -
?
heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
Substrates: -
Products: -
Products: -
?
heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
Substrates: 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
Products: -
Products: -
?
heme + electron donor + O2
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
Substrates: porphyrins without chelated iron and metalloporphyrins other than iron porphyrins are not oxidized
Products: -
Products: -
?
heme + NADH + O2
biliverdin + Fe2+ + CO + NAD+ + H2O
-
Substrates: -
Products: -
Products: -
?
heme + NADH + O2
biliverdin + Fe2+ + CO + NAD+ + H2O
-
Substrates: -
Products: -
Products: -
?
heme + NADPH + H+ + O2
biliverdin IXalpha + Fe2+ + CO + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
heme + NADPH + H+ + O2
biliverdin IXalpha + Fe2+ + CO + NADP+ + H2O
Substrates: -
Products: wild-type, selective production of biliverdin IXalpha
Products: wild-type, selective production of biliverdin IXalpha
?
heme + [reduced NADPH-hemoprotein reductase] + O2
biliverdin + Fe2+ + CO + [oxidized NADPH-hemoprotein reductase] + H2O
-
Substrates: -
Products: -
Products: -
?
heme + [reduced NADPH-hemoprotein reductase] + O2
biliverdin + Fe2+ + CO + [oxidized NADPH-hemoprotein reductase] + H2O
Leptospira interrogans serovar Icterohaemorrhagiae serovar Lai 56601
-
Substrates: -
Products: -
Products: -
?
methemoglobin + electron donor + O2
?
-
Substrates: 30% of activity with heme
Products: -
Products: -
?
protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2
biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O
-
Substrates: -
Products: -
Products: -
?
protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2
biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O
-
Substrates: -
Products: -
Products: -
?
protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2
biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O
Substrates: -
Products: -
Products: -
?
protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2
biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O
Substrates: -
Products: -
Products: -
?
protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2
biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O
Substrates: -
Products: -
Products: -
?
protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2
biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O
-
Substrates: -
Products: -
Products: -
?
protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2
biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O
Substrates: -
Products: -
Products: -
?
protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2
biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O
Substrates: -
Products: -
Products: -
?
protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2
biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O
-
Substrates: -
Products: -
Products: -
?
protoheme + [reduced NADPH-hemoprotein reductase] + H+ + O2
biliverdin-IX-alpha + CO + Fe2+ + [oxidized NADPH-hemoprotein reductase] + H2O
-
Substrates: -
Products: -
Products: -
?
protoheme + [reduced NADPH-hemoprotein reductase] + H+ + O2
biliverdin-IX-alpha + CO + Fe2+ + [oxidized NADPH-hemoprotein reductase] + H2O
-
Substrates: -
Products: -
Products: -
?
protoheme + [reduced NADPH-hemoprotein reductase] + H+ + O2
biliverdin-IX-alpha + CO + Fe2+ + [oxidized NADPH-hemoprotein reductase] + H2O
-
Substrates: -
Products: -
Products: -
?
protoheme + [reduced NADPH-hemoprotein reductase] + O2
biliverdin + Fe2+ + CO + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
Products: -
?
protoheme + [reduced NADPH-hemoprotein reductase] + O2
biliverdin + Fe2+ + CO + [oxidized NADPH-hemoprotein reductase] + H2O
-
Substrates: -
Products: -
Products: -
?
protoheme + [reduced NADPH-hemoprotein reductase] + O2
biliverdin + Fe2+ + CO + [oxidized NADPH-hemoprotein reductase] + H2O
-
Substrates: -
Products: -
Products: -
?
protoheme + [reduced NADPH-hemoprotein reductase] + O2
biliverdin + Fe2+ + CO + [oxidized NADPH-hemoprotein reductase] + H2O
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: screening for heme proteins with heme oxygenase activity after de novo synthesis of the heme proteins on a membrane-coupled template, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: screening for heme proteins with heme oxygenase activity after de novo synthesis of the heme proteins on a membrane-coupled template, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: structure-function relationship and analysis, overview
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: expression of Hepatitis C virus core protein sensitizes hepatocytes to toxic injury and inhibits the induction of HO-1 in response to stress, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: expression of Hepatitis C virus core protein sensitizes hepatocytes to toxic injury and inhibits the induction of HO-1 in response to stress, overview
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: heme oxygenase-1 inhibits breast cancer invasion via suppressing the expression of matrix metalloproteinase-9, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: heme oxygenase-1 inhibits breast cancer invasion via suppressing the expression of matrix metalloproteinase-9, overview
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme is involved in cancer cell response to photodynamic therapy, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in cancer cell response to photodynamic therapy, overview
Products: -
Products: -
?
additional information
?
-
Substrates: structure-function analysis
Products: -
Products: -
?
additional information
?
-
-
Substrates: structure-function analysis
Products: -
Products: -
?
additional information
?
-
-
Substrates: ho-1 forms complexes with proteins from heavy metal-treated HeLa cells
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: structure-function relationship and analysis, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: hemoglobin neurotoxicity is attenuated by inhibitors of the protein kinase CK2 and protein kinase C independent of heme oxygenase activity
Products: -
Products: -
?
additional information
?
-
Substrates: overexpression of HO-1 in B16F10 cells confers resistance to cisplatin treatment, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: overexpression of HO-1 in B16F10 cells confers resistance to cisplatin treatment, overview
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: the anti-inflammatory activity of Phellinus linteus is mediated through the PKCdelta/Nrf2/ARE signaling to up-regulation of heme oxygenase-1
Products: -
Products: -
?
additional information
?
-
Substrates: LPS-induced maturation of dendritic cells is dependent on STAT3 phosphorylation and independent of HO-1 activity, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: LPS-induced maturation of dendritic cells is dependent on STAT3 phosphorylation and independent of HO-1 activity, overview
Products: -
Products: -
?
additional information
?
-
Substrates: PMA-dependent activation of HO-1 is mediated via a nonclassical NF-kappaB pathway that is independent of IKK2 activity
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: LPS-induced maturation of dendritic cells is dependent on STAT3 phosphorylation and independent of HO-1 activity, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: involved in the control of wound healing
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: HO-1 is involved in host defense reactions against various stresses, HO-1 modulates immunocyte activation and functions and suppresses mast cell degranulation, overview
Products: -
Products: -
?
additional information
?
-
Substrates: HO-1 is involved in host defense reactions against various stresses, HO-1 modulates immunocyte activation and functions and suppresses mast cell degranulation, overview
Products: -
Products: -
?
additional information
?
-
Substrates: butylated hydroxyanisole stimulates heme oxygenase-1 gene expression and inhibits neointima formation in rat arteries involving Nrf2 activation, overview
Products: -
Products: -
?
additional information
?
-
Substrates: expression and activity of heme oxygenase-1 is elevated in artificially induced low-flow priapism in rat penile tissues, overview
Products: -
Products: -
?
additional information
?
-
Substrates: HO-1 regulation, HO-1 autoregulation, and HO-1 regulatory functions, activation of MAPK pathways is not required in HO-1 self-regulation, overview
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme activity is positively correlated with nitric oxide and cGMP levels in cavernous tissue, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: PMA-dependent activation of HO-1 is mediated via a nonclassical NF-kappaB pathway that is independent of IKK2 activity
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: HO-1 and its byproduct biliverdin play major roles in the pathophysiological cascade leading to renal I/R injury
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: structure-function relationship and analysis, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
heme + 2 NADH + 2 H+ + 2 O2
biliverdin + Fe2+ + CO + 2 NAD+ + H2O
-
Substrates: 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
Products: -
Products: -
?
protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2
biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O
protoheme + reduced acceptor + O2 + Fe2+
biliverdin-IX-alpha + CO + Fe3+ + acceptor + H2O
-
Substrates: -
Products: -
Products: -
?
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
heme + 2 NADPH + 2 H+ + 2 O2
biliverdin + Fe2+ + CO + 2 NADP+ + H2O
-
Substrates: involved in heme metabolism
Products: -
Products: -
?
heme + 2 NADPH + 2 H+ + 2 O2
biliverdin + Fe2+ + CO + 2 NADP+ + H2O
-
Substrates: involved in heme metabolism
Products: -
Products: -
?
heme + 2 NADPH + 2 H+ + 2 O2
biliverdin + Fe2+ + CO + 2 NADP+ + H2O
-
Substrates: involved in heme metabolism
Products: -
Products: -
?
heme + 2 NADPH + 2 H+ + 2 O2
biliverdin + Fe2+ + CO + 2 NADP+ + H2O
-
Substrates: involved in heme metabolism
Products: -
Products: -
?
heme + 2 NADPH + 2 H+ + 2 O2
biliverdin + Fe2+ + CO + 2 NADP+ + H2O
-
Substrates: involved in heme metabolism
Products: -
Products: -
?
heme + 2 NADPH + 2 H+ + 2 O2
biliverdin + Fe2+ + CO + 2 NADP+ + H2O
-
Substrates: involved in heme metabolism
Products: -
Products: -
?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
-
Substrates: -
Products: -
Products: -
?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
-
Substrates: requires three oxidative reaction steps, via alpha-meso-hydroxy-heme and verdoheme, detailed overview
Products: -
Products: -
?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
Substrates: -
Products: -
Products: -
?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
-
Substrates: -
Products: -
Products: -
?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
-
Substrates: requires three oxidative reaction steps, via alpha-meso-hydroxy-heme and verdoheme, detailed overview
Products: -
Products: -
?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
Substrates: -
Products: -
Products: -
?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
Substrates: -
Products: -
Products: -
?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
Substrates: -
Products: -
Products: -
?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
-
Substrates: -
Products: -
Products: -
?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
Substrates: requires three oxidative reaction steps, via alpha-meso-hydroxy-heme and verdoheme, detailed overview
Products: -
Products: -
?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
Substrates: -
Products: -
Products: -
?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
Substrates: -
Products: -
Products: -
?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
Substrates: -
Products: -
Products: -
?
heme + 3 AH2 + 3 O2
biliverdin + Fe2+ + CO + 3 A + 3 H2O
Substrates: -
Products: -
Products: -
?
heme + 3 AH2 + 3 O2
biliverdin IXalpha + Fe2+ + CO + 3 A + 3 H2O
Substrates: -
Products: -
Products: -
?
heme + 3 AH2 + 3 O2
biliverdin IXalpha + Fe2+ + CO + 3 A + 3 H2O
-
Substrates: -
Products: -
Products: -
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: 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
Products: -
Products: -
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: 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
Products: -
Products: -
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
-
Substrates: induction of HO-1 via the ERK-Nrf2-ARE signaling pathway is involved in protecting cells from oxidative stress, overview
Products: -
Products: -
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: HO-1 induction in vivo inhibits cytokine production in synovial tissue, while HO-1 inhibition restores it, overview
Products: -
Products: -
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: -
Products: -
Products: -
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: 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
Products: -
Products: -
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: HO-1 participates in the degradation of heme, the enzyme is involved in tumor development
Products: -
Products: -
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: heme oxygenase-1 is regulated by the Nrf2/anti-oxidant response element, ARE, pathway, which plays an important role in regulating cellular anti-oxidants
Products: -
Products: -
?
heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: 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
Products: -
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: 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
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: -
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: 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
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: 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
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: 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
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: 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
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: first step in the heme degradation pathway
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
-
Substrates: 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
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: 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
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: 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
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: HO-1 transcriptional regulation system, overview
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: -
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: biliverdin is involved in hemin degradation
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: 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
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: inhibition or selective knockdown of HO-1 has anti-inflammatory effects via bilirubin, overview
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: activation of the enzyme leads to induction of the ABC transporter ABCG2, but not of ABCB6
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: HO-1 participates in the degradation of heme, the enzyme is involved in tumor development
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: the enzyme shows anti-inflammatory activity, HO-1 expression is induced via the ERK1/2 activation pathway
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: 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
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: 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
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: 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
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: heme oxygenase-1 upregulation significantly inhibits TNF-alpha and Hmgb1 releasing and attenuates lipopolysaccharide-induced acute lung injury in mice, overview
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: endogenous HO-1 shows anti-apoptotic activity, and is overexpressed in various cancer diseases and might contribute to cancer progression
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
-
Substrates: HO-1 is the rate-limiting enzyme in heme degradation
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: -
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: HO-1 shows anti-inflammatory properties
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: 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
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: -
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: 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
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
-
Substrates: 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
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: 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
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: HO-1 is an inducible enzyme that catalyzes the rate-limiting step in the degradation of heme to biliverdin, CO and iron
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: statin-induced heme oxygenase-1 increases NF-kappaB activation and oxygen radical production in cultured neuronal cells exposed to lipopolysaccharide, overview
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: 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
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: endogenous HO-1 shows anti-apoptotic activity, and is overexpressed in various cancer diseases and might contribute to cancer progression
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: HO-1 shows anti-inflammatory properties
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: 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
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
-
Substrates: -
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
-
Substrates: -
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: -
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: 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
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: the enzyme plays a protective role against hypoxic injury, and in the vicious cycle of low-flow priapism
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: HO-1 is a heat shock protein, and it provides endogenous anti-oxidant and anti-inflammatory moieties which can modulate colonic inflammation
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: 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
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: 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
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: HO-1 is the rate-limiting enzyme in heme degradation
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
-
Substrates: heme degradation
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: 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
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: 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
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: -
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: statin-induced heme oxygenase-1 increases NF-kappaB activation and oxygen radical production in cultured neuronal cells exposed to lipopolysaccharide, overview
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heme + AH2 + O2
biliverdin + Fe2+ + CO + A + H2O
Substrates: -
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protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2
biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O
-
Substrates: -
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protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2
biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O
-
Substrates: -
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protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2
biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O
Substrates: -
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protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2
biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O
Substrates: -
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protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2
biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O
Substrates: -
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protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2
biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O
-
Substrates: -
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protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2
biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O
Substrates: -
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protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2
biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O
Substrates: -
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protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2
biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O
-
Substrates: -
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protoheme + [reduced NADPH-hemoprotein reductase] + H+ + O2
biliverdin-IX-alpha + CO + Fe2+ + [oxidized NADPH-hemoprotein reductase] + H2O
-
Substrates: -
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protoheme + [reduced NADPH-hemoprotein reductase] + H+ + O2
biliverdin-IX-alpha + CO + Fe2+ + [oxidized NADPH-hemoprotein reductase] + H2O
-
Substrates: -
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protoheme + [reduced NADPH-hemoprotein reductase] + H+ + O2
biliverdin-IX-alpha + CO + Fe2+ + [oxidized NADPH-hemoprotein reductase] + H2O
-
Substrates: -
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protoheme + [reduced NADPH-hemoprotein reductase] + O2
biliverdin + Fe2+ + CO + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
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protoheme + [reduced NADPH-hemoprotein reductase] + O2
biliverdin + Fe2+ + CO + [oxidized NADPH-hemoprotein reductase] + H2O
-
Substrates: -
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protoheme + [reduced NADPH-hemoprotein reductase] + O2
biliverdin + Fe2+ + CO + [oxidized NADPH-hemoprotein reductase] + H2O
-
Substrates: -
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protoheme + [reduced NADPH-hemoprotein reductase] + O2
biliverdin + Fe2+ + CO + [oxidized NADPH-hemoprotein reductase] + H2O
-
Substrates: -
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additional information
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Substrates: 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
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additional information
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Substrates: 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
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additional information
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Substrates: 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
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additional information
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Substrates: 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
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additional information
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Substrates: expression of Hepatitis C virus core protein sensitizes hepatocytes to toxic injury and inhibits the induction of HO-1 in response to stress, overview
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additional information
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Substrates: expression of Hepatitis C virus core protein sensitizes hepatocytes to toxic injury and inhibits the induction of HO-1 in response to stress, overview
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additional information
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Substrates: 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
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additional information
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Substrates: heme oxygenase-1 inhibits breast cancer invasion via suppressing the expression of matrix metalloproteinase-9, overview
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additional information
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Substrates: heme oxygenase-1 inhibits breast cancer invasion via suppressing the expression of matrix metalloproteinase-9, overview
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additional information
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Substrates: 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
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additional information
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Substrates: 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
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additional information
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Substrates: the enzyme is involved in cancer cell response to photodynamic therapy, overview
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additional information
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Substrates: the enzyme is involved in cancer cell response to photodynamic therapy, overview
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additional information
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Substrates: 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
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additional information
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Substrates: hemoglobin neurotoxicity is attenuated by inhibitors of the protein kinase CK2 and protein kinase C independent of heme oxygenase activity
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additional information
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Substrates: overexpression of HO-1 in B16F10 cells confers resistance to cisplatin treatment, overview
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additional information
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Substrates: overexpression of HO-1 in B16F10 cells confers resistance to cisplatin treatment, overview
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additional information
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Substrates: 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
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additional information
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Substrates: 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
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additional information
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Substrates: the anti-inflammatory activity of Phellinus linteus is mediated through the PKCdelta/Nrf2/ARE signaling to up-regulation of heme oxygenase-1
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additional information
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Substrates: LPS-induced maturation of dendritic cells is dependent on STAT3 phosphorylation and independent of HO-1 activity, overview
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additional information
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Substrates: LPS-induced maturation of dendritic cells is dependent on STAT3 phosphorylation and independent of HO-1 activity, overview
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additional information
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Substrates: PMA-dependent activation of HO-1 is mediated via a nonclassical NF-kappaB pathway that is independent of IKK2 activity
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additional information
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Substrates: 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
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additional information
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Substrates: LPS-induced maturation of dendritic cells is dependent on STAT3 phosphorylation and independent of HO-1 activity, overview
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additional information
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Substrates: involved in the control of wound healing
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additional information
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Substrates: HO-1 is involved in host defense reactions against various stresses, HO-1 modulates immunocyte activation and functions and suppresses mast cell degranulation, overview
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additional information
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Substrates: HO-1 is involved in host defense reactions against various stresses, HO-1 modulates immunocyte activation and functions and suppresses mast cell degranulation, overview
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additional information
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Substrates: butylated hydroxyanisole stimulates heme oxygenase-1 gene expression and inhibits neointima formation in rat arteries involving Nrf2 activation, overview
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additional information
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Substrates: expression and activity of heme oxygenase-1 is elevated in artificially induced low-flow priapism in rat penile tissues, overview
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additional information
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Substrates: HO-1 regulation, HO-1 autoregulation, and HO-1 regulatory functions, activation of MAPK pathways is not required in HO-1 self-regulation, overview
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additional information
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Substrates: 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
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additional information
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Substrates: the enzyme activity is positively correlated with nitric oxide and cGMP levels in cavernous tissue, overview
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additional information
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Substrates: 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
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additional information
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Substrates: PMA-dependent activation of HO-1 is mediated via a nonclassical NF-kappaB pathway that is independent of IKK2 activity
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additional information
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Substrates: 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
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additional information
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Substrates: HO-1 and its byproduct biliverdin play major roles in the pathophysiological cascade leading to renal I/R injury
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additional information
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Substrates: 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
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
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CO as a ferrous heme ligand or ferricyanide as an oxidant have no effect
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heme
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hemoprotein, heme is both substrate and cofactor, heme oxygenase-2 binds heme at heme regulatory motifs with a conserved Cys-Pro pair
heme
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high-spin heme oxygenase-2,4-dimethyldeuterohemin-H2O complex dominates at low pH, low-spin heme oxygenase-2,4-dimethyldeuterohemin-OH complex dominates at alkaline pH
heme
-
the heme is located at the intermonomer interface and is bound by both monomers. The heme iron is coordinated by the side chain of His245 and an azide molecule when it is present in crystallization conditions
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cd2+
-
0.2 mM, induction of enzyme and 4.5fold enhancement of activity, biliverdin partly prevents
Fe2+
Iron
Mg2+
Iron
-
heme oxygenase consists of 3 required protein components: a ferredoxin-like Fe-S cluster protein that can be replaced by ferredoxin, a protein that is inactivated by diethyldicarbonate, inactivation is blocked by heme, a protein with ferredoxin-linked cytochrome c reductase activity
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(+-)-1-(1H-imidazol-1-yl)-4-(4-iodophenyl)-2-butanol hydrochloride
-
IC50: 0.00006 mM
(+-)-1-(1H-imidazol-1-yl)-4-phenyl-2-butanol hydrochloride
-
IC50: 0.0062 mM
(+-)-4-(4-bromophenyl)-1-(1H-imidazol-1-yl)-2-butanol hydrochloride
-
IC50: 0.00014 mM
(+-)-4-(4-chlorophenyl)-1-(1H-imidazol-1-yl)-2-butanol hydrochloride
-
IC50: 0.0005 mM
(+-)-4-(4-fluorophenyl)-1-(1H-imidazol-1-yl)-2-butanol hydrochloride
-
IC50: 0.0014 mM
(2-[2-(4-chlorophenyl)ethyl]-2-[1H-imidazol-1-yl)methyl]-1,3-dioxolane
-
(2E)-2-[4-(dimethylamino)benzylidene]hydrazinecarboximidamide
-
binding affinity 0.0229 mM, inhibition of biliverdin production in Escherichia coli expressing the enzyme
(2E)-2-[[4-(dimethylamino)phenyl]methylidene]hydrazinecarboximidamide
-
binding affinity is 0.0229 mM, complete inhibition
(2R,4R)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-(methoxymethyl)-1,3-dioxolane hydrochloride monohydrate
-
potent but non-selective inhibitor of HO-2
(2R,4R)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-(phenoxymethyl)-1,3-dioxolane hydrochloride
-
potent but non-selective inhibitor of HO-2
(2R,4R)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane dihydrochloride dihydrate
-
-
(2R,4R)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-[(4-iodophenoxy)methyl]-1,3-dioxolane hydrochloride
-
-
(2R,4R)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-[(4-methoxyphenoxy)methyl]-1,3-dioxolane hydrochloride
-
moderately high potency and selectivity toward HO-1
(2R,4R)-2-[2-(4-chlorophenyl)ethyl]-4-(hydroxymethyl)-2-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane hydrochloride
-
-
(2R,4R)-2-[2-(4-chlorophenyl)ethyl]-4-[(4-cyanophenoxy)methyl]-2-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane hydrochloride
-
potent but non-selective inhibitor of HO-2
(2R,4R)-2-[2-(4-chlorophenyl)ethyl]-4-[(4-fluorophenoxy)methyl]-2-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane hydrochloride
-
potent but non-selective inhibitor of HO-2
(2R,4R)-2-[2-(4-chlorophenyl)ethyl]-4-[(4-hydroxyphenoxy)methyl]-2-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane hydrochloride
-
-
(2R,4R)-4-(aminomethyl)-2-[(1H-imidazol-1-yl)methyl]-2-[(2-phenyl)ethyl]-1,3-dioxolane dihydrochloride
-
-
(2R,4R)-4-(azidomethyl)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane
-
moderately high potency and selectivity toward HO-1
(2R,4R)-4-[((4-adamantan-1-yl)phenoxy)methyl]-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane hydrochloride
-
-
(2R,4R)-4-[(4-aminophenoxy)methyl]-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane dihydrochloride
-
-
(2R,4R)-4-[(4-bromophenoxy)methyl]-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane hydrochloride
-
-
(2R,4R)-4-[(biphenyl-4-yloxy)methyl]-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane hydrochloride
-
moderately high potency and selectivity toward HO-1
(2R,4S)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)-methyl]-4-methyl-1,3-dioxolane
-
IC50: 0.0026 mM
(2R,4S)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-[((5-trifluoromethyl)pyridin-2-ylsulfanyl)methyl]-1,3-dioxolane hydrochloride
-
-
(2R,4S)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-[((5-trifluoromethylpyridin-2-yl)thio)methyl]-1,3-dioxolane
(2R,4S)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-[(4-methoxyphenylsulfanyl)methyl]-1,3-dioxolane hydrochloride
-
potent but non-selective inhibitor of HO-2
(2R,4S)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-[(4-nitrophenylsulfanyl)methyl]-1,3-dioxolane hydrochloride
-
-
(2R,4S)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-[(methylthio)methyl]-1,3-dioxolane hydrochloride
-
-
(2R,4S)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-[(naphthalen-2-ylsulfanyl)methyl]-1,3-dioxolane hydrochloride
-
moderately high potency and selectivity toward HO-1
(2R,4S)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-[(phenylsulfanyl)methyl]-1,3-dioxolane hydrochloride
-
moderately high potency and selectivity toward HO-1
(2R,4S)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-[(phenylsulphanyl)methyl]-1,3-dioxolane
-
(2R,4S)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-[(pyridin-4-ylsulfanyl)methyl]-1,3-dioxolane dihydrochloride
-
-
(2R,4S)-2-[2-(4-chlorophenyl)ethyl]-4-(fluoromethyl)-2-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane hydrochloride
-
potent but non-selective inhibitor of HO-2
(2R,4S)-2-[2-(4-chlorophenyl)ethyl]-4-[(4-chlorophenylsulfanyl)methyl]-2-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane hydrochloride
-
-
(2R,4S)-2-[2-(4-chlorophenyl)ethyl]-4-[(4-fluorophenylsulfanyl)methyl]-2-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane hydrochloride
-
-
(2R,4S)-2-[2-(4-chlorophenyl)ethyl]-4-[(cyclohexylsulfanyl)methyl]-2-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane hydrochloride
-
moderately high potency and selectivity toward HO-1
(2R,4S)-4-(chloromethyl)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane hydrochloride monohydrate
-
moderately high potency and selectivity toward HO-1
(2R,4S)-4-[(2-bromophenylsulfanyl)methyl]-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane hydrochloride
-
-
(2R,4S)-4-[(3-bromophenylsulfanyl)methyl]-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane hydrochloride
-
-
(2R,4S)-4-[(4-bromophenylsulfanyl)methyl]-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane hydrochloride
-
potent but non-selective inhibitor of HO-2
(2S, 4S)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-[((4-aminophenyl)thio)methyl]-1,3-dioxolane
(2S,4R)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)-methyl]-4-methyl-1,3-dioxolane
-
IC50: 0.02 mM
(2S,4S)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-methyl-1,3-dioxolane
-
IC50: 0.012 mM
(2Z)-4-[(4-anilinophenyl)amino]-4-oxobut-2-enoic acid
-
binding affinity 0.0156 mM, inhibition of biliverdin production in Escherichia coli expressing the enzyme
(2Z)-N'-[(1Z)-pyridin-3-ylmethylene]-2-(pyridin-3-ylmethylene)hydrazinecarboximidohydrazide
-
binding affinity 0.0122 mM, inhibition of biliverdin production in Escherichia coli expressing the enzyme
(2Z)-N'-[(1Z)-pyridin-3-ylmethylidene]-2-(pyridin-3-ylmethylidene)hydrazinecarboximidohydrazide
-
binding affinity is 0.0122 mM, complete inhibition
(E)-2-(4-isopropylbenzylidene)hydrazinecarboximidamide
compound shows a binding affinity of 5.7 microM and an MIC50 of 52.3 microg/ml against Pseudomonas aeruginosa PAO1 and increased activity against clinical isolates of Pseudomonas aeruginosa
1-((2-(2-(4-bromophenyl)ethyl)-1,3-dioxolan-2-yl)methyl)-1H-imidazole hydrochloride
-
IC50: 0.0019 mM
1-((2-(2-(4-chlorophenyl)ethyl)-1,3-dioxolan-2-yl)methyl)-1H-imidazole hydrochloride
-
IC50: 0.0043 mM
1-((2-(2-(4-fluorophenyl)ethyl)-1,3-dioxolan-2-yl)methyl)-1H-imidazole hydrochloride
-
IC50: 0.0038 mM
1-((2-(2-(4-iodophenyl)ethyl)-1,3-dioxolan-2-yl)methyl)-1H-imidazole hydrochloride
-
IC50: 0.0037 mM
1-((2-(2-phenylethyl)-1,3-dioxolan-2-yl)methyl)-1H-imidazole hydrochloride
-
IC50: 0.0007 mM
1-(1H-imidazol-1-yl)-4-(4-iodophenyl)-2-butanone hydrochloride
-
IC50: 0.00011 mM
1-(4-trifluoromethylbenzyl)-2-(pyrrolidin-1-ylmethyl)-1H-benzimidazole
-
1-(naphthalen-2-ylmethyl)-2-(pyrrolidin-1-ylmethyl)-1H-benzimidazole
-
2-(4-chlorophenyl)-N'-[(1E)-1H-indol-3-ylmethylidene]acetohydrazide
-
binding affinity is 0.0141 mM, complete inhibition
2-(4-chlorophenyl)-N'-[(1Z)-1H-inden-3-ylmethylene]acetohydrazide
-
binding affinity 0.0141 mM, inhibition of biliverdin production in Escherichia coli expressing the enzyme
2-[2-(4-bromophenyl)ethyl]-2-[(1H-imidazol-1-yl) methyl]-1,3-dioxolane
-
2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl) methyl]-1,3-dioxolane
-
2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-1,3-dithiolane
-
IC50: 0.0047 mM
2-[2-(4-fluorophenyl)ethyl]-2-[(1H-imidazol-1-yl) methyl]-1,3-dioxolane
-
3-morpholinosydnonimine
-
NO-donor, 27% inhibition of recombinant heme oxygenase-2
4-(4-bromophenyl)-1-(1H-imidazol-1-yl)-2-butanone hydrochloride
-
IC50: 0.0017 mM
4-(4-chlorophenyl)-1-(1H-imidazol-1-yl)-2-butanone hydrochloride
-
IC50: 0.0047 mM
4-(4-fluorophenyl)-1-(1H-imidazol-1-yl)-2-butanone hydrochloride
-
IC50: 0.0027 mM
4-oxo-4-[[4-(phenylamino)phenyl]amino]butanoic acid
-
binding affinity is 0.0156 mM, complete inhibition
4-phenyl-1-(1H-1,2,4-triazol-1-yl)-2-butanone
-
the inhibitor binds at the distal pocket through the coordination of heme iron by the N4 in the triazole mpiety, whereas the phenyl group is stabilized by hydrophobic interactions from residues within the binding pocket, binding structure, modelling, overview
4-[(2-hydroxyphenyl)amino]naphthalene-1,2-dione
-
binding affinity is 0.0288 mM, partial inhibition
calmidazolium chloride
-
inhibition of calmodulin-stimulation, 50% inhibition at 0.008 mM
copoly(styrene-maleic acid)-zinc protoporphyrin
micelles, competitive inhibition
Fe-deuteroporphyrin IX 2,4-bisglycol
-
0.01 mM, 46.8% inhibition of kidney heme oxygenase
FR180204
-
ERK inhibitor, reduces baseline culture HO activity, without altering the activity of recombinant HO-1 or HO-2
N'-(pyridin-4-ylcarbonyl)pyridine-4-carbohydrazide
-
binding affinity is 0.0335 mM, partial inhibition
N-(4-imidazo[1,2-a]pyridin-2-ylphenyl)-2-nitrobenzamide
-
binding affinity is 0.0209 mM, complete inhibition
N-(4-imidazo[1,2-a]pyridin-2-ylphenyl)-3-nitrobenzamide
-
binding affinity 0.0209 mM, inhibition of biliverdin production in Escherichia coli expressing the enzyme
S-nitroso-N-acetyl-pennicillamine
-
NO-donor, 23% inhibition of recombinant heme oxygenase-2
SL327
-
MEK inhibitor, reduces baseline culture HO activity, without altering the activity of recombinant HO-1 or HO-2
sodium nitroprusside
-
NO-donor, 58% inhibition of recombinant heme oxygenase-2
U0126
-
MEK inhibitor, reduces baseline culture HO activity, without altering the activity of recombinant HO-1 or HO-2
Zn (II) protoporphyrin IX
a specific HO-1 inhibitor, inhibition of HO-1 activity by Zn (II) protoporphyrin IX, a specific HO-1 inhibitor, prevents the suppression of TNF-alpha production. The cytokine inhibition by HO-1 is associated with selective suppression of the DNA-binding activity of AP-1 transcription factors
Zn protoporphyrin IX
-
pretreatment prior to administration of Cd2+, decrease of enzyme activity to half
Zn-deuteroporphyrin IX 2,4-bisglycol
-
0.002 mM, complete inhibition of kidney heme oxygenase
(2R,4R)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-methyl-1,3-dioxolane
-
IC50: 0.0015 mM
(2R,4R)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-methyl-1,3-dioxolane
-
IC50: 0.0008 mM
(2R,4S)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-[((5-trifluoromethylpyridin-2-yl)thio)methyl]-1,3-dioxolane
-
(2R,4S)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-[((5-trifluoromethylpyridin-2-yl)thio)methyl]-1,3-dioxolane
-
(2S, 4S)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-[((4-aminophenyl)thio)methyl]-1,3-dioxolane
azalanstat, potent inhibitor of HO
(2S, 4S)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-[((4-aminophenyl)thio)methyl]-1,3-dioxolane
azalanstat, potent inhibitor of HO; azalanstat, potent inhibitor of HO
1-(4-bromophenyl)-2-[2-(1-methylethyl)-1H-imidazol-1-yl]ethanone
27% inhibition at 0.1 mM
2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane
1 mM, potent inhibitor
2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane
-
IC50: 0.004 mM
benzyl isocyanide
-
most potent uncompetitive inhibitor with respect to heme, is the strongest ligand to ferrous heme
benzyl isocyanide
-
most potent uncompetitive inhibitor with respect to heme, is the strongest ligand to ferrous heme with an almost 42fold greater binding affinity for HO-1 than isopropyl isocyanide. HO-2 displays a similar trend. Ferric verdoheme-HO-1 shows a 2fold higher affinity for the inhibitor than ferric heme-HO-1
cobalt protoporphyrin
i.e. CoPP, significantly reduces the viability of glioma cells GBM8401 in the absence of serum, fetal bovine serum or bovine serum albumin completely abolishes the cytotoxic effect, overview, N-acetyl-l-cysteine does not protect against cell death
cobalt protoporphyrin
i.e. CoPP, significantly reduces the viability of glioma cells C6 in the absence of serum, fetal bovine serum or bovine serum albumin completely abolishes the cytotoxic effect, overview, N-acetyl-l-cysteine does not protect against cell death
DTT
-
shows high-affinity binding, structure, overview. The noncoordinating thiol group of DTT is critical for its high affinity to the mammalian HO
DTT
shows high-affinity binding, structure, overview. The noncoordinating thiol group of DTT is critical for its high affinity to the mammalian HO
ferric protoporphyrin
i.e. FePP or hemin, significantly reduces the viability of glioma cells GBM8401 in the absence of serum, fetal bovine serum or bovine serum albumin completely abolishes the cytotoxic effect, overview, N-acetyl-l-cysteine protects against cell death
ferric protoporphyrin
i.e. FePP or hemin, significantly reduces the viability of glioma cells C6 in the absence of serum, fetal bovine serum or bovine serum albumin completely abolishes the cytotoxic effect, overview, N-acetyl-l-cysteine protects against cell death
Hg2+
-
inhibition of NADPH-cytochrome c reductase or biliverdin reductase in reconstituted heme oxygenase system
isopropyl isocyanide
-
binding affinity is the weakest for HO-1. HO-2 displays a similar trend
n-butyl isocyanide
-
displays a 9fold higher affinity than isopropyl isocyanide for HO-1. HO-2 displays a similar trend. Ferric verdoheme-HO-1 shows a 2fold higher affinity for the inhibitor than ferric heme-HO-1
p-chloromercuribenzoate
-
inhibition of NADPH-cytochrome c reductase in reconstituted heme oxygenase system
Porphyrins
-
metalloporphyrins, decreasing order of inhibition potency: Sn-mesoporphyrin, Sn-protoporphyrin, Zn-protoporphyrin, Mn-protoporphyrin, Co-protoporphyrin
Porphyrins
-
protoporphyrin IX, Zn-protoporphyrin IX, 2,4-diacetyldeuteroporphyrin IX, deuteroporphyrin IX, coproporphyrin II, III and IV
Sn-protoporphyrin
-
0.001 mM, 84% inhibition of HO-1, 99% inhibition of HO-2
Sn-protoporphyrin
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
Sn-protoporphyrin IX
-
Sn-PPIX, inhibits the enzyme and reduces the activating effect of lipopolysaccharides
thioglycerol
-
binds weakly, shows high affinity to the mammalian HO
thioglycerol
-
binds with 10fold lower affinity than DTT, shows high affinity to the mammalian HO
thioglycerol
binds with 10fold lower affinity than DTT, shows high affinity to the mammalian HO
tin protoporphyrin
SnPP, specific HO-1 inhibition abrogating the inhibition of COX-2 expression by Wy-14,643
tin protoporphyrin
i.e. SnPP, does not affect the viability of glioma cells GBM8401 in the absence of serum
tin protoporphyrin
i.e. SnPP, does not affect the viability of glioma cells C6 in the absence of serum
zinc protoporphyrin
dose-dependently increases SMC proliferation, induced by either platelet-derived growth factor or 15% fetal bovine serum
zinc protoporphyrin
ZnPP, supresses enzyme induction and inhibits HO-1, it also abolishes the anti-colitic effect of 5-aminosalicylic acid
zinc protoporphyrin IX
ZnPP, high-loading nanosized micelles of copoly(styrene-maleic acid)-zinc protoporphyrin for targeted delivery of a potent heme oxygenase inhibitor, method development, overview
-
zinc protoporphyrin IX
Zn(II)PPIX, a selective HO-1 inhibitor, Zn(II)PPIX exerts dose-dependent antitumor effects and shows retardation of tumor growth
-
zinc protoporphyrin IX
Zn(II)PPIX, a selective HO-1 inhibitor, Zn(II)PPIX exerts dose-dependent antitumor effects and shows retardation of tumor growth
-
zinc protoporphyrin IX
-
activity of both recombinant isoenzymes HO-1 and HO-2 is strongly inhibited
-
Zn(II) protoporphyrin IX
-
mitigates brazilin-induced activity of HO-1 and inhibition of NO, PEG2, TNF-alpha and IL-1beta production in lipopolysaccharide-stimulated RAW264.7 macrophages
Zn-protoporphyrin
-
0.001 mM, 87% inhibition of HO-1, 91% inhibition of HO-2
additional information
-
whereas equilibrium binding of the isocyanides to ferric human heme oxygenases is rapid, binding to ferric Hmx1 is much slower
-
additional information
-
development of HO-specific inhibitors targeting the critical distal hydrogen bonding network, e.g. thiol compounds, overview. HmuO exhibits similar affinity for DTT, DTE, and thioglycerol in contrast to the mammalian enzyme, indicating no functionality of the noncoordinating thiol group in complex formation with this bacterial HO
-
additional information
imidazole-based inhibitor derivatives, overview; imidazole-based inhibitor derivatives, overview
-
additional information
imidazole-based inhibitor derivatives, overview; imidazole-based inhibitor derivatives, overview
-
additional information
-
HO-1-generated hydrogen peroxide leads to a decrease in HO-1 activity
-
additional information
azole-based, HO-1 inhibitors act in a non-competitive manner with respect to heme. These inhibitors bind to the distal side of heme in the heme-binding pocket with the imidazolyl group in the eastern region of the inhibitor serving as an anchor by coordinating with the heme iron. The western region of the respective inhibitors fits into a hydrophobic pocket that extends back towards the distal side of the heme-binding pocket. The inherent flexibility of the distal helix results in the opening up of the heme-binding pocket so as to accommodate the inhibitor
-
additional information
-
azole-based, HO-1 inhibitors act in a non-competitive manner with respect to heme. These inhibitors bind to the distal side of heme in the heme-binding pocket with the imidazolyl group in the eastern region of the inhibitor serving as an anchor by coordinating with the heme iron. The western region of the respective inhibitors fits into a hydrophobic pocket that extends back towards the distal side of the heme-binding pocket. The inherent flexibility of the distal helix results in the opening up of the heme-binding pocket so as to accommodate the inhibitor
-
additional information
-
development of HO-specific inhibitors targeting the critical distal hydrogen bonding network, e.g. thiol compounds, overview. Thiol binding significantly suppresses but does not completely interrupt the reduction of the ferric heme to the ferrous state. HO is inhibited thus at higher thiol concentration than expected from the dissociation equilibrium constants
-
additional information
synthesis and inhibitory potency on isozyme HO-1 of imidazole-based compounds, molecular docking and modelling, overview. No inhibition by 1-[6-(4-bromophenoxy)exyl]-1H-imidazole, 1-(2-phenoxyethyl)-1H-imidazole, 2-(1H-imidazol-1-yl)-1-(4-nitrophenyl)ethanol, and 1-(4-bromophenyl)-2-(1H-imidazol-1-yl)ethanone
-
additional information
-
synthesis and inhibitory potency on isozyme HO-1 of imidazole-based compounds, molecular docking and modelling, overview. No inhibition by 1-[6-(4-bromophenoxy)exyl]-1H-imidazole, 1-(2-phenoxyethyl)-1H-imidazole, 2-(1H-imidazol-1-yl)-1-(4-nitrophenyl)ethanol, and 1-(4-bromophenyl)-2-(1H-imidazol-1-yl)ethanone
-
additional information
metalloporphyrins are used as competitive enzyme inhibitors. Development of isozyme-selective heme oxygenase inhibitors. Development and evaluation of non-competitive inhibitors with selectivity for isozyme HO-1, and synthesis and analysis of a series of 2-oxy-substituted 1-(1H-imidazol-1-yl)-4-phenylbutanes, overview. Synthesis of a series of alpha-(1H-imidazol-1-yl)-omega-phenylalkanes to examine the effect of introducing heteroatoms into the central alkyl linker. Imidazole-dioxolane-based HO inhibitors are all selective for HO-1, and exhibit substantially lower activity towards HO-2. HO-1-inhibitor, binding mechanism, detailed overview. HO-1 inducible binding mode, overview
-
additional information
metalloporphyrins are used as competitive enzyme inhibitors. Development of isozyme-selective heme oxygenase inhibitors. Development and evaluation of non-competitive inhibitors with selectivity for isozyme HO-1, and synthesis and analysis of a series of 2-oxy-substituted 1-(1H-imidazol-1-yl)-4-phenylbutanes, overview. Synthesis of a series of alpha-(1H-imidazol-1-yl)-omega-phenylalkanes to examine the effect of introducing heteroatoms into the central alkyl linker. Imidazole-dioxolane-based HO inhibitors are all selective for HO-1, and exhibit substantially lower activity towards HO-2. HO-1-inhibitor, binding mechanism, detailed overview. HO-1 inducible binding mode, overview
-
additional information
-
metalloporphyrins are used as competitive enzyme inhibitors. Development of isozyme-selective heme oxygenase inhibitors. Development and evaluation of non-competitive inhibitors with selectivity for isozyme HO-1, and synthesis and analysis of a series of 2-oxy-substituted 1-(1H-imidazol-1-yl)-4-phenylbutanes, overview. Synthesis of a series of alpha-(1H-imidazol-1-yl)-omega-phenylalkanes to examine the effect of introducing heteroatoms into the central alkyl linker. Imidazole-dioxolane-based HO inhibitors are all selective for HO-1, and exhibit substantially lower activity towards HO-2. HO-1-inhibitor, binding mechanism, detailed overview. HO-1 inducible binding mode, overview
-
additional information
imidazole-based inhibitor derivatives, overview; imidazole-based inhibitor derivatives, overview
-
additional information
imidazole-based inhibitor derivatives, overview; imidazole-based inhibitor derivatives, overview
-
additional information
-
no inhibition by phosphatidylinositol 3-kinase inhibitors LY294002 and LY303511, by 4,5,6,7-tetrabromobenzotriazole, 2-dimethyl-amino-4,5,6,7-tetrabromo-1H-benzimidazole, and by the PKC inhibitor GF109203X
-
additional information
-
synthesis of a series of 2-oxy-substituted 1-(1H-imidazol-1-yl)-4-phenylbutanes comprising imidazole-ketones, imidazole-dioxolanes, and imidazole-alcohols substituted with halogens in the phenyl ring, evaluation of the inhibitory potency on heme oxygenase, overview
-
additional information
EtOH combined with burn injury significantly increases neutrophil O2- production and p47phox and p67phox activation and decreases caspase-3 activity and apoptosis, accompanied with a decrease in neutrophil HO-1 levels, overview
-
additional information
azole-based, HO-1 inhibitors act in a non-competitive manner with respect to heme. These inhibitors bind to the distal side of heme in the heme-binding pocket with the imidazolyl group in the eastern region of the inhibitor serving as an anchor by coordinating with the heme iron. The western region of the respective inhibitors fits into a hydrophobic pocket that extends back towards the distal side of the heme-binding pocket. The inherent flexibility of the distal helix results in the opening up of the heme-binding pocket so as to accommodate the inhibitor
-
additional information
azole-based, HO-1 inhibitors act in a non-competitive manner with respect to heme. These inhibitors bind to the distal side of heme in the heme-binding pocket with the imidazolyl group in the eastern region of the inhibitor serving as an anchor by coordinating with the heme iron. The western region of the respective inhibitors fits into a hydrophobic pocket that extends back towards the distal side of the heme-binding pocket. The inherent flexibility of the distal helix results in the opening up of the heme-binding pocket so as to accommodate the inhibitor
-
additional information
-
design and synthesis, and inhibitory potency of a series of 2-oxy-substituted 1-azolyl-4-phenylbutanes, inhibition of heme oxygenase-1 and heme oxygenase-2, overview
-
additional information
development of HO-specific inhibitors targeting the critical distal hydrogen bonding network, e.g. thiol compounds, overview. Thiol binding significantly suppresses but does not completely interrupt the reduction of the ferric heme to the ferrous state. HO is inhibited thus at higher thiol concentration than expected from the dissociation equilibrium constants
-
additional information
selective inhibition of heme oxygenase-2 activity by analogues of 1-(4-chlorobenzyl)-2-(pyrrolidin-1-ylmethyl)-1H-benzimidazole (clemizole), exploration of the effects of substituents at the N-1 position, overview. Many of the compounds are potent and highly selective for the constitutive HO-2 isozyme, but show substantially less inhibitory activity against the inducible HO-1 isozyme
-
additional information
synthesis and inhibitory potency on isozyme HO-1 of imidazole-based compounds, molecular docking and modelling, overview
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,4,6-Trinitrobenzene sulfonic acid
induces HO-1 expression in the colon and stimulates its catalytic activity
5-aminosalicylic acid
induces HO-1 expression in the colon and stimulates its catalytic activity
ascorbate
-
addition of a second electron donor like ascorbate leads to 10times faster heme conversion
brazilin
-
main constituent of Caesalpinia sappan, induces HO-1 expression in a concentration-dependent manner at 0.01-0.3 mM at the level of protein synthesis, thus without affecting mRNA transcription of HO-1
Calmodulin
-
calcium-dependent binding to enzyme, 3fold increase in catalytic activity
Fe/S cluster
-
heme oxygenase consists of 3 required protein components: a ferredoxin-like Fe-S cluster protein that can be replaced by ferredoxin, a protein that is inactivated by diethyldicarbonate, inactivation is blocked by heme, a protein with ferredoxin-linked cytochrome c reductase activity
lipopolysaccharide
-
activates the enzyme, activation is partly reduced by addition of inhibitor Sn-protoporphyrin
propionate
-
the enzyme requires only a single propionate interacting with the buried terminus of Lys16 to exhibit full activity, and it tolerates the existence of a propionate at the exposed 8-position
SnCl2
is a potent and specific inducer of renal HO-1 expression and activity
additional information
-
heme turnover is promoted by light when spinach thylakoids are present
-
additional information
HO-1 is induced by epibatidine via neuronal nicotinic acetylcholine receptors and ERK1/2 in the neuroprotective signaling cascade, overview
-
additional information
-
HO-1 is induced by epibatidine via neuronal nicotinic acetylcholine receptors and ERK1/2 in the neuroprotective signaling cascade, overview
-
additional information
-
triphlorethol-A, i.e. 2-[2-(3,5-dihydroxyphenoxy)-3,5-dihydroxyphenoxy]benzene-1,3,5-triol, a phlorotannin isolated from Ecklonia cava, induces heme oxygenase-1 via activation of ERK and NF-E2 related factor 2 transcription factor, triphlorethol-A increases nuclear translocation, ARE, binding, and transcriptional activity of Nrf2, transcription factor Nrf2 regulates antioxidant response element, ARE, of phase 2 detoxifying and antioxidant enzymes, requirement for ERK activation in the induction of HO-1 expression by triphlorethol-A because an ERK inhibitor significantly reduces HO-1 protein expression in response to triphlorethol-A, overview
-
additional information
enzyme activity is increased by 7.5 and 15 kJ/squaremeter UV-B doses
-
additional information
-
enzyme activity is increased by 7.5 and 15 kJ/squaremeter UV-B doses
-
additional information
hemin and taurine chloramine, Tau-Cl, raise the transcription of the gene encoding HO-1
-
additional information
capsaicin, i.e. trans-8-methyl-N-vanillyl-6-nonenamide, induces heme oxygenase-1 expression in Hep-G2 cells via activation of PI3K-Nrf2 signaling
-
additional information
epigallocatechin activates heme oxygenase-1 expression via protein kinase Cdelta, not PKCalpha and PKCbeta, and Nrf2, siRNA knock down of Nrf2 significantly inhibits EGC-induced HO-1 expression, inhibition of PKCdelta, e.g. by Ro-31-8220, decreases EGC-induced HO-1 mRNA expression, whereas MAP kinase and phosphatidylinositol-3-kinase pathway inhibitors have no significant effect, overview
-
additional information
the enzyme expression is induced by enterolactone from enterobacteria through activation of nuclear factor-E2-related factor 2, Nrf2, in endothelial cells
-
additional information
-
the enzyme expression is induced by enterolactone from enterobacteria through activation of nuclear factor-E2-related factor 2, Nrf2, in endothelial cells
-
additional information
HO-1 expression, prooxidative activity, and cytotoxicity are increased after treatment with heme, heavy metals, and peroxides compared to control cells
-
additional information
-
HO-1 expression, prooxidative activity, and cytotoxicity are increased after treatment with heme, heavy metals, and peroxides compared to control cells
-
additional information
exogenous CO activates Nrf2 through the phosphorylation of protein kinase R-like endoplasmic reticulum kinase, PERK, resulting in HO-1 expression
-
additional information
-
exogenous CO activates Nrf2 through the phosphorylation of protein kinase R-like endoplasmic reticulum kinase, PERK, resulting in HO-1 expression
-
additional information
dehydrocostus lactone induces HO-1 expression in Hep-G2 cells, while mokko lactone, a reduced product of dehydrocostus lactone, and alpha-methyl-gamma-butyrolactone, a parent structure of mokko lactone, do not induce HO-1 expression
-
additional information
curcumin, but not its metabolite tetrahydrocurcumin, induces HO-1 expression and growth inhibition of aortic smooth muscle cells through Nrf2-dependent antioxidant response element, ARE, activation, mechanism, overview, curcumin is isolated from the rhizomes of turmeric
-
additional information
-
curcumin, but not its metabolite tetrahydrocurcumin, induces HO-1 expression and growth inhibition of aortic smooth muscle cells through Nrf2-dependent antioxidant response element, ARE, activation, mechanism, overview, curcumin is isolated from the rhizomes of turmeric
-
additional information
HO-1 is strongly induced in the skin after long wave ultraviolet radiation, UVA-1 irradiation generates oxidized phospholipids derived from 1-palmitoyl-2-arachidonoyl-sn-glycero-3-phosphorylcholine that mediate the expression of HO-1 in skin cells, epoxyisoprostanephosphatidylcholine also induces the enzyme in the skin, overview
-
additional information
ferric protoporphyrin IX enhances the HO-1 expression in MCF-7 cells
-
additional information
-
ferric protoporphyrin IX enhances the HO-1 expression in MCF-7 cells
-
additional information
oxidized-1-palmitoyl-2-arachidonoyl-sn-glycerol-3-phosphocholine, i.e. Ox-PAPC, induces HO-1 involving Nrf2 activation, the transcriptional activation is regulated by the plasma membrane electron transport complex, PMET, containing ecto-NADH oxidase 1, eNOX1, and NADPH:quinone oxidoreductase 1, NQO1. Chemical inhibitors of PMET system and siRNAs to PMET components NQO1 and eNOX1, as well as exogenous NAD(P)H significantly decrease HO-1 induction by Ox-PAPC
-
additional information
-
oxidized-1-palmitoyl-2-arachidonoyl-sn-glycerol-3-phosphocholine, i.e. Ox-PAPC, induces HO-1 involving Nrf2 activation, the transcriptional activation is regulated by the plasma membrane electron transport complex, PMET, containing ecto-NADH oxidase 1, eNOX1, and NADPH:quinone oxidoreductase 1, NQO1. Chemical inhibitors of PMET system and siRNAs to PMET components NQO1 and eNOX1, as well as exogenous NAD(P)H significantly decrease HO-1 induction by Ox-PAPC
-
additional information
HO-1 is induced by NO in macrophages and hepatocytes inhibiting apoptotic cell death of hepatocytes via the regulation of cellular homeostasis of prooxidant iron
-
additional information
vitreous induces heme oxygenase-1 expression mediated by transforming growth factor-beta and reactive oxygen species generation in human retinal pigment epithelial cells. Activator protein-1 binding sites are located in the promoter region of HO-1, and TGF-beta also induces the enzyme, while inhibitors of TGF-beta signaling, e.g. SB431542 or TGF-beta-neutralizing antibodies, decrease the vitreous induction of HO-1, but PD98059, an inhibitor of the ERK pathway, has no effect on HO-1 induction, overview
-
additional information
-
vitreous induces heme oxygenase-1 expression mediated by transforming growth factor-beta and reactive oxygen species generation in human retinal pigment epithelial cells. Activator protein-1 binding sites are located in the promoter region of HO-1, and TGF-beta also induces the enzyme, while inhibitors of TGF-beta signaling, e.g. SB431542 or TGF-beta-neutralizing antibodies, decrease the vitreous induction of HO-1, but PD98059, an inhibitor of the ERK pathway, has no effect on HO-1 induction, overview
-
additional information
the enzyme is induced by 5-aminolevulinic acid, the activation is reduced to 29% by gene silencing with siRNA, overview
-
additional information
oxidative stress and arsenite strongly induce HMOX1, heme oxygenase-1 induction by NRF2 requires inactivation of the transcriptional repressor BACH1, BACH1 repression is dominant over NRF2-mediated HMOX1 transcription and inactivation of BACH1 is a prerequisite for HMOX1 induction, but nuclear accumulation of NRF2 is not necessary for HMOX1 induction
-
additional information
hemin induces heme oxygenase-1 expression in human umbilical vein endothelial cells
-
additional information
-
hemin induces heme oxygenase-1 expression in human umbilical vein endothelial cells
-
additional information
far infrared irradiation induces HO-1 protein, mRNA and promoter activity through heat stress which activates the antioxidant responsive element/NF-E2-related factor-2 complex, overview
-
additional information
-
far infrared irradiation induces HO-1 protein, mRNA and promoter activity through heat stress which activates the antioxidant responsive element/NF-E2-related factor-2 complex, overview
-
additional information
induction of HO-1 by hemin and Zn2+-protoporphyrin IX in presence or absence of light, Nrf2-dependent induction of human ABC transporter ABCG2 and heme oxygenase-1 in HepG2 cells by photoactivation of porphyrins, overview
-
additional information
-
induction of HO-1 by hemin and Zn2+-protoporphyrin IX in presence or absence of light, Nrf2-dependent induction of human ABC transporter ABCG2 and heme oxygenase-1 in HepG2 cells by photoactivation of porphyrins, overview
-
additional information
-
positive correlation between seminal plasma HO enzyme activity and sperm concentration, sperm motility percentage, motile spermatozoa ml-1 and sperm normal morphology per cent
-
additional information
-
the proximal residue histidine 25 plays a key role in HO-1 activity
-
additional information
-
a higher dilauroylphosphatidylcholine/HO-1 ratio than typically used provides an improved environment for HO-1 activity
-
additional information
-
gamma-irradition of 0.5 Gy/min dose power causes a significant increase of activity
-
additional information
tranilast, i.e. N-[3',4'-dimethoxycinnamonyl] anthranilic acid, an orally active anti-allergic drug, tranilast induces heme oxygenase-1 expression through the extracellular signal-regulated kinase-1/2 pathway in RAW264.7 macrophages. Effects of tranilast on LPS-induced PGE2, NO, TNF-alpha, and IL-1beta production are partially reversed by the HO-1 inhibitor tin protoporphyrin, overview. UO126 significantly inhibits tranilast-induced HO-1 expression, but neither SB203580 nor SP600125 have a significant effect on HO-1 expression by tranilast
-
additional information
at low concentrations curcumin induces the expression of HO-1 in RAW264.7 macrophages
-
additional information
methoxychalcones, especially 5-methoxychalcone, 3,4,5-trimethoxychalcone, and 3,4,5,3',4',5'-hexamethoxychalcone, induce the enzyme expression and activity in macrophages, overview, increase in heme oxygenase activity and HO-1 protein expression mediated by CH25 is significantly attenuated by the presence of an inhibitor of PI3K LY2940002, as well as by the addition of the glutathione precursor NAC
-
additional information
the PKCdelta/Nrf2/ARE signaling up-regulates heme oxygenase-1
-
additional information
cobalt protoporphyrin, CoPPIX, induces the enzyme, molecular mechanism, overview, CoPPIX inhibits STAT3 phosphorylation and the LPS-mediated maturation of bone marrow-derived dendritic cells independently of HO-1
-
additional information
-
cobalt protoporphyrin, CoPPIX, induces the enzyme, molecular mechanism, overview, CoPPIX inhibits STAT3 phosphorylation and the LPS-mediated maturation of bone marrow-derived dendritic cells independently of HO-1
-
additional information
the HO-1 gene is transcriptionally induced by the phorbol ester PMA in cell cultures of monocytic cells with a regulatory pattern that is different from that of LPS-dependent HO-1 induction in these cells, overview, the upregulation is abrogated in embryonic fibroblasts from p65-/- mice, antioxidant N-acetylcysteine and inhibitors of p38 MAPK or serine/threonine kinase CK2 also block the upregulating effect of PMA, thus induction of HO-1 gene expression by PMA is regulated via an IkappaB kinase-independent, atypical NFkappaB pathway that is mediated via the activation of p38 MAPK and CK2, overview, PMA-dependent HO-1 gene activation requires IkappaBalpha, but notIKK2
-
additional information
striatal blood injection increases HO activity, and oxidative stress induces the enzyme, overview
-
additional information
-
striatal blood injection increases HO activity, and oxidative stress induces the enzyme, overview
-
additional information
tanshinone IIA from Salvia miltiorrhiza induces heme oxygenase-1 expression via intracellular production of reactive oxygen species, and inhibits lipopolysaccharide-induced nitric oxide expression in RAW 264.7 cells. Inhibition of HO-1 or scavenging of CO significantly reverses the inhibition of LPS-stimulated nitrite accumulation by tanshinone IIA, signaling pathways, overview. Activation of PI 3-K and ERK signaling pathways are required for tanshinone-induction of HO-1 protein expression in RAW 264.7 macrophages
-
additional information
-
hemin is an inducer of HO-1, additive effect of hemin with dexamethasone, overview
-
additional information
the toll-like receptor 2 is involved in HO-1 induction in glial cells, 34fold induction of HO-1 by stab-wound injury in wild-type mice, overview
-
additional information
-
the toll-like receptor 2 is involved in HO-1 induction in glial cells, 34fold induction of HO-1 by stab-wound injury in wild-type mice, overview
-
additional information
lipopolysaccharide, from Escherichia coli, serotype 0127:B8, upregulates the expression of HO-1 in adult and fetal mouse liver, maternal LPS exposure results in oxidative stress in fetuses, which may contribute to LPS-induced developmental toxicity, LPS-induced upregulation of HO-1 is blocked by alpha-phenyl-N-t-butylnitrone, PBN, a free radical spin trapping agent, overview
-
additional information
-
lipopolysaccharide, from Escherichia coli, serotype 0127:B8, upregulates the expression of HO-1 in adult and fetal mouse liver, maternal LPS exposure results in oxidative stress in fetuses, which may contribute to LPS-induced developmental toxicity, LPS-induced upregulation of HO-1 is blocked by alpha-phenyl-N-t-butylnitrone, PBN, a free radical spin trapping agent, overview
-
additional information
simvastatin induces the enzyme in neurons, HO-1 upregulation is significantly associated with increased nuclear factor kappa B activation, manifested as IkappaBalpha phosphorylation and p65 nuclear translocation, as well as increased production of superoxides, inhibition of the effects by zinc protoporphyrin
-
additional information
butylated hydroxyanisole stimulates heme oxygenase-1 gene expression after rat carotid artery injury, overview
-
additional information
heme oxygenase-1 is induced by tert-butylhydroquinone and by deltamethrin via activation of Nrf2, overview
-
additional information
HO-1 is a heat shock protein with anti-inflammatory activity
-
additional information
curcumin, but not its metabolite tetrahydrocurcumin, induces HO-1 expression and growth inhibition of vascular smooth muscle cells through Nrf2-dependent antioxidant response element, ARE, activation, mechanism, overview, curcumin is isolated from the rhizomes of turmeric
-
additional information
HO-1 is inducible in response to a variety of chemical and physical stress conditions to function as a cytoprotective molecule, hemin and cadmium chloride-mediated HO-1 induction, overview
-
additional information
-
the enzyme activity is positively correlated with nitric oxide and cGMP levels in cavernous tissue, overview
-
additional information
the HO-1 gene is transcriptionally induced by the phorbol ester PMA, mediated via a newly identified kappaB element of the proximal rat HO-1 gene promoter region, overview
-
additional information
simvastatin induces the enzyme in neurons, HO-1 upregulation is significantly associated with increased nuclear factor kappa B activation, manifested as IkappaBalpha phosphorylation and p65 nuclear translocation, as well as increased production of superoxides, inhibition of the effects by zinc protoporphyrin
-
additional information
-
no significant changes in HO-1 mRNA levels between ethanol treated and pair-fed control
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.006
heme
-
recombinant heme oxygenase-1/cytochrome P450 reductase fusion protein
0.9
[reduced cytochrome P450 reductase]
mutant R87A, pH 8.0, 37°C
-
2.3
[reduced cytochrome P450 reductase]
mutant L201A, pH 8.0, 37°C
-
15.2
[reduced cytochrome P450 reductase]
mutant K169A, pH 8.0, 37°C
-
21.7
[reduced cytochrome P450 reductase]
mutant K149A, pH 8.0, 37°C
-
0.00177
[reduced NADPH-hemoprotein reductase]
-
wild-type, pH 7.5, 25°C
0.00271
[reduced NADPH-hemoprotein reductase]
-
mutant F157I, pH 7.5, 25°C
additional information
additional information
Michaelis-Menten kinetics, overview
-
additional information
additional information
-
Michaelis-Menten kinetics, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00006
(+-)-1-(1H-imidazol-1-yl)-4-(4-iodophenyl)-2-butanol hydrochloride
Rattus norvegicus
-
IC50: 0.00006 mM
0.0062
(+-)-1-(1H-imidazol-1-yl)-4-phenyl-2-butanol hydrochloride
Rattus norvegicus
-
IC50: 0.0062 mM
0.00014
(+-)-4-(4-bromophenyl)-1-(1H-imidazol-1-yl)-2-butanol hydrochloride
Rattus norvegicus
-
IC50: 0.00014 mM
0.0005
(+-)-4-(4-chlorophenyl)-1-(1H-imidazol-1-yl)-2-butanol hydrochloride
Rattus norvegicus
-
IC50: 0.0005 mM
0.0014
(+-)-4-(4-fluorophenyl)-1-(1H-imidazol-1-yl)-2-butanol hydrochloride
Rattus norvegicus
-
IC50: 0.0014 mM
0.00173 - 0.0033
(2R,4R)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-(methoxymethyl)-1,3-dioxolane hydrochloride monohydrate
0.00059 - 0.0016
(2R,4R)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-(phenoxymethyl)-1,3-dioxolane hydrochloride
0.0008 - 0.0015
(2R,4R)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-methyl-1,3-dioxolane
0.01 - 0.026
(2R,4R)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane dihydrochloride dihydrate
0.009 - 0.015
(2R,4R)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-[(4-iodophenoxy)methyl]-1,3-dioxolane hydrochloride
0.00133 - 0.019
(2R,4R)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-[(4-methoxyphenoxy)methyl]-1,3-dioxolane hydrochloride
0.012 - 0.1
(2R,4R)-2-[2-(4-chlorophenyl)ethyl]-4-(hydroxymethyl)-2-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane hydrochloride
0.00067 - 0.0017
(2R,4R)-2-[2-(4-chlorophenyl)ethyl]-4-[(4-cyanophenoxy)methyl]-2-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane hydrochloride
0.00028 - 0.0005
(2R,4R)-2-[2-(4-chlorophenyl)ethyl]-4-[(4-fluorophenoxy)methyl]-2-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane hydrochloride
0.0018 - 0.0071
(2R,4R)-2-[2-(4-chlorophenyl)ethyl]-4-[(4-hydroxyphenoxy)methyl]-2-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane hydrochloride
0.0036 - 0.038
(2R,4R)-4-(azidomethyl)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane
0.1
(2R,4R)-4-[((4-adamantan-1-yl)phenoxy)methyl]-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane hydrochloride
0.0014 - 0.013
(2R,4R)-4-[(4-aminophenoxy)methyl]-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane dihydrochloride
0.0035 - 0.022
(2R,4R)-4-[(4-bromophenoxy)methyl]-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane hydrochloride
0.002 - 0.043
(2R,4R)-4-[(biphenyl-4-yloxy)methyl]-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane hydrochloride
0.0026
(2R,4S)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)-methyl]-4-methyl-1,3-dioxolane
Rattus norvegicus
-
IC50: 0.0026 mM
0.0021 - 0.016
(2R,4S)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-[((5-trifluoromethyl)pyridin-2-ylsulfanyl)methyl]-1,3-dioxolane hydrochloride
0.0021
(2R,4S)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-[((5-trifluoromethylpyridin-2-yl)thio)methyl]-1,3-dioxolane
0.0007 - 0.0025
(2R,4S)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-[(4-methoxyphenylsulfanyl)methyl]-1,3-dioxolane hydrochloride
0.006 - 0.019
(2R,4S)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-[(4-nitrophenylsulfanyl)methyl]-1,3-dioxolane hydrochloride
0.009 - 0.019
(2R,4S)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-[(methylthio)methyl]-1,3-dioxolane hydrochloride
0.0009 - 0.03
(2R,4S)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-[(naphthalen-2-ylsulfanyl)methyl]-1,3-dioxolane hydrochloride
0.00103 - 0.034
(2R,4S)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-[(phenylsulfanyl)methyl]-1,3-dioxolane hydrochloride
0.025 - 0.069
(2R,4S)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-[(pyridin-4-ylsulfanyl)methyl]-1,3-dioxolane dihydrochloride
0.0012 - 0.0044
(2R,4S)-2-[2-(4-chlorophenyl)ethyl]-4-(fluoromethyl)-2-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane hydrochloride
0.0028 - 0.012
(2R,4S)-2-[2-(4-chlorophenyl)ethyl]-4-[(4-chlorophenylsulfanyl)methyl]-2-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane hydrochloride
0.0022 - 0.005
(2R,4S)-2-[2-(4-chlorophenyl)ethyl]-4-[(4-fluorophenylsulfanyl)methyl]-2-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane hydrochloride
0.0035 - 0.122
(2R,4S)-4-(chloromethyl)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane hydrochloride monohydrate
0.006 - 0.0123
(2R,4S)-4-[(2-bromophenylsulfanyl)methyl]-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane hydrochloride
0.005 - 0.022
(2R,4S)-4-[(3-bromophenylsulfanyl)methyl]-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane hydrochloride
0.0021 - 0.0024
(2R,4S)-4-[(4-bromophenylsulfanyl)methyl]-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane hydrochloride
0.02
(2S,4R)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)-methyl]-4-methyl-1,3-dioxolane
Rattus norvegicus
-
IC50: 0.02 mM
0.012
(2S,4S)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-methyl-1,3-dioxolane
Rattus norvegicus
-
IC50: 0.012 mM
0.0019 - 100
1-((2-(2-(4-bromophenyl)ethyl)-1,3-dioxolan-2-yl)methyl)-1H-imidazole hydrochloride
0.0043 - 100
1-((2-(2-(4-chlorophenyl)ethyl)-1,3-dioxolan-2-yl)methyl)-1H-imidazole hydrochloride
0.0038 - 100
1-((2-(2-(4-fluorophenyl)ethyl)-1,3-dioxolan-2-yl)methyl)-1H-imidazole hydrochloride
0.0037 - 100
1-((2-(2-(4-iodophenyl)ethyl)-1,3-dioxolan-2-yl)methyl)-1H-imidazole hydrochloride
0.00027
1-(1H-imidazol-1-yl)-4,4-diphenyl-2-butanone
Homo sapiens
pH and temperature not specified in the publication
0.1
1-(4-bromophenyl)-2-[2-(1-methylethyl)-1H-imidazol-1-yl]ethanone
Rattus norvegicus
pH 7.4, 37°C
0.1
2-(norborn-2-yl)methyl-1H-benzimidazole
Rattus norvegicus
-
IC50 above 0.1 mM, isoform HO-1, at pH 7.4 and 37°C
0.00014
2-[2-(4-bromophenyl)ethyl]-2-[(1H-imidazol-1-yl) methyl]-1,3-dioxolane
Homo sapiens
pH and temperature not specified in the publication
0.0005
2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl) methyl]-1,3-dioxolane
Homo sapiens
pH and temperature not specified in the publication
0.004
2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane
Rattus norvegicus
-
IC50: 0.004 mM
0.0047
2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-1,3-dithiolane
Rattus norvegicus
-
IC50: 0.0047 mM
0.0014
2-[2-(4-fluorophenyl)ethyl]-2-[(1H-imidazol-1-yl) methyl]-1,3-dioxolane
Homo sapiens
pH and temperature not specified in the publication
0.0062
2-[2-phenylethyl]-2-[(1H-imidazol-1-yl) methyl]-1,3-dioxolane
Homo sapiens
pH and temperature not specified in the publication
0.00076
2-[2-phenylethyl]-2-[(1H-imidazol-1-yl)methyl]1,3-dioxolane
Homo sapiens
pH and temperature not specified in the publication
0.00406
4-phenyl-1-(1H-imidazol-1-yl)-2-butanone
Homo sapiens
pH and temperature not specified in the publication
0.06
(+/-)-1-(1H-imidazol-1-yl)-4-(4-iodophenyl)-2-butanol hydrochloride
Rattus norvegicus
-
pH 7.4, 37°C, spleen isozyme HO-1
1.8
(+/-)-1-(1H-imidazol-1-yl)-4-(4-iodophenyl)-2-butanol hydrochloride
Rattus norvegicus
-
pH 7.4, 37°C, brain isozyme HO-2
6.2
(+/-)-1-(1H-imidazol-1-yl)-4-phenyl-2-butanol hydrochloride
Rattus norvegicus
-
pH 7.4, 37°C, spleen isozyme HO-1
16
(+/-)-1-(1H-imidazol-1-yl)-4-phenyl-2-butanol hydrochloride
Rattus norvegicus
-
pH 7.4, 37°C, brain isozyme HO-2
0.14
(+/-)-4-(4-bromophenyl)-1-(1H-imidazol-1-yl)-2-butanol hydrochloride
Rattus norvegicus
-
pH 7.4, 37°C, spleen isozyme HO-1
2.6
(+/-)-4-(4-bromophenyl)-1-(1H-imidazol-1-yl)-2-butanol hydrochloride
Rattus norvegicus
-
pH 7.4, 37°C, brain isozyme HO-2
0.5
(+/-)-4-(4-chlorophenyl)-1-(1H-imidazol-1-yl)-2-butanol hydrochloride
Rattus norvegicus
-
pH 7.4, 37°C, spleen isozyme HO-1
4
(+/-)-4-(4-chlorophenyl)-1-(1H-imidazol-1-yl)-2-butanol hydrochloride
Rattus norvegicus
-
pH 7.4, 37°C, brain isozyme HO-2
0.00006
(2-[2-(4-chlorophenyl)ethyl]-2-[1H-imidazol-1-yl)methyl]-1,3-dioxolane
Rattus norvegicus
substitution of the chlorophenyl group in the western region to a iodophenyl group
0.00014
(2-[2-(4-chlorophenyl)ethyl]-2-[1H-imidazol-1-yl)methyl]-1,3-dioxolane
Rattus norvegicus
substitution of the chlorophenyl group in the western region to a bromophenyl group
0.0014
(2-[2-(4-chlorophenyl)ethyl]-2-[1H-imidazol-1-yl)methyl]-1,3-dioxolane
Rattus norvegicus
substitution of the chlorophenyl group in the western region to a fluorophenyl group
0.004
(2-[2-(4-chlorophenyl)ethyl]-2-[1H-imidazol-1-yl)methyl]-1,3-dioxolane
Rattus norvegicus
-
0.0062
(2-[2-(4-chlorophenyl)ethyl]-2-[1H-imidazol-1-yl)methyl]-1,3-dioxolane
Rattus norvegicus
substitution of the chlorophenyl group in the western region to a phenyl group
0.00173
(2R,4R)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-(methoxymethyl)-1,3-dioxolane hydrochloride monohydrate
Rattus norvegicus
-
HO-1
0.0033
(2R,4R)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-(methoxymethyl)-1,3-dioxolane hydrochloride monohydrate
Rattus norvegicus
-
HO-2
0.00059
(2R,4R)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-(phenoxymethyl)-1,3-dioxolane hydrochloride
Rattus norvegicus
-
HO-1
0.0016
(2R,4R)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-(phenoxymethyl)-1,3-dioxolane hydrochloride
Rattus norvegicus
-
HO-2
0.0008
(2R,4R)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-methyl-1,3-dioxolane
Rattus norvegicus
-
IC50: 0.0008 mM
0.0015
(2R,4R)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-methyl-1,3-dioxolane
Homo sapiens
-
IC50: 0.0015 mM
0.01
(2R,4R)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane dihydrochloride dihydrate
Rattus norvegicus
-
HO-1
0.026
(2R,4R)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane dihydrochloride dihydrate
Rattus norvegicus
-
HO-2
0.009
(2R,4R)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-[(4-iodophenoxy)methyl]-1,3-dioxolane hydrochloride
Rattus norvegicus
-
HO-1
0.015
(2R,4R)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-[(4-iodophenoxy)methyl]-1,3-dioxolane hydrochloride
Rattus norvegicus
-
HO-2
0.00133
(2R,4R)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-[(4-methoxyphenoxy)methyl]-1,3-dioxolane hydrochloride
Rattus norvegicus
-
HO-1
0.019
(2R,4R)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-[(4-methoxyphenoxy)methyl]-1,3-dioxolane hydrochloride
Rattus norvegicus
-
HO-2
0.012
(2R,4R)-2-[2-(4-chlorophenyl)ethyl]-4-(hydroxymethyl)-2-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane hydrochloride
Rattus norvegicus
-
HO-1
0.1
(2R,4R)-2-[2-(4-chlorophenyl)ethyl]-4-(hydroxymethyl)-2-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane hydrochloride
Rattus norvegicus
-
HO-2
0.00067
(2R,4R)-2-[2-(4-chlorophenyl)ethyl]-4-[(4-cyanophenoxy)methyl]-2-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane hydrochloride
Rattus norvegicus
-
HO-1
0.0017
(2R,4R)-2-[2-(4-chlorophenyl)ethyl]-4-[(4-cyanophenoxy)methyl]-2-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane hydrochloride
Rattus norvegicus
-
HO-2
0.00028
(2R,4R)-2-[2-(4-chlorophenyl)ethyl]-4-[(4-fluorophenoxy)methyl]-2-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane hydrochloride
Rattus norvegicus
-
HO-1
0.0005
(2R,4R)-2-[2-(4-chlorophenyl)ethyl]-4-[(4-fluorophenoxy)methyl]-2-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane hydrochloride
Rattus norvegicus
-
HO-2
0.0018
(2R,4R)-2-[2-(4-chlorophenyl)ethyl]-4-[(4-hydroxyphenoxy)methyl]-2-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane hydrochloride
Rattus norvegicus
-
HO-1
0.0071
(2R,4R)-2-[2-(4-chlorophenyl)ethyl]-4-[(4-hydroxyphenoxy)methyl]-2-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane hydrochloride
Rattus norvegicus
-
HO-2
0.0036
(2R,4R)-4-(azidomethyl)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane
Rattus norvegicus
-
HO-1
0.038
(2R,4R)-4-(azidomethyl)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane
Rattus norvegicus
-
HO-2
0.1
(2R,4R)-4-[((4-adamantan-1-yl)phenoxy)methyl]-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane hydrochloride
Rattus norvegicus
-
HO-1
0.1
(2R,4R)-4-[((4-adamantan-1-yl)phenoxy)methyl]-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane hydrochloride
Rattus norvegicus
-
HO-2
0.0014
(2R,4R)-4-[(4-aminophenoxy)methyl]-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane dihydrochloride
Rattus norvegicus
-
HO-1
0.013
(2R,4R)-4-[(4-aminophenoxy)methyl]-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane dihydrochloride
Rattus norvegicus
-
HO-2
0.0035
(2R,4R)-4-[(4-bromophenoxy)methyl]-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane hydrochloride
Rattus norvegicus
-
HO-1
0.022
(2R,4R)-4-[(4-bromophenoxy)methyl]-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane hydrochloride
Rattus norvegicus
-
HO-2
0.002
(2R,4R)-4-[(biphenyl-4-yloxy)methyl]-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane hydrochloride
Rattus norvegicus
-
HO-1
0.043
(2R,4R)-4-[(biphenyl-4-yloxy)methyl]-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane hydrochloride
Rattus norvegicus
-
HO-2
0.0021
(2R,4S)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-[((5-trifluoromethyl)pyridin-2-ylsulfanyl)methyl]-1,3-dioxolane hydrochloride
Rattus norvegicus
-
HO-1
0.016
(2R,4S)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-[((5-trifluoromethyl)pyridin-2-ylsulfanyl)methyl]-1,3-dioxolane hydrochloride
Rattus norvegicus
-
HO-2
0.0021
(2R,4S)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-[((5-trifluoromethylpyridin-2-yl)thio)methyl]-1,3-dioxolane
Homo sapiens
-
0.0021
(2R,4S)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-[((5-trifluoromethylpyridin-2-yl)thio)methyl]-1,3-dioxolane
Homo sapiens
pH and temperature not specified in the publication
0.0007
(2R,4S)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-[(4-methoxyphenylsulfanyl)methyl]-1,3-dioxolane hydrochloride
Rattus norvegicus
-
HO-1
0.0025
(2R,4S)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-[(4-methoxyphenylsulfanyl)methyl]-1,3-dioxolane hydrochloride
Rattus norvegicus
-
HO-2
0.006
(2R,4S)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-[(4-nitrophenylsulfanyl)methyl]-1,3-dioxolane hydrochloride
Rattus norvegicus
-
HO-1
0.019
(2R,4S)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-[(4-nitrophenylsulfanyl)methyl]-1,3-dioxolane hydrochloride
Rattus norvegicus
-
HO-2
0.009
(2R,4S)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-[(methylthio)methyl]-1,3-dioxolane hydrochloride
Rattus norvegicus
-
HO-1
0.019
(2R,4S)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-[(methylthio)methyl]-1,3-dioxolane hydrochloride
Rattus norvegicus
-
HO-2
0.0009
(2R,4S)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-[(naphthalen-2-ylsulfanyl)methyl]-1,3-dioxolane hydrochloride
Rattus norvegicus
-
HO-1
0.03
(2R,4S)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-[(naphthalen-2-ylsulfanyl)methyl]-1,3-dioxolane hydrochloride
Rattus norvegicus
-
HO-2
0.00103
(2R,4S)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-[(phenylsulfanyl)methyl]-1,3-dioxolane hydrochloride
Rattus norvegicus
-
HO-1
0.034
(2R,4S)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-[(phenylsulfanyl)methyl]-1,3-dioxolane hydrochloride
Rattus norvegicus
-
HO-2
0.025
(2R,4S)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-[(pyridin-4-ylsulfanyl)methyl]-1,3-dioxolane dihydrochloride
Rattus norvegicus
-
HO-1
0.069
(2R,4S)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-[(pyridin-4-ylsulfanyl)methyl]-1,3-dioxolane dihydrochloride
Rattus norvegicus
-
HO-2
0.0012
(2R,4S)-2-[2-(4-chlorophenyl)ethyl]-4-(fluoromethyl)-2-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane hydrochloride
Rattus norvegicus
-
HO-1
0.0044
(2R,4S)-2-[2-(4-chlorophenyl)ethyl]-4-(fluoromethyl)-2-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane hydrochloride
Rattus norvegicus
-
HO-2
0.0028
(2R,4S)-2-[2-(4-chlorophenyl)ethyl]-4-[(4-chlorophenylsulfanyl)methyl]-2-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane hydrochloride
Rattus norvegicus
-
HO-1
0.012
(2R,4S)-2-[2-(4-chlorophenyl)ethyl]-4-[(4-chlorophenylsulfanyl)methyl]-2-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane hydrochloride
Rattus norvegicus
-
HO-2
0.0022
(2R,4S)-2-[2-(4-chlorophenyl)ethyl]-4-[(4-fluorophenylsulfanyl)methyl]-2-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane hydrochloride
Rattus norvegicus
-
HO-1
0.005
(2R,4S)-2-[2-(4-chlorophenyl)ethyl]-4-[(4-fluorophenylsulfanyl)methyl]-2-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane hydrochloride
Rattus norvegicus
-
HO-2
0.0035
(2R,4S)-4-(chloromethyl)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane hydrochloride monohydrate
Rattus norvegicus
-
HO-1
0.122
(2R,4S)-4-(chloromethyl)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane hydrochloride monohydrate
Rattus norvegicus
-
HO-2
0.006
(2R,4S)-4-[(2-bromophenylsulfanyl)methyl]-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane hydrochloride
Rattus norvegicus
-
HO-1
0.0123
(2R,4S)-4-[(2-bromophenylsulfanyl)methyl]-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane hydrochloride
Rattus norvegicus
-
HO-2
0.005
(2R,4S)-4-[(3-bromophenylsulfanyl)methyl]-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane hydrochloride
Rattus norvegicus
-
HO-1
0.022
(2R,4S)-4-[(3-bromophenylsulfanyl)methyl]-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane hydrochloride
Rattus norvegicus
-
HO-2
0.0021
(2R,4S)-4-[(4-bromophenylsulfanyl)methyl]-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane hydrochloride
Rattus norvegicus
-
HO-1
0.0024
(2R,4S)-4-[(4-bromophenylsulfanyl)methyl]-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane hydrochloride
Rattus norvegicus
-
HO-2
0.0019
1-((2-(2-(4-bromophenyl)ethyl)-1,3-dioxolan-2-yl)methyl)-1H-imidazole hydrochloride
Rattus norvegicus
-
IC50: 0.0019 mM
1.9
1-((2-(2-(4-bromophenyl)ethyl)-1,3-dioxolan-2-yl)methyl)-1H-imidazole hydrochloride
Rattus norvegicus
-
pH 7.4, 37°C, spleen isozyme HO-1
100
1-((2-(2-(4-bromophenyl)ethyl)-1,3-dioxolan-2-yl)methyl)-1H-imidazole hydrochloride
Rattus norvegicus
-
above, pH 7.4, 37°C, brain isozyme HO-2
0.0043
1-((2-(2-(4-chlorophenyl)ethyl)-1,3-dioxolan-2-yl)methyl)-1H-imidazole hydrochloride
Rattus norvegicus
-
IC50: 0.0043 mM
1.4
1-((2-(2-(4-chlorophenyl)ethyl)-1,3-dioxolan-2-yl)methyl)-1H-imidazole hydrochloride
Rattus norvegicus
-
pH 7.4, 37°C, spleen isozyme HO-1
4.3
1-((2-(2-(4-chlorophenyl)ethyl)-1,3-dioxolan-2-yl)methyl)-1H-imidazole hydrochloride
Rattus norvegicus
-
pH 7.4, 37°C, spleen isozyme HO-1
17.9
1-((2-(2-(4-chlorophenyl)ethyl)-1,3-dioxolan-2-yl)methyl)-1H-imidazole hydrochloride
Rattus norvegicus
-
pH 7.4, 37°C, brain isozyme HO-2
100
1-((2-(2-(4-chlorophenyl)ethyl)-1,3-dioxolan-2-yl)methyl)-1H-imidazole hydrochloride
Rattus norvegicus
-
above, pH 7.4, 37°C, brain isozyme HO-2
0.0038
1-((2-(2-(4-fluorophenyl)ethyl)-1,3-dioxolan-2-yl)methyl)-1H-imidazole hydrochloride
Rattus norvegicus
-
IC50: 0.0038 mM
3.8
1-((2-(2-(4-fluorophenyl)ethyl)-1,3-dioxolan-2-yl)methyl)-1H-imidazole hydrochloride
Rattus norvegicus
-
pH 7.4, 37°C, spleen isozyme HO-1
100
1-((2-(2-(4-fluorophenyl)ethyl)-1,3-dioxolan-2-yl)methyl)-1H-imidazole hydrochloride
Rattus norvegicus
-
above, pH 7.4, 37°C, brain isozyme HO-2
0.0037
1-((2-(2-(4-iodophenyl)ethyl)-1,3-dioxolan-2-yl)methyl)-1H-imidazole hydrochloride
Rattus norvegicus
-
IC50: 0.0037 mM
3.7
1-((2-(2-(4-iodophenyl)ethyl)-1,3-dioxolan-2-yl)methyl)-1H-imidazole hydrochloride
Rattus norvegicus
-
pH 7.4, 37°C, spleen isozyme HO-1
100
1-((2-(2-(4-iodophenyl)ethyl)-1,3-dioxolan-2-yl)methyl)-1H-imidazole hydrochloride
Rattus norvegicus
-
above, pH 7.4, 37°C, brain isozyme HO-2
0.0007
1-((2-(2-phenylethyl)-1,3-dioxolan-2-yl)methyl)-1H-imidazole hydrochloride
Rattus norvegicus
-
IC50: 0.0007 mM
0.7
1-((2-(2-phenylethyl)-1,3-dioxolan-2-yl)methyl)-1H-imidazole hydrochloride
Rattus norvegicus
-
pH 7.4, 37°C, spleen isozyme HO-1
100
1-((2-(2-phenylethyl)-1,3-dioxolan-2-yl)methyl)-1H-imidazole hydrochloride
Rattus norvegicus
-
above, pH 7.4, 37°C, brain isozyme HO-2
0.00011
1-(1H-imidazol-1-yl)-4-(4-iodophenyl)-2-butanone hydrochloride
Rattus norvegicus
-
IC50: 0.00011 mM
0.11
1-(1H-imidazol-1-yl)-4-(4-iodophenyl)-2-butanone hydrochloride
Rattus norvegicus
-
pH 7.4, 37°C, spleen isozyme HO-1
1.8
1-(1H-imidazol-1-yl)-4-(4-iodophenyl)-2-butanone hydrochloride
Rattus norvegicus
-
pH 7.4, 37°C, brain isozyme HO-2
0.004
1-(1H-imidazol-1-yl)-4-phenyl-2-butanone hydrochloride
Rattus norvegicus
-
IC50: 0.004 mM
4
1-(1H-imidazol-1-yl)-4-phenyl-2-butanone hydrochloride
Rattus norvegicus
-
pH 7.4, 37°C, spleen isozyme HO-1
11.3
1-(1H-imidazol-1-yl)-4-phenyl-2-butanone hydrochloride
Rattus norvegicus
-
pH 7.4, 37°C, brain isozyme HO-2
0.0027
1-(4-bromobenzyl)-2-(1H-imidazol-1-yl)methyl-1H-benzimidazole
Rattus norvegicus
-
isoform HO-1, at pH 7.4 and 37°C
0.0042
1-(4-bromobenzyl)-2-(1H-imidazol-1-yl)methyl-1H-benzimidazole
Rattus norvegicus
-
isoform HO-2, at pH 7.4 and 37°C
0.0301
1-(4-bromobenzyl)-2-(N-morpholinyl)methyl-1H-benzimidazole
Rattus norvegicus
-
isoform HO-2, at pH 7.4 and 37°C
0.1
1-(4-bromobenzyl)-2-(N-morpholinyl)methyl-1H-benzimidazole
Rattus norvegicus
-
IC50 above 0.1 mM, isoform HO-1, at pH 7.4 and 37°C
0.0051
1-(4-bromobenzyl)-2-(norborn-2-yl)methyl-1H-benzimidazole
Rattus norvegicus
-
isoform HO-2, at pH 7.4 and 37°C
0.1
1-(4-bromobenzyl)-2-(norborn-2-yl)methyl-1H-benzimidazole
Rattus norvegicus
-
IC50 above 0.1 mM, isoform HO-1, at pH 7.4 and 37°C
0.0084
1-(4-bromobenzyl)-2-cyclopentylmethyl-1H-benzimidazole
Rattus norvegicus
-
isoform HO-2, at pH 7.4 and 37°C
0.0756
1-(4-bromobenzyl)-2-cyclopentylmethyl-1H-benzimidazole
Rattus norvegicus
-
isoform HO-1, at pH 7.4 and 37°C
0.0053
1-(4-chlorobenzyl)-2-(1H-imidazol-1-yl)methyl-1H-benzimidazole
Rattus norvegicus
-
isoform HO-1, at pH 7.4 and 37°C
0.0085
1-(4-chlorobenzyl)-2-(1H-imidazol-1-yl)methyl-1H-benzimidazole
Rattus norvegicus
-
isoform HO-2, at pH 7.4 and 37°C
0.0043
1-(4-chlorobenzyl)-2-(2-norbornylmethyl)-1H-benzimidazole
Rattus norvegicus
-
isoform HO-2, at pH 7.4 and 37°C
0.1
1-(4-chlorobenzyl)-2-(2-norbornylmethyl)-1H-benzimidazole
Rattus norvegicus
-
IC50 above 0.1 mM, isoform HO-1, at pH 7.4 and 37°C
0.0319
1-(4-chlorobenzyl)-2-(N-morpholinyl)methyl-1H-benzimidazole
Rattus norvegicus
-
isoform HO-2, at pH 7.4 and 37°C
0.1
1-(4-chlorobenzyl)-2-(N-morpholinyl)methyl-1H-benzimidazole
Rattus norvegicus
-
IC50 above 0.1 mM, isoform HO-1, at pH 7.4 and 37°C
0.0033
1-(4-chlorobenzyl)-2-cyclopentylmethyl-1H-benzimidazole
Rattus norvegicus
-
isoform HO-2, at pH 7.4 and 37°C
0.0324
1-(4-chlorobenzyl)-2-cyclopentylmethyl-1H-benzimidazole
Rattus norvegicus
-
isoform HO-1, at pH 7.4 and 37°C
0.1
1-(4-methylbenzyl)-2-(N-morpholinyl)methyl-1H-benzimidazole
Rattus norvegicus
-
IC50 above 0.1 mM, isoform HO-1, at pH 7.4 and 37°C
0.1
1-(4-methylbenzyl)-2-(N-morpholinyl)methyl-1H-benzimidazole
Rattus norvegicus
-
IC50 above 0.1 mM, isoform HO-2, at pH 7.4 and 37°C
0.0112
1-(4-methylbenzyl)-2-(norborn-2-yl)methyl-1H-benzimidazole
Rattus norvegicus
-
isoform HO-2, at pH 7.4 and 37°C
0.1
1-(4-methylbenzyl)-2-(norborn-2-yl)methyl-1H-benzimidazole
Rattus norvegicus
-
IC50 above 0.1 mM, isoform HO-1, at pH 7.4 and 37°C
0.0509
1-(n-heptyl)-2-(norborn-2-yl)methyl-1H-benzimidazole
Rattus norvegicus
-
isoform HO-2, at pH 7.4 and 37°C
0.1
1-(n-heptyl)-2-(norborn-2-yl)methyl-1H-benzimidazole
Rattus norvegicus
-
IC50 above 0.1 mM, isoform HO-1, at pH 7.4 and 37°C
0.0173
1-(n-hexyl)-2-(norborn-2-yl)methyl-1H-benzimidazole
Rattus norvegicus
-
isoform HO-2, at pH 7.4 and 37°C
0.1
1-(n-hexyl)-2-(norborn-2-yl)methyl-1H-benzimidazole
Rattus norvegicus
-
IC50 above 0.1 mM, isoform HO-1, at pH 7.4 and 37°C
0.0073
1-benzyl-2-(1H-imidazol-1-yl)methyl-1H-benzimidazole
Rattus norvegicus
-
isoform HO-1, at pH 7.4 and 37°C
0.0499
1-benzyl-2-(1H-imidazol-1-yl)methyl-1H-benzimidazole
Rattus norvegicus
-
isoform HO-2, at pH 7.4 and 37°C
0.0643
1-benzyl-2-(N-morpholinyl)methyl-1H-benzimidazole
Rattus norvegicus
-
isoform HO-2, at pH 7.4 and 37°C
0.1
1-benzyl-2-(N-morpholinyl)methyl-1H-benzimidazole
Rattus norvegicus
-
IC50 above 0.1 mM, isoform HO-1, at pH 7.4 and 37°C
0.0063
1-benzyl-2-(norborn-2-yl)methyl-1H-benzimidazole
Rattus norvegicus
-
isoform HO-2, at pH 7.4 and 37°C
0.1
1-benzyl-2-(norborn-2-yl)methyl-1H-benzimidazole
Rattus norvegicus
-
IC50 above 0.1 mM, isoform HO-1, at pH 7.4 and 37°C
0.0103
1-benzyl-2-cyclohexylmethyl-1H-benzimidazole hydrochloride
Rattus norvegicus
-
isoform HO-2, at pH 7.4 and 37°C
0.1
1-benzyl-2-cyclohexylmethyl-1H-benzimidazole hydrochloride
Rattus norvegicus
-
IC50 above 0.1 mM, isoform HO-1, at pH 7.4 and 37°C
0.0054
1-bromobenzyl-2-cyclohexylmethyl-1H-benzimidazole
Rattus norvegicus
-
isoform HO-2, at pH 7.4 and 37°C
0.1
1-bromobenzyl-2-cyclohexylmethyl-1H-benzimidazole
Rattus norvegicus
-
IC50 above 0.1 mM, isoform HO-1, at pH 7.4 and 37°C
0.0054
1-chlorobenzyl-2-cyclohexylmethyl-1H-benzimidazole
Rattus norvegicus
-
isoform HO-2, at pH 7.4 and 37°C
0.1
1-chlorobenzyl-2-cyclohexylmethyl-1H-benzimidazole
Rattus norvegicus
-
IC50 above 0.1 mM, isoform HO-1, at pH 7.4 and 37°C
0.1
2-(1-cyclopentylmethyl)-1-(n-decyl)-1H-benzimidazole
Rattus norvegicus
-
IC50 above 0.1 mM, isoform HO-1, at pH 7.4 and 37°C
0.1
2-(1-cyclopentylmethyl)-1-(n-decyl)-1H-benzimidazole
Rattus norvegicus
-
IC50 above 0.1 mM, isoform HO-2, at pH 7.4 and 37°C
0.1
2-(1-cyclopentylmethyl)-1-(n-heptyl)-1H-benzimidazole
Rattus norvegicus
-
IC50 above 0.1 mM, isoform HO-1, at pH 7.4 and 37°C
0.1
2-(1-cyclopentylmethyl)-1-(n-heptyl)-1H-benzimidazole
Rattus norvegicus
-
IC50 above 0.1 mM, isoform HO-2, at pH 7.4 and 37°C
0.0363
2-(1-cyclopentylmethyl)-1-(n-hexyl)-1H-benzimidazole
Rattus norvegicus
-
isoform HO-2, at pH 7.4 and 37°C
0.1
2-(1-cyclopentylmethyl)-1-(n-hexyl)-1H-benzimidazole
Rattus norvegicus
-
IC50 above 0.1 mM, isoform HO-1, at pH 7.4 and 37°C
0.1
2-(1-cyclopentylmethyl)-1-(n-octadecyl)-1H-benzimidazole
Rattus norvegicus
-
IC50 above 0.1 mM, isoform HO-1, at pH 7.4 and 37°C
0.1
2-(1-cyclopentylmethyl)-1-(n-octadecyl)-1H-benzimidazole
Rattus norvegicus
-
IC50 above 0.1 mM, isoform HO-2, at pH 7.4 and 37°C
0.0044
2-(1H-imidazol-1-yl)methyl-1-(4-methylbenzyl)-1H-benzimidazole
Rattus norvegicus
-
isoform HO-1, at pH 7.4 and 37°C
0.0079
2-(1H-imidazol-1-yl)methyl-1-(4-methylbenzyl)-1H-benzimidazole
Rattus norvegicus
-
isoform HO-2, at pH 7.4 and 37°C
0.0475
2-(1H-imidazol-1-yl)methyl-1H-benzimidazole
Rattus norvegicus
-
isoform HO-1, at pH 7.4 and 37°C
0.1
2-(1H-imidazol-1-yl)methyl-1H-benzimidazole
Rattus norvegicus
-
IC50 above 0.1 mM, isoform HO-2, at pH 7.4 and 37°C
0.1
2-(N-morpholinyl)methyl-1H-benzimidazole
Rattus norvegicus
-
IC50 above 0.1 mM, isoform HO-1, at pH 7.4 and 37°C
0.1
2-(N-morpholinyl)methyl-1H-benzimidazole
Rattus norvegicus
-
IC50 above 0.1 mM, isoform HO-2, at pH 7.4 and 37°C
0.0174
2-cyclohexylmethyl-1-(4-methylbenzyl)-1H-benzimidazole
Rattus norvegicus
-
isoform HO-1, at pH 7.4 and 37°C
0.1
2-cyclohexylmethyl-1-(4-methylbenzyl)-1H-benzimidazole
Rattus norvegicus
-
IC50 above 0.1 mM, isoform HO-1, at pH 7.4 and 37°C
0.1
2-cyclohexylmethyl-1-(n-decyl)-1H-benzimidazole
Rattus norvegicus
-
IC50 above 0.1 mM, isoform HO-1, at pH 7.4 and 37°C
0.1
2-cyclohexylmethyl-1-(n-decyl)-1H-benzimidazole
Rattus norvegicus
-
IC50 above 0.1 mM, isoform HO-2, at pH 7.4 and 37°C
0.0572
2-cyclohexylmethyl-1-(n-heptyl)-1H-benzimidazole
Rattus norvegicus
-
isoform HO-2, at pH 7.4 and 37°C
0.1
2-cyclohexylmethyl-1-(n-heptyl)-1H-benzimidazole
Rattus norvegicus
-
IC50 above 0.1 mM, isoform HO-1, at pH 7.4 and 37°C
0.0223
2-cyclohexylmethyl-1-(n-hexyl)-1H-benzimidazole
Rattus norvegicus
-
isoform HO-2, at pH 7.4 and 37°C
0.1
2-cyclohexylmethyl-1-(n-hexyl)-1H-benzimidazole
Rattus norvegicus
-
IC50 above 0.1 mM, isoform HO-1, at pH 7.4 and 37°C
0.1
2-cyclohexylmethyl-1H-benzimidazole
Rattus norvegicus
-
IC50 above 0.1 mM, isoform HO-1, at pH 7.4 and 37°C
0.1
2-cyclohexylmethyl-1H-benzimidazole
Rattus norvegicus
-
IC50 above 0.1 mM, isoform HO-2, at pH 7.4 and 37°C
0.0086
2-cyclopentylmethyl-1-(4-methylbenzyl)-1H-benzimidazole
Rattus norvegicus
-
isoform HO-2, at pH 7.4 and 37°C
0.0181
2-cyclopentylmethyl-1-(4-methylbenzyl)-1H-benzimidazole
Rattus norvegicus
-
isoform HO-1, at pH 7.4 and 37°C
0.1
2-cyclopentylmethyl-1H-benzimidazole
Rattus norvegicus
-
IC50 above 0.1 mM, isoform HO-1, at pH 7.4 and 37°C
0.1
2-cyclopentylmethyl-1H-benzimidazole
Rattus norvegicus
-
IC50 above 0.1 mM, isoform HO-2, at pH 7.4 and 37°C
0.0017
4-(4-bromophenyl)-1-(1H-imidazol-1-yl)-2-butanone hydrochloride
Rattus norvegicus
-
IC50: 0.0017 mM
1.7
4-(4-bromophenyl)-1-(1H-imidazol-1-yl)-2-butanone hydrochloride
Rattus norvegicus
-
pH 7.4, 37°C, spleen isozyme HO-1
9.5
4-(4-bromophenyl)-1-(1H-imidazol-1-yl)-2-butanone hydrochloride
Rattus norvegicus
-
pH 7.4, 37°C, brain isozyme HO-2
0.0047
4-(4-chlorophenyl)-1-(1H-imidazol-1-yl)-2-butanone hydrochloride
Rattus norvegicus
-
IC50: 0.0047 mM
4.7
4-(4-chlorophenyl)-1-(1H-imidazol-1-yl)-2-butanone hydrochloride
Rattus norvegicus
-
pH 7.4, 37°C, spleen isozyme HO-1
43.1
4-(4-chlorophenyl)-1-(1H-imidazol-1-yl)-2-butanone hydrochloride
Rattus norvegicus
-
pH 7.4, 37°C, brain isozyme HO-2
0.0027
4-(4-fluorophenyl)-1-(1H-imidazol-1-yl)-2-butanone hydrochloride
Rattus norvegicus
-
IC50: 0.0027 mM
1.9
4-(4-fluorophenyl)-1-(1H-imidazol-1-yl)-2-butanone hydrochloride
Rattus norvegicus
-
pH 7.4, 37°C, brain isozyme HO-2
2.7
4-(4-fluorophenyl)-1-(1H-imidazol-1-yl)-2-butanone hydrochloride
Rattus norvegicus
-
pH 7.4, 37°C, spleen isozyme HO-1
0.0025
4-phenyl-1-(1,2,4-1H-triazol-1-yl)butan-2-one
Homo sapiens
pH and temperature not specified in the publication
0.089
4-phenyl-1-(1,2,4-1H-triazol-1-yl)butan-2-one
Homo sapiens
1,2,3-triazolyl variant
0.017
DTE
Homo sapiens
-
isozyme HO-1, pH not specified in the publication, temperature not specified in the publication
1.2
DTE
Homo sapiens
-
isozyme HO-2, pH not specified in the publication, temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.075 - 0.1
-
liver heme oxygenase from Co-treated animals, 2 fractions during purification
additional information
additional information
-
the specific HO-1 activity increases from 0.82 to 24.8 U/mg during purification steps
additional information
transcription factor activation activity of recombinant wild-type and mutant enzymes, overview
additional information
activity in nonexposed control and SnPP-IX/CCl4-exposed liver tissue, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
7.6
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
two types of isoforms: an inducible heme oxygenase-1, HO1, and a constitutive heme oxygenase-2/3, HO2/3
UniProt
brenda
heme oxygenase-1 is identical to the major 32000 Da mammalian stress-protein inducible by heat shock, H2O2, ultraviolet-A radiation, NaAsO2, pro-inflammatory cytokines, bacterial endotoxins, growth factors, NO, and tumor promotors, heme oxygenase-1 confers protection against oxidative stress
-
-
brenda
heme oxygenase is induced by light and delta-aminolevulinic acid, induction is inhibited by D-glucose
-
-
brenda
-
-
-
brenda
-
684386, 684502, 684777, 684789, 684932, 685099, 685495, 685815, 685997, 686118, 686555, 686599, 686898, 687181, 687555, 687576
UniProt
brenda
2 isoforms: heme oxygenase-1, inducible, heme oxygenase-2, constitutive
-
-
brenda
-
288603, 438243, 438244, 438247, 438248, 438249, 438250, 438259, 438261, 438270, 438273, 438275, 438276
-
-
brenda
-
UniProt
brenda
heme oxygenase-1 is a heat shock protein that is inducible by numerous stimuli, including heavy metals, oxidative stress and injury, and cytokines, a 3 isomer, heme oxygenase-3, exhibits 90% homology to heme oxygenase-2, its mRNA has been detected in several tissues including kidney
-
-
brenda
two isoforms, an inducible HO-1 and a constitutive HO-2
UniProt
brenda
inducible isozyme HO-1, constitutive isozyme HO-2
UniProt
brenda
enzyme induction by curcumin is dramatically reduced by decreasing the temperature from 37°C to 10°C, cells pretreated with curcumin at 37°C or during a programmed decrease in temperature exhibit increased resistance to oxidative stress-mediated injury
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
high expression of the enzyme (HO-1) in male C57BL/6 (wild-type) and homozygous BTB and CNC-homolog 1 (Bach1)-deficient mice induced with acute colitis
brenda
-
in vivo, high HO-1 expression. HO-1 protein is strongly expressed in proliferative, Ki67-positive cytotrophoblasts of cell columns. HO-1 is strongly expressed in cycling cytotrophoblasts of first trimester explant cultures
brenda
-
increased expression on inflammation, particularly in infiltrating cells
brenda
neutrophil HO-1 expression is similar in rats receiving burn injury alone compared with shams gavaged with saline, however, as compared with rats receiving EtOH intoxication, neutrophil HO-1 expression in burn rats is significantly decreased. Furthermore, a significant decrease in neutrophil HO-1 expression is observed in rats receiving a combined insult of EtOH intoxication and burn injury compared with rats receiving either sham or burn injury alone
brenda
expression and immunohistochemic analysis in veno-occlusive priapism, overview
brenda
-
HLA-A2/HO-1-restricted, CD8+ T cells in peripheral blood lymphocytes of cancer patients
brenda
-
activity is very low in obstructive azoospermia specimens, low in nonobstructive azoospermia, moderate in oligozoospermia while higher in normozoospermia. HO-2 expression in all studied groups whereas HO-1 is highly expressed in fertile normozoospermic group compared with other groups
brenda
-
is slightly detectable in the abdominal skeletal muscle
brenda
obtained from the knee joints at the time of joint surgery or synovectomy, performed as a normal part of clinical care, from 20 rheumatoid arthritis patients, HO-1 expression analysis
brenda
additional information
HCV-infected liver biopsies and core protein-expressing hepatocytes show diminished levels of heme oxygenase-1
brenda
-
high level of heme oxygenase-2 in the outer medulla followed by inner medulla/papilla and cortex, heme oxygenase-1 is barely detectable in tissue from untreated animals but increases strongly in SnCl2 treated animals
brenda
HO-1 and HO-2 contents, immunohistochemic analysis, overview
brenda
-
24 h after a CoCl2 injection heme-oxygenase-1 activity increases 13fold, enzyme may play a role in the liver oxidative-stress defence
brenda
HO-1 is expressed primarily in Kupffer cells, HCV-infected liver biopsies and core protein-expressing hepatocytes show diminished levels of heme oxygenase-1
brenda
-
-
brenda
-
enzyme is constitutively expressed in Kupffer cells, inducible in hepatocytes
brenda
the concentration of the heme oxygenase I is higher in the summer (the long day) and lower in the winter (the short day)
brenda
-
the concentration of heme oxygenase 2 is higher in the summer (the long day) and lower in the winter (the short day)
brenda
-
increased expression on inflammation, particularly in infiltrating cells
brenda
-
highest expression of HO-1 mRNA levels in the spleen, 6.6fold of those in the liver
brenda
additional information
-
gene is ubiquitously expressed in cabbage tissues
brenda
additional information
-
in vivo, no HO-1 expression in extravillous trophoblasts and in nonproliferating, Kip2/p57-positive extravillous trophoblasts
brenda
additional information
isozyme HO-2 has a wider tissue distribution than isozyme HO-1
brenda
additional information
isozyme HO-2 has a wider tissue distribution than isozyme HO-1
brenda
additional information
-
isozyme HO-2 has a wider tissue distribution than isozyme HO-1
brenda
additional information
expressions of MsHO1 are higher in alfalfa stems and leaves than those in germinating seeds and roots, expression patterns, overview
brenda
additional information
-
expressions of MsHO1 are higher in alfalfa stems and leaves than those in germinating seeds and roots, expression patterns, overview
brenda
additional information
-
expression of HO-1 is tissue-specific, and there is a correspondence between levels of HO-1 mRNA and protein
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
HY1, HO3, and HO4 are present as the processed mature protein in the plastid compartment
brenda
-
recombinant heme oxygenase-2 expressed in Escherichia coli
brenda
-
presence of the membrane-spanning region on HO-1 is required for efficient membrane incorporation, which is achieved after a 2 h preincubation period at room temperature
brenda
-
-
-
brenda
-
77% activity in inner membrane, specifically associated with complex I, NADH: ubiquinone oxidoreductase
brenda
-
in response to different stimuli, e.g. hypoxia by 3% oxygen or incubation with hemin or heme-hemopexin, HO-1 can migrate to the nucleus. Nuclear translocation is associated with truncation of the C-terminus of HO-1
brenda
in response to different stimuli, e.g. hypoxia by 3% oxygen or incubation with hemin or heme-hemopexin, HO-1 can migrate to the nucleus. Nuclear translocation is associated with truncation of the C-terminus of HO-1 by 52 amino acids, the C-terminal region of HO-1 inhibits the nuclear import
brenda
-
full-length HO-1 is an integral membrane protein
brenda
full-length HO-1 is an integral membrane protein
brenda
additional information
-
no mitochondrial localization of HY1, HO3, and HO4
-
brenda
additional information
effect of nuclear localization of HO-1oncell viability
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug target
targeted induction of heme oxygenase-1 (HO-1) may be a useful therapeutic strategy to supplement conventional pharmaceutical anti-TB therapy, and to help serve a protective function by improving oxidative stress disorders, to decrease lesional inflammatory cell infiltration, to further support antiinflammatory activity, and to induce tissue repair at later stages of Mycobacterium tuberculosis infection
evolution
malfunction
metabolism
physiological function
additional information
evolution
-
Pseudomonas strains exhibit four possible enzyme compositions: (I) BphO, (II) PigA, (III) BphO and PigA and (IV) two PigAs. In Pseudomonas syringae DC3000, PigA is encoded in a cluster together with proteins involved in iron utilization while BphO is functionally and genetically coupled to the phytochrome BphP
evolution
bacterial HmuO and mammalian heme oxygenases are similar in their reaction mechanisms and structures
evolution
bacterial HmuO and mammalian heme oxygenases are similar in their reaction mechanisms and structures
evolution
HmuO and mammalian heme oxygenases are similar in their reaction mechanisms and structures
evolution
-
Pseudomonas strains exhibit four possible enzyme compositions: (I) BphO, (II) PigA, (III) BphO and PigA and (IV) two PigAs. In Pseudomonas aeruginosa PAO1, PigA is encoded in a cluster together with proteins involved in iron utilization while BphO is functionally and genetically coupled to the phytochrome BphP
evolution
-
Pseudomonas strains exhibit four possible enzyme compositions: (I) BphO, (II) PigA, (III) BphO and PigA and (IV) two PigAs. Only one of the two PigA homologues identified in Pseudomonas putida KT2440 is encoded in an iron-associated gene cluster
evolution
-
Pseudomonas strains exhibit four possible enzyme compositions: (I) BphO, (II) PigA, (III) BphO and PigA and (IV) two PigAs. In Pseudomonas fluorescence Pf-5, PigA is encoded in a cluster together with proteins involved in iron utilization while BphO is functionally and genetically coupled to the phytochrome BphP
evolution
-
Pseudomonas strains exhibit four possible enzyme compositions: (I) BphO, (II) PigA, (III) BphO and PigA and (IV) two PigAs. In Pseudomonas mendocina YMP, PigA is encoded in a cluster together with proteins involved in iron utilization while BphO is functionally and genetically coupled to the phytochrome BphP
evolution
-
Pseudomonas strains exhibit four possible enzyme compositions: (I) BphO, (II) PigA, (III) BphO and PigA and (IV) two PigAs. Only one of the two PigA homologues identified in Pseudomonas putida KT2440 is encoded in an iron-associated gene cluster
evolution
-
Pseudomonas strains exhibit four possible enzyme compositions: (I) BphO, (II) PigA, (III) BphO and PigA and (IV) two PigAs. In Pseudomonas syringae DC3000, PigA is encoded in a cluster together with proteins involved in iron utilization while BphO is functionally and genetically coupled to the phytochrome BphP
-
evolution
-
Pseudomonas strains exhibit four possible enzyme compositions: (I) BphO, (II) PigA, (III) BphO and PigA and (IV) two PigAs. In Pseudomonas fluorescence Pf-5, PigA is encoded in a cluster together with proteins involved in iron utilization while BphO is functionally and genetically coupled to the phytochrome BphP
-
evolution
-
Pseudomonas strains exhibit four possible enzyme compositions: (I) BphO, (II) PigA, (III) BphO and PigA and (IV) two PigAs. Only one of the two PigA homologues identified in Pseudomonas putida KT2440 is encoded in an iron-associated gene cluster
-
evolution
Pseudomonas aeruginosa KT 2240
-
Pseudomonas strains exhibit four possible enzyme compositions: (I) BphO, (II) PigA, (III) BphO and PigA and (IV) two PigAs. Only one of the two PigA homologues identified in Pseudomonas putida KT2440 is encoded in an iron-associated gene cluster
-
evolution
-
Pseudomonas strains exhibit four possible enzyme compositions: (I) BphO, (II) PigA, (III) BphO and PigA and (IV) two PigAs. In Pseudomonas mendocina YMP, PigA is encoded in a cluster together with proteins involved in iron utilization while BphO is functionally and genetically coupled to the phytochrome BphP
-
malfunction
mutation of the distal Asp decreases the verdoheme ring opening activity
malfunction
mutation of the distal Asp decreases the verdoheme ring opening activity
malfunction
mutation of the distal Asp decreases the verdoheme ring opening activity
malfunction
-
mutation of ChuZ abolishes the ability of Campylobacter jejuni to use hemin or hemoglobin as sources of iron
malfunction
a deficiency in heme oxygenase 1 expression due to HMOX1 polymorphism may be considered as an underlying cause of human pregnancy disorders, particularly those related to placental dysfunction
metabolism
-
isoform HO-1 modulates the function of transcriptional factor Nuclear factor erythroid 2-related factor 2 (Nrf2). In oxidative stress, nuclear isoform HO-1 interacts with Nrf2 and stabilizes it from glycogen synthase kinase 3beta-mediated phosphorylation coupled with ubiquitin-proteasomal degradation, thereby prolonging its accumulation in the nucleus
metabolism
the enzyme (HO-1) plays a protective role against dextran sodium sulfate-induced intestinal inflammation, possibly by regulating prox02inflammatory cytokines in intestinal tissues
metabolism
heme oxygenase-2 (HO2) and heme oxygenase-1 (HO1) catalyze heme degradation to biliverdin, CO, and iron, forming an essential link in the heme metabolism network. Tight regulation of the cellular levels and catalytic activities of HO1 and HO2 is important for maintaining heme homeostasis. HO1 expression is transcriptionally regulated. HO2 expression is constitutive. HO2 is degraded by the lysosome through chaperone-mediated autophagy
physiological function
-
HO-1-specific T cells isolated from the peripheral blood of cancer patients inhibit cytokine release, proliferation, and cytotoxicity of other immune cells
physiological function
-
HO-1 is critically involved in macrophage polarization toward an M2 phenotype. HO-1 affects anti-inflammatory and antiapoptotic pathways in macrophages
physiological function
-
HO enzyme activity in the human seminal plasma is related to spermatogenesis and sperm-motility processes
physiological function
-
HO-1 is a negative regulator of trophoblast motility acting via up-regulation of peroxisome proliferator activated receptor (PPAR) gamma. In wound healing assays, trophoblast migration into the denuded area is diminished upon induction of HO-1
physiological function
-
because HO-1 and NADPH-cytochrome P450 reductase (CPR) are membrane-bound proteins, the presence of membrane hydrophobic milieu (dilauroylphosphatidylcholine or endoplasmic reticulum membrane) may alter the mechanism by which cytosolic biliverdin reductase metabolizes its substrate biliverdin to bilirubin
physiological function
-
mice lacking the HO-1 gene frequently die in utero, and the mice that survive to adulthood exhibit growth failure, anemia, chronic inflammation characterized by hepatosplenomegaly, leukocytosis, glomerulonephritis, and histological hepatoportal cellular infiltration. HO-1 serves to provide cytoprotection against oxidative stress and is necessary in mammals
physiological function
-
human patient wiht HO-1-deficiency died in his childhood with clinical manifestations, including growth failure, anemia, tissue iron deposition, lymphoadenopathy, leukocytosis and increased sensitivity to oxidative injury. HO-1 serves to provide cytoprotection against oxidative stress and is necessary in mammals
physiological function
-
inducible form of HO-1, biliverdin, and CO possess generalized endogenous anti-inflammatory activities and provide protection against intestinal ischemia/reperfusion injury. Exogenous HO-1 expression, as well as exogenously administered CO and biliverdin, have potent cytoprotective effects on intestinal ischemia/reperfusion injury as well
physiological function
-
heme oxygenase-1 signals are involved in preferential inhibition of pro-inflammatory cytokine release by surfactin, produced by Bacillus subtilis, in cells activated with Porphyromonas gingivalis lipopolysaccharide
physiological function
-
HugZ is part of the iron acquisition mechanism of Helicobacter pylori, and is required for the adaptive colonization of the pathogen in human hosts. Arg166, which is involved in azide binding, is essential for HugZ enzymatic activity, whereas His245 is not, implying that HugZ has an enzymatic mechanism distinct from other heme oxygenases
physiological function
-
HO-1 together with dichloromethane induces interleukin-10 expression in liver. HO-1, acting through the Nfe2l2, i.e. Nrf2, transcription factor, links anti-inflammatory cytokine expression to activation of mitochondrial biogenesis. HO1 induction after LPS stimulates anti-inflammatory interleukin-10 and interleukin-1 receptor antagonist expression in mouse liver, human HepG2 cells, and mouse J774.1 macrophages but blunted tumor necrosis factor-alpha expression
physiological function
-
heme oxygenase-1/CO induces vascular endothelial growth factor expression via p38 kinase-dependent activation of Sp1. CO-induced VEGF promoter activation requires the binding of the Sp1 transcriptional factor to a cis-regulatory sequence located at the VEGF promoter. HO-1/CO induced p38-dependent phosphorylation of Sp1 at Thr453 and Thr739 both in vitro and in vivo
physiological function
-
by catalyzing the first step in heme degradation, heme oxygenase plays a vital role in maintaining proper heme homeostasis. Isozymes HO-1 and HO-2, exist that catalyze the same reaction but differ in several notable ways, overview
physiological function
-
heme oxygenases are widely distributed enzymes involved in the oxidative cleavage of the heme macrocycle that yields the open-chain tetrapyrrole biliverdin IX, CO, and iron
physiological function
-
heme oxygenases are widely distributed enzymes involved in the oxidative cleavage of the heme macrocycle that yields the open-chain tetrapyrrole biliverdin IX, CO, and iron
physiological function
BrHO1 may play an important role in abiotic stress tolerance of Chinese cabbage. Heme oxygenase is a regulatory enzyme that cleaves heme to biliverdin IXalpha, with the concomitant release of carbon monoxide and the production of free Fe2+
physiological function
MsHO1 may play an important role in oxidative responses
physiological function
-
4-hydroxy hexenal stimulates expression of the antioxidant enzyme HO-1 through the activation of Nrf2 in vascular endothelial cells resulting in prevention of oxidative stress-induced cytotoxicity, this may represent a possible mechanism to partly explain the cardioprotective effects of n-3 polyunsaturated fatty acids
physiological function
heme oxygenase has cytoprotective properties and may play a role in several disease states. HO-1 activity is upregulated in response to several therapeutic treatments and is implicated in promoting tumour growth. HO-1-derived CO is associated with angiogenesis, inducing vascular endothelial growth factor synthesis, and stimulating the proliferation of endothelial cells. Role of the HO/CO system in neuronal complications, particularly of HO-1
physiological function
heme oxygenase-1 is the limiting enzyme in heme catabolism. Induction of HO-1 expression decreases dramatically NADPH oxidase Nox4 activity in C-20/A4 and HEK-293T-RExTM Nox4 cell lines, mediated by carbon monoxide, the decrease is not accompanied by any change in the expression, the subcellular localization or the maturation of Nox4. Inhibition of the heme synthesis by succinylacetone rather than heme catabolism by HO-1, leads to a confinement of the Nox4/p22phox heterodimer in the endoplasmic reticulum with an absence of redox differential spectrum highlighting an incomplete maturation. HO-1 decreases MMP-1 expression and chondrocytes DNA fragmentation via CO release
physiological function
-
the enzyme enables the organism to use heme as the sole iron source
physiological function
-
role of PigA in iron acquisition, in strains containing no PigA, this function may be fulfilled by BphO
physiological function
heme oxygenase has cytoprotective properties and may play a role in several disease states. Role of the HO/CO system in neuronal complications, particularly of HO-1
physiological function
-
role of PigA in iron acquisition, in strains containing no PigA, this function may be fulfilled by BphO
physiological function
-
role of PigA in iron acquisition, in strains containing no PigA, this function may be fulfilled by BphO
physiological function
-
role of PigA in iron acquisition, in strains containing no PigA, this function may be fulfilled by BphO
physiological function
-
the enzyme exhibits protective effects on cecal ligation and puncture-induced acute lung injury via regulating cell surface thrombomodulin and activated protein C expression and modulating blood coagulation
physiological function
-
enzyme overexpression is critical for tumor cell death with an impaired mitochondrial energetics
physiological function
enzyme interacts and acquires heme from cytoplasmic heme transport protein holo-PhuS. In mutant strains, the absence of bilverdin IXbeta and bilverdinIXdelta leads to a decrease in extracellular levels of hemophore HasA
physiological function
-
overexpression of Brassica oleracea HO1 in transgenic Arabidopsis plants significantly alleviates salinity stress-inhibited seedling growth, accompanied by the reestablishment of reactive oxygen species and ion homeostasis. Protein abundance related to light reactions is greatly suppressed by NaCl stress in wild-type, but is partially recovered in the transgenic strain. HO1 may activate multiple stress-responsive pathways to help Arabidopsis thaliana regain cellular homeostasis during salinity stress
physiological function
isoform Hmox2 contains two C-terminal heme regulatory motifs centered at Cys265 and Cys282. The same mechanism of heme hydroxylation to alpha-meso-hydroxyheme is employed by both isoform Hmox1 and Hmox2 and the heme regulatory motifs do not affect the physicochemical properties of the oxy-Fe(II) and HOO-Fe(III) states of Hmox2. Heme oxygenation by Hmox2 occurs solely at the catalytic core and hydroxylation proceeds three times slower and the oxy-Fe(II) state is 100fold less stable in Hmox2 than in Hmox1
physiological function
pharmacological induction or genetic overexpression of Hmox1 significantly ameliorates the effects of amyloid-beta1-42 in SH-SY5Y cells
physiological function
pharmacological induction of Hmox1 significantly ameliorates the effects of amyloid-beta1-42 in rat primary hippocampal neurons
physiological function
Hmox2 and cytochrome P450 reductase form a dynamic ensemble of complexes that precede formation of the productive electron transfer complex. Specific residues, including Leu201, near the heme face of Hmox2 are affected by the addition of cytochrome P450 reductase. Hmox2 and biliverdin reductase form a very weak complex, and biliverdin reductase binds Hmox2 weakly
physiological function
the enzyme catalyses heme breakdown to biliverdin, carbon monoxide, and Fe2+. Heme oxygenase 1 (HO-1), the inducible heme oxygenase isoenzyme, is involved in placental development. HO-1 decreases the oxidative stress and promotes an immune tolerant microenvironment at the foetomaternal interface. The isozyme also regulates angiogenesis and vasculogenesis, and trophoblasts proliferation, migration and invasion, thus contributing to the adaptive changes in the uterine circulation to pregnancy. Human chorionic gonadotropin (hCG) is the first hormonal signal of pregnancy whose effects in pregnancy are mediated by heme oxygenase 1
physiological function
heme oxygenase I plays a very important role in the fight against the oxidative stress
physiological function
heme oxygenase-1 (HO-1) plays an important role in iron homeostasis and the antioxidant system as a cytoprotective enzyme to control oxidative stress-induced cellular damage. The dual role of HO-1 in tuberculosis may depend on different pathological conditions. On the one hand, HO-1 plays amainly cytoprotective role in the early stages of the disease, and on the other hand, HO-1 can potentially be cytotoxic due to accumulation of large amounts of heme, and the human host may have an impaired ability to maintain iron homeostasis during the later stages of Mycobacterium tuberculosis infection
physiological function
key rate-limiting enzyme in the process of degradation of the iron-containing molecule. Major cytoprotective players in conditions associated with inflammation and oxidative stress (metabolic and cardiovascular disorders). The cytoprotective effects of HO-1 depend on several cellular mechanisms including the generation of bilirubin, an anti-oxidant molecule, from the degradation of heme, the induction of ferritin, a strong chelator of free iron, and the release of CO, that displays multiple anti-inflammatory and anti-apoptotic actions. The enzyme is a marker of oxidative stress
physiological function
key regulator of cellular signaling and of stress response. The cytoprotective enzyme degrades heme to generate carbon monoxide (CO), biliverdin, and molecular iron. Depending upon host cell type and the pathogen, the enzyme (HMOX1) can act in protection of the host from infection or it may assist the growth of intracellular pathogen CO and biliverdin (or bilirubin derived from it) can restrict the growth of a few pathogens. Protective role is clear in microbial sepsis and in several viral infections including HIV. HMOX1 helps in the survival of intracellular leishmania. The role of HMOX1 is not clear in case of malaria, TB and salmonella infection
physiological function
the heme oxygenase-1/biliverdin/carbon monoxide pathway downregulates hypernociception in rats by a mechanism dependent on cGMP/ATP-sensitive K+ channels
physiological function
the enzyme (HO-1) plays a protective role against inflammatory processes
physiological function
heme oxygenase-1 (HO-1) is a cytoprotective, inducible enzyme that degrades toxic free heme released from destabilized heme proteins and, during this process, releases beneficial by-products such as carbon monoxide and biliverdin/bilirubin and promotes ferritin synthesis. HO-1 induction and/or delivery of its products can protect against AKI
physiological function
-
the ability of Acinetobacter baumannii {LAC-4} to internalize and utilize heme is dependent on the presence of the hemO gene cluster
physiological function
-
heme oxygenase I plays a very important role in the fight against the oxidative stress
physiological function
-
role of PigA in iron acquisition, in strains containing no PigA, this function may be fulfilled by BphO
-
physiological function
-
HO-1 together with dichloromethane induces interleukin-10 expression in liver. HO-1, acting through the Nfe2l2, i.e. Nrf2, transcription factor, links anti-inflammatory cytokine expression to activation of mitochondrial biogenesis. HO1 induction after LPS stimulates anti-inflammatory interleukin-10 and interleukin-1 receptor antagonist expression in mouse liver, human HepG2 cells, and mouse J774.1 macrophages but blunted tumor necrosis factor-alpha expression
-
physiological function
-
role of PigA in iron acquisition, in strains containing no PigA, this function may be fulfilled by BphO
-
physiological function
-
role of PigA in iron acquisition, in strains containing no PigA, this function may be fulfilled by BphO
-
physiological function
-
the ability of Acinetobacter baumannii {LAC-4} to internalize and utilize heme is dependent on the presence of the hemO gene cluster
-
additional information
QM/MM calculations based on this crystal structure exploring the reaction mechanisms starting from the FeOOH-verdoheme and FeHOOH-verdoheme complexes, which mimic, respectively, the O2- and H2O2-supported degradations. The rate-determining step is the initial O-O bond breaking step, which is either homolytic, for FeHOOH-verdoheme, or coupled to electron and proton transfers, in FeOOH-verdoheme. The FeHOOH-verdoheme complex is more reactive than the FeOOH-verdoheme complex
additional information
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QM/MM calculations based on this crystal structure exploring the reaction mechanisms starting from the FeOOH-verdoheme and FeHOOH-verdoheme complexes, which mimic, respectively, the O2- and H2O2-supported degradations. The rate-determining step is the initial O-O bond breaking step, which is either homolytic, for FeHOOH-verdoheme, or coupled to electron and proton transfers, in FeOOH-verdoheme. The FeHOOH-verdoheme complex is more reactive than the FeOOH-verdoheme complex
additional information
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in cells, Hmox1 or Nfe2l2 RNA silencing prevents IL-10 and IL-1Ra up-regulation, and HO-1 induction fails post-LPS in Nfe2l2-silenced cells and post-sepsis in Nfe2l2-/- mice
additional information
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regulation of isozyme HO-2, overview. Presence of three Cys residues as part of heme-regulatory motifs in HO-2, low-spin Fe(III) heme species are characteristic of thiolate ligation is formed when Cys265 is reduced. Resonance Raman data collected at different temperatures reveal an intriguing temperature dependence of the iron spin state in the heme-HO-2 complex
additional information
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modulation of HO catalysis by ligands targeting the critical distal pocket structure, overview
additional information
modulation of HO catalysis by ligands targeting the critical distal pocket structure, overview
additional information
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modulation of HO catalysis by ligands targeting the critical distal pocket structure, overview
additional information
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physiological effects of angiotensin II with and without tin mesoporphyrin on renal and aortic HO-1 activity, overview
additional information
heme oxygenase is an enzyme that catalyzes the regiospecific conversion of heme to biliverdin IXalpha, carbon monoxide, and free Fe(II). Heme degradation by heme oxygenase proceeds through three successive steps of O2 activation. The first step is formation of alpha-meso-hydroxyheme from from heme, second formation of verdoheme from alpha-meso-hydroxyheme, the third step is the ring opening of verdoheme, Only alpha-verdoheme with the O atom in its alpha position, and not beta-, gamma-, or delta-verdoheme, is converted to biliverdin. The third step, like the first, shows regiospecificity, the distal Asp plays an important role in this step, similar to the first. The substrate heme is sandwiched between two helices, termed the proximal and distal helices
additional information
heme oxygenase is an enzyme that catalyzes the regiospecific conversion of heme to biliverdin IXalpha, carbon monoxide, and free Fe(II). Heme degradation by heme oxygenase proceeds through three successive steps of O2 activation. The first step is formation of alpha-meso-hydroxyheme from from heme, second formation of verdoheme from alpha-meso-hydroxyheme, the third step is the ring opening of verdoheme, Only alpha-verdoheme with the O atom in its alpha position, and not beta-, gamma-, or delta-verdoheme, is converted to biliverdin. The third step, like the first, shows regiospecificity, the distal Asp plays an important role in this step, similar to the first. The substrate heme is sandwiched between two helices, termed the proximal and distal helices
additional information
heme oxygenase is an enzyme that catalyzes the regiospecific conversion of heme to biliverdin IXalpha, carbon monoxide, and free Fe(II). Heme degradation by heme oxygenase proceeds through three successive steps of O2 activation. The first step is formation of alpha-meso-hydroxyheme from heme, second formation of verdoheme from alpha-meso-hydroxyheme, the third step is the ring opening of verdoheme. Only alpha-verdoheme with the O atom in its alpha position, and not beta-, gamma-, or delta-verdoheme, is converted to biliverdin. The third step, like the first, shows regiospecificity, the distal Asp plays an important role in this step, similar to the first. The substrate heme is sandwiched between two helices, termed the proximal and distal helices
additional information
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heme is bound in its binding site on the dimer interface by four histidine side-chains through hydrophobic interactions, canonical heme-binding site structure, reaction mechanism and structure-function relationship, overview
additional information
-
the enzyme shows substrate-protein, specifically pyrrole-I/II-helix-2, peripheral interactions. The enzyme's C-terminus interacts with substrate in solution, interaction of the C-terminus with the active site destabilizes the crystallographic protohemin orientation, which is consistent with optimizing the His207-Asp27 H-bond, active site stress for product release, NMR analysis of wild-type and mutant enzymes, overview. Thermodynamics of substrate orientational isomerism are mapped for substrates with individual vinyl to methyl to hydrogen substitutions and with enzyme C-terminal deletions. Replacing bulky vinyls with hydrogens results in a 180 degree rotation of substrate about the alpha,gamma-meso axis in the active site
additional information
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analysis of enzyme-protohemin substrate variant complexes and of enzyme-propionate substrate complexes by NMR, active site structure, overview. The enzyme's C-terminal fragment interacts with the active site of the enzyme. The C-terminal dipeptide Arg208-His209 cleaves spontaneously. Stronger hydrophobic contacts between pyrroles A and B with the enzyme contribute more substantially to the substrate binding free energy than in mammalian HOs, liberating one propionate to stabilize the C-terminus
additional information
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in cells, Hmox1 or Nfe2l2 RNA silencing prevents IL-10 and IL-1Ra up-regulation, and HO-1 induction fails post-LPS in Nfe2l2-silenced cells and post-sepsis in Nfe2l2-/- mice
-
additional information
-
physiological effects of angiotensin II with and without tin mesoporphyrin on renal and aortic HO-1 activity, overview
-
Show AA Sequence and Transmembrane Helices (4564 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
200000
25000
28000
32000
33000
36000
additional information
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heme oxygenase consists of 3 components: a 22000 Da ferredoxin-like Fe/S cluster protein that can be replaced by ferredoxin, a 38000 Da protein that is inactivated by diethyldicarbonate, inactivation is blocked by heme, a 37000 Da protein with ferredoxin-linked cytochrome c reductase activity
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
-
with a splitbarrel fold. One heme-binding site is at the dimer interface and another novel heme-binding site is found on the protein surface
additional information
?
x * x* 36500, precursor protein including N-terminal transit leader peptide, calculated, x * 35000, SDS-PAGE of mature recombinant protein including His-tag
dimer
-
HugZ is a dimer in solution, that adopts a split-barrel fold. HugZ-hemin crystallizes as a trimer of dimers. Structure overview
additional information
three-dimensional structure of BrHO1, analysis and comparison, overview
additional information
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three-dimensional structure of BrHO1, analysis and comparison, overview
additional information
the C-terminal 23 amino acids are essential for maximal catalytic activity
additional information
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the C-terminal 23 amino acids are essential for maximal catalytic activity
additional information
structure comparison of isozymes HO-1 and HO-2, overview. Both apo- and holoenzymes contain a hydrogen-bond network involving Asn210, Arg136, as well as a second level of residues, which includes Tyr58 and Tyr114 to stabilize the position of the catalytically critical Asp140 residue for HO-1 and Asp160 for HO-2. Structure-activity relationship analysis
additional information
structure comparison of isozymes HO-1 and HO-2, overview. Both apo- and holoenzymes contain a hydrogen-bond network involving Asn210, Arg136, as well as a second level of residues, which includes Tyr58 and Tyr114 to stabilize the position of the catalytically critical Asp140 residue for HO-1 and Asp160 for HO-2. Structure-activity relationship analysis
additional information
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structure comparison of isozymes HO-1 and HO-2, overview. Both apo- and holoenzymes contain a hydrogen-bond network involving Asn210, Arg136, as well as a second level of residues, which includes Tyr58 and Tyr114 to stabilize the position of the catalytically critical Asp140 residue for HO-1 and Asp160 for HO-2. Structure-activity relationship analysis
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
HO-1 contains several thrombin cleavage sites, one of which is located at the C-terminus to cleave the membrane binding domain, overview
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant His-tagged enzyme complexed with hemin, hemin:ChuZ ratio of 2:1, microbatch method, mixing of 0..001 ml of 170 mg/ml ChuZ-hemin in 20 mM Tris-HCl, pH 8.0, and 5 mM sodium azide with 0.001 ml of reservoir solution consisting of 0.1 M MES, pH 6.5, 24% PEG400 v/v, and 0.1 M imidazole, X-ray diffraction structure determination and analysis at 2.5 A resolution
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azide-bound Fe(II)-verdoheme-HmuO, 30°C, a hanging drop vapor diffusion method, the reservoir solution containing 50 mM MES, pH 5.4, 2.3-2.5 M ammonium sulfate, 0.27 M sodium bromide, and 0.1% dioxane, X-ray diffraction structure determination and analysis at 3.0 A resolution
DTT-bound forms of ferric heme-HO-1 complexes, X-ray diffraction structure analysis of crystal structures with PDB IDSs I9T and 3I9U, resolution is 1.5 A
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hanging drop vapor diffusion method, free enzyme is crystallized by using 85 mM sodium cacodylate, pH 6.5, 25.5% (w/v) PEG8000, 170 mM sodium acetate, and 23.5% (v/v) glycerol, while substrate-bound enzyme is crystallized by using 50 mM MES, pH 6.1, 2.2 M ammonium sulfate, and 25% (w/v) sucrose, supplemented with 200 mM sodium ascorbate
heme oxygenase HmuO in tertiary complex with reaction intermediate verdoheme and N3, X-ray diffraction structure determination and analysis at 1.7 resolution
sitting drop vapour diffusion method using 12-15% (w/v) polyethylene glycol 3350, 0.15-0.20 M magnesium formate, and 10-20 mM NAD
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purified recombinant HugZ, hanging-drop vapour diffusion method, mixing of 0.001 ml of 25 mg/ml HugZ-hemin in 20 mM Tris, pH 8.0, 5 mM sodium azide, with 0.001 ml of reservoir solution consisting of 16% w/v PEG 3350, 3% Tacsimate, 0.1 M imidazole, pH 7.5, and 12% methanol, X-ray diffraction structure determination and analysis at 1.8-2.3 A resolution
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apo- and heme-bound truncated HO-2, lacking the three heme regulatory motifs and the membrane binding region, apo-HO-2: hanging drop method, 0.0015 ml of 5 mg/ml protein in 50 mM KCl, 50 mM Tris-HCl, pH 7.5, are mixed with 0.001 ml of well solution containing 40% PEG 1500, 200 mM potassium glutamate, and 100 mM triethanolamine, pH 8.5, at 4°C, heme-bound HO-2: hanging drop vapour diffusion method, 0.0015 ml of 5 mg/ml protein in 50 mM KCl, 50 mM Tris-HCl, pH 7.5, are mixed with 0.001 ml of well solution containing 33% PEG dimethlyether 500, 20 mM MgCl2, and 100 mM HEPES, pH 8.5, at 4°C, X-ray diffraction structure determination and analysis at 2.4 A resolution for the apoenzyme, and at 2.6 A resolution for the heme-bound enzyme
crystal structure determination and analysis of HO-1 in complex with different inhibitors, i.e. 2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl) methyl]-1,3-dioxolane, (2R,4S)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-[((5-trifluoromethylpyridin-2-yl)thio)methyl]-1,3-dioxolane, 1-(adamantan-1-yl)-2-(1H-imidazol-1-yl)ethanone, 4-phenyl-1-(1,2,4-1H-triazol-1-yl)butan-2-one, and 1-(1H-imidazol-1-yl)-4,4-diphenyl-2-butanone, overview
heme oxygenase HO1 complexed with reaction intermediate verdoheme, and in tertiary complex with verdoheme and NO, X-ray diffraction structure determination and analysis at 2.2 and 2.1 A resolution, respectively
HO-1 in complex with 1-(adamantan-1-yl)-2-(1H-imidazol-1-yl)ethanone to a resolution of 1.54 A, the coordinating nitrogen atom of His25 is shifted by 0.91 A while the Fe moiety is shifted by 0.85 A. Distal pocket of in the complex is more-open than that of the native holoenzyme. HO-1 in complex with 4-phenyl-1-(1,2,4-1H-triazol-1-yl)butan-2-one to a resolution of 2.20 A, or in complex with (2R,4S)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-[((5-trifluoromethylpyridin-2-yl)thio)methyl]-1,3-dioxolane
HO-1 in complex with 1-(adamantan-1-yl)-2-(1H-imidazol-1-yl)ethanone, by sitting-drop vapor diffusion method, at room temperature, to 1.5 A resolution. Overall structure of the HO-1-inhibitor complex is very similar to that of the native heme-conjugated HO-1, being mostly alpha-helical with the heme sandwiched between the proximal and distal helices. The inhibitor binds to the HO-1 distal pocket such that the imidazolyl moiety coordinates with heme iron while the adamantyl group is stabilized by a hydrophobic binding pocket. Distal helix flexibility, coupled with shifts in proximal residues and heme, acts to expand the distal pocket, thus accommodating the bulky inhibitor without displacing heme. Inhibitor binding effectively displaces the catalytically critical distal water ligand
in complex with ferrous and ferrous-NO forms of verdoheme, absence of network of water-molecules in both structures
mutant H25R with bound heme, to 2.95 A resolution. Contrary to wild-type, the Arg25 side-chain in the H25R mutant is oriented away from the parent His25 position, accompanied by reorientation of the Glu29 side-chain
wild-type and mutant H25A, by hanging drop vapor diffusion method, at 2.8 A resolution. Mutant heme-HO-1 crystal is monoclinic, space group P21, there are four molecules in an asymmetric unit cell. The molecular surfaces of wild-type and mutant are of little difference, though the active pocket in the mutant is larger. The two have the same substrate affinity in electrostatic potential. A positive charge region on the edge of heme forms around the catalytic reaction pocket. After mutation, Ala is still located in the surface and does not influence the electrostatic potential of the reaction pocket
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heme oxygenase-heme complex at 1.73 A resolution. A hydrogen-bonded network of structural water molecules that extends from the catalytic site to the protein surface is observed. A long-range communication exists between the outer fringes of the hydrogen-bonded network of structural waters and the heme active site during catalysis. Model for the productive association of ferredoxin-NADP+ reductase and heme oxygenase
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crystal structure at 1.5 A resolution, comparison with heme oxygenase-1 from mammalian sources
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molecular docking of inhibitor (E)-2-(4-isopropylbenzylidene)hydrazinecarboximidamide to HemO on the back site and the heme site
heme oxygenase HO1 complexed with reaction intermediate verdoheme, X-ray diffraction structure determination and analysis at 2.2 A resolution
HO-1 in complex with (2-[2-(4-chlorophenyl)ethyl]-2-[1H-imidazol-1-yl)methyl]-1,3-dioxolane to 2.70 A resolution, the heme and helix are shifted by ca. 0.8 A toward the alpha-meso carbon along the alpha-gamma axis of the heme
thiol-bound forms of ferric heme-HO-1 complexes, thiols are from DTT or DTE, X-ray diffraction structure analysis of crystal structures with PDB IDSs I9T and 3I9U, resolution is 2.15-2.25 A
truncated heme oxygenase-1, hanging-drop vapor diffusion, enzyme solution is mixed with an equal volume of each reservoir solution and equilibrated, crystals are obtained at 293 K, reservoir solution contains 4 M sodium formate, 18 mg/ml enzyme concentration in 50 mM potassium phosphate, pH 7.0, hexagonal rod-shaped crystals appear after 3 d, X-ray structure of heme oxygenase in complex with heme bound to azide at 1.9 A resolution
truncated, soluble hHO-1 variant, consisting of 233 amino acids, in complex with 4-phenyl-1-(1H-1,2,4-triazol-1-yl)-2-butanone, sitting-drop vapor diffusion, room temperature, 0.412 mM heme-HO-1 complex in 20 mM potassium phosphate is mixed with inhibitor in a 1:3 molar ratio, the reservoir solution contains100 mM HEPES, pH 7.5, 2.00-2.28 M ammonium sulfate, and 0.8-1.1% 1,6-hexanediol, X-ray diffraction structure determination and analysis
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mutant H25R with bound heme, to 2.95 A resolution. Contrary to wild-type, the Arg25 side-chain in the H25R mutant is oriented away from the parent His25 position, accompanied by reorientation of the Glu29 side-chain
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D136A
reduced heme degradation activity, formation of ferryl heme
D136F
reduced heme degradation activity, formation of ferryl heme
H20A
-
capable of NADPH dependent hydroxylation of heme to alpha-mesohydroxyheme in contrast to human H25A heme oxygenase-1 mutant, ability to catalyze the conversion of verdoheme to biliverdin is rescued by imidazole titration
H245A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
H245Q
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R166A
-
site-directed mutagenesis, the mutation completely abolished the HO activity of HugZ
C127A
-
site-directed mutagenesis of the truncated HO-2 variant lacking the membrane spanning domain, spectral properties in comparison to the wild-type HO-2, overview
C127A/C282A
-
site-directed mutagenesis of the truncated HO-2 variant lacking the membrane spanning domain, spectral properties in comparison to the wild-type HO-2, overview
D140A
G143H
the replacement of Gly143 with His leads to the formation of a bis-histidine complex
H25A
R183E
R254K
F157A
-
mutant is unable to carry out the complete degradation of heme to biliverdin, the reaction is arrested at the verdoheme stage. The protein displays bands at 357, 525 and 678 nm, reminiscent of the absorption spectrum reported for the HO-verdoheme complex. Overexpression of the HO F157 variants causes the Escherichia coli cells to turn dark green color
F157I
-
mutant is unable to carry out the complete degradation of heme to biliverdin, the reaction is arrested at the verdoheme stage. The protein displays bands at 357, 525 and 678 nm, reminiscent of the absorption spectrum reported for the HO-verdoheme complex. Overexpression of the HO F157 variants causes the Escherichia coli cells to turn dark green color
F157A
Leptospira interrogans serovar Icterohaemorrhagiae serovar Lai 56601
-
mutant is unable to carry out the complete degradation of heme to biliverdin, the reaction is arrested at the verdoheme stage. The protein displays bands at 357, 525 and 678 nm, reminiscent of the absorption spectrum reported for the HO-verdoheme complex. Overexpression of the HO F157 variants causes the Escherichia coli cells to turn dark green color
-
F157I
Leptospira interrogans serovar Icterohaemorrhagiae serovar Lai 56601
-
mutant is unable to carry out the complete degradation of heme to biliverdin, the reaction is arrested at the verdoheme stage. The protein displays bands at 357, 525 and 678 nm, reminiscent of the absorption spectrum reported for the HO-verdoheme complex. Overexpression of the HO F157 variants causes the Escherichia coli cells to turn dark green color
-
H26A/K34A/K132A
mutant does not interact with holo-PhuS and shows no enzymatic activity
N19K/K34A/F117Y/K132A
change in regioselectivity, product is biliverdin IXalpha
H25A
site-directed mutagenesis, the mutant is translocated to the nucleus losing its C-terminus
L213I
-
increases the distance between the phenyl ring of inhibitor (2R,4S)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-[(phenylsulfanyl)methyl]-1,3-dioxolane hydrochloride and the residue from 3.6 to 4.4 A
M34V
-
increases the distance to the phenyl group in the northeastern region of inhibitor (2R,4S)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-[(phenylsulfanyl)methyl]-1,3-dioxolane hydrochloride
R183a
-
same alpha-regioselectivity as wild-type, only alpha-biliverdin is produced
R183D
-
in contrast to wild-type heme oxygenase-1 which converts heme exclusively to alpha-biliverdin, the R183D mutant converts heme to 20% delta-biliverdin in addition to alpha-biliverdin
R183E
-
in contrast to wild-type heme oxygenase-1 which converts heme exclusively to alpha-biliverdin, the R183E mutant converts heme to 35% delta-biliverdin and small amounts of beta and gamma-biliverdin in addition to alpha-biliverdin
R183N
-
same alpha-regioselectivity as wild-type, only alpha-biliverdin is produced
R183Q
-
same alpha-regioselectivity as wild-type, only alpha-biliverdin is produced
S53A
-
distance from the Ser53 of HO-1 to inhibitor (2R,4S)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-[(phenylsulfanyl)methyl]-1,3-dioxolane hydrochloride will be similar if substituted with Ala (4.5 A), the hydroxyl group of Ser53 in the HO-1 model will be close enough to be within van der Waals contact of the inhibitor if it is rotated toward the hydrophobic pocket
V50A
-
increases the distance between residue and inhibitor (2R,4S)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-[(phenylsulfanyl)methyl]-1,3-dioxolane hydrochloride by ca. 0.8 A
H17F
very poor or no activity in live-cell assay, presence of heme, no binding of biliverdin observed
H17K
mutant retains activity in live-cell assay, and binds biliverdin
H17R
mutant retains activity in live-cell assay, and binds biliverdin. No activity in vitro
additional information
D140A
-
abolished activity, retains the unusual wild-type azide complex spin/orbital ground state
D140A
-
exhibits resolved and relaxed 2,4-dimethyldeuterohemin resonances at low pH and at high pH
H25A
-
about 10% of wild-type activity, binding activity to heme similar to wild-type
H25A
-
mutation leads to an empty pocket underneath the ferric ion in the heme, leading to loss of binding iron ligand. Enzymatic activity is reduced by 90.5%. By supplementing imidazole, the HO-1 activity is restored approximately 87.5% to its normal level
R183E
in addition to product biliverdin IXalpha, mutant yields biliverdin IXdelta and traces of biliverdin IXbeta. Crystal structure reveals altered active site hydrogen bonding network
R254K
site-directed mutagenesis, the exchange eliminates a thrombin cleavage site in the full-length enzyme, the mutant enzyme shows similar activity compared to the wild-type enzyme
R254K
-
enhances protein stability during the glutathione S-transferase-tag removal procedure involving the protease thrombin
additional information
de novo synthesis of the heme proteins on a membrane-coupled template, and screening for heme proteins with heme oxygenase activity, overview
additional information
-
de novo synthesis of the heme proteins on a membrane-coupled template, and screening for heme proteins with heme oxygenase activity, overview
additional information
a clinically relevant polymorphism within the HO-1 promoter critically influences its transcriptional activation by both PPAR isoforms, overview
additional information
-
a clinically relevant polymorphism within the HO-1 promoter critically influences its transcriptional activation by both PPAR isoforms, overview
additional information
high-loading nanosized micelles of copoly(styrene-maleic acid)-zinc protoporphyrin with an average molecular size of 144 kDa for targeted delivery of a potent heme oxygenase inhibitor, method development, overview
additional information
-
high-loading nanosized micelles of copoly(styrene-maleic acid)-zinc protoporphyrin with an average molecular size of 144 kDa for targeted delivery of a potent heme oxygenase inhibitor, method development, overview
additional information
construction of deletion and/or disruption mutants of HO-1, phenotypes, overview
additional information
construction of deletion and/or disruption mutants of HO-1, phenotypes, overview
additional information
enzyme suppression with siRNA abolishes the cytoprotective effect of HO-1
additional information
construction of apo- and heme-bound truncated HO-2, lacking the three heme regulatory motifs and the membrane binding region
additional information
-
construction of apo- and heme-bound truncated HO-2, lacking the three heme regulatory motifs and the membrane binding region
additional information
HO-1 expression is enhanced in BI-1 transfected cells compared to untransfected cells, phenotype, overview
additional information
protective effect by iron chelation in HO1-deficient fibroblasts
additional information
enzyme downregulation by expression of HO-1 siRNA in WM451Lu cells, reverses the upregulating effect of 5-aminolevulinic acid, oerview
additional information
construction of deletion and/or disruption mutants of HO-2, phenotypes, overview
additional information
construction of deletion and/or disruption mutants of HO-2, phenotypes, overview
additional information
a variant of ascorbate peroxidase, W41A, which reacts slowly with tert-butyl hydroperoxide does not form the usual peroxidase compound I intermediate, but instead forms a product in which the heme is cleaved at the alpha-meso position, analogous to the heme oxygenase mechanism
additional information
-
adenovirus-mediated HO-1 transduction of Rattus norvegicus primary cardiomyocytes and H9C2 myocytes results in significant induction of VEGF expression, overview
additional information
-
construction of a truncated HO-2 variant lacking the membrane spanning domain, spectral properties in comparison to the wild-type HO-2, overview
additional information
a variant of Hmox1 lacking the C-terminal heme regulatory domain exhibits the same specific activity as one containing both the catalytic core and heme regulatory domain. A truncated variant containing only the heme regulatory region binds but cannot oxidize heme
additional information
-
a variant of Hmox1 lacking the C-terminal heme regulatory domain exhibits the same specific activity as one containing both the catalytic core and heme regulatory domain. A truncated variant containing only the heme regulatory region binds but cannot oxidize heme
additional information
an heme oxygenase-2 catalytic site variant that is unable to bind heme exhibits a constant low protein level and an enhanced protein degradation rate compared with the wild-type heme oxygenase-2
additional information
-
a C26S variant lacking the last 20 C-terminal residues incorporates the prosthetic group efficiently and is active
additional information
Leptospira interrogans serovar Icterohaemorrhagiae serovar Lai 56601
-
a C26S variant lacking the last 20 C-terminal residues incorporates the prosthetic group efficiently and is active
-
additional information
knock-down of HO-1 expression by siRNA expression, overexpression of HO-1 in B16F10 cells confers resistance to cisplatin treatment, overview
additional information
-
knock-down of HO-1 expression by siRNA expression, overexpression of HO-1 in B16F10 cells confers resistance to cisplatin treatment, overview
additional information
construction of deletion and/or disruption mutants of HO-2, phenotypes, overview
additional information
construction of deletion and/or disruption mutants of HO-2, phenotypes, overview
additional information
inhibition of HO-1 expression by small interfering RNA decreases cellular survival and apoptosis in the mouse hepatoma cell lines Hepa129 and Hepa1-6, and orthotopic tumor growth in immune-competent C3H/HeN mice, mechanism. But application of siHO1 does not induce liver or kidney damage in mice, overview
additional information
-
inhibition of HO-1 expression by small interfering RNA decreases cellular survival and apoptosis in the mouse hepatoma cell lines Hepa129 and Hepa1-6, and orthotopic tumor growth in immune-competent C3H/HeN mice, mechanism. But application of siHO1 does not induce liver or kidney damage in mice, overview
additional information
HO-1 expression is reduced in toll-like receptor 2 TLR2-knockout mice after stab-wound injury, overview
additional information
-
HO-1 expression is reduced in toll-like receptor 2 TLR2-knockout mice after stab-wound injury, overview
additional information
RNA interference with HO-1 siRNA reduces the expression of HO-1 transcripts and protein as well as oxygen radical production
additional information
construction of deletion and/or disruption mutants of HO-1, phenotypes, overview
additional information
construction of deletion and/or disruption mutants of HO-1, phenotypes, overview
additional information
-
inhibition of HO-1 expression by small interfering RNA decreases cellular survival and apoptosis in the mouse hepatoma cell lines Hepa129 and Hepa1-6, and orthotopic tumor growth in immune-competent C3H/HeN mice, mechanism. But application of siHO1 does not induce liver or kidney damage in mice, overview
-
additional information
-
HO-1 expression is reduced in toll-like receptor 2 TLR2-knockout mice after stab-wound injury, overview
-
additional information
-
C-terminal truncation of the enzyme, e.g. by sequential deletion of three residues, His207, Arg208, His209. Deleting His209 minimally perturbs the interaction of the C-terminus, but deletion of Arg208 completely abolishes it
additional information
-
rat HO-1 cDNA transfected RBL-2H3 cells show altered cytokine production in response to stimulation with anti-ovalbumin OA serum/OA compared to Mock transfected RBL-2H3 cells. HO-1 inhibits anti-OA serum/OA-induced IL-3 and TNF-alpha production. Inhibition of HO-1 activity by Zn (II) protoporphyrin IX, a specific HO-1 inhibitor, prevents the suppression of TNF-alpha production. The cytokine inhibition by HO-1 is associated with selective suppression of the DNA-binding activity of AP-1 transcription factors, phenotype, overview
additional information
rat HO-1 cDNA transfected RBL-2H3 cells show altered cytokine production in response to stimulation with anti-ovalbumin OA serum/OA compared to Mock transfected RBL-2H3 cells. HO-1 inhibits anti-OA serum/OA-induced IL-3 and TNF-alpha production. Inhibition of HO-1 activity by Zn (II) protoporphyrin IX, a specific HO-1 inhibitor, prevents the suppression of TNF-alpha production. The cytokine inhibition by HO-1 is associated with selective suppression of the DNA-binding activity of AP-1 transcription factors, phenotype, overview
additional information
HO-1-specific siRNA significantly reduces hemin and cadmium chloride-mediated HO-1 induction, cobstruction of HO-1 deletion mutants showing decreased enzyme activity
additional information
HO-1 overexpression activates an oxidant-responsive HO-1 promoter
additional information
RNA interference with HO-1 siRNA reduces the expression of HO-1 transcripts and protein as well as oxygen radical production
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10.3
-
sequential Ni-Ni+1 connections for Ile57-Ala60, His84-Lys86, Leu93-Trp96, and Leu164-Phe167 can be observed even at pH 10.3, with chemical shift similar to those for heme oxygenase-2,4-dimethyldeuterohemin-H2O
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0 - 4
35
-
liver heme oxygenase-1: 65-70% activity after 10 min at 60°C, testis heme oxygenase-2: 20% activity after 10 min at 60°C
50
54 - 56
melting temperature, wild-type and mutants H26A/K34A/K132A and N19K/K34A/F117Y/K132A
65
-
10 min, 30% loss of heme oxygenase-1 activity, 80% loss of heme oxygenase-2 activity
50
-
10 min, 80% loss of liver heme oxygenase-1 and testis heme oxygenase 2 activity
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
an heme oxygenase-2 catalytic site variant that is unable to bind heme exhibits a constant low protein level and an enhanced protein degradation rate compared with the wild-type heme oxygenase-2
heme oxygenase-2 is degraded by the lysosome through chaperone-mediated autophagy
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 20 mM potassium phosphate, pH 7.5, 0.2% Triton X-100, 20% glycerol, 2 d, 50% loss of activity
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
2 separate fractions after first DEAE-cellulose, hydroxyapatite, Sephadex G-150, DEAE-cellulose
-
ammonium sulfate, Sephadex G-75, DEAE-cellulose, hydroxyapatite, tryptic 28000 Da fragment of recombinant heme oxygenase-2
-
DEAE-ion exchange expanded bed adsorption and Superdex 75 gel filtration, the specific HO-1 activity increases from 0.82 to 24.8 U/mg during purification steps
-
deletion of 23 C-terminal amino acids, which serve as the membrane-spanning domain, allows for a rapid purification of truncated, soluble HO-1 in large quantities, by standard column chromatography
-
HY1, HO3, and HO4. HO3 and HO4 purified by cobalt affinity chromatography, to over 90% purity
-
hydroxylapatite column chromatography and POROS-HQ column chromatography
on Ni-NTA column, wild-type 32fold purified and mutant H25A 31fold purified, more than 95% pure
-
partial
recombinant C-terminal truncated heme oxygenase-1, ammonium sulfate, Mono Q, recombinant heme oxygenase-1/cytochrome P450 reductase fusion protein, ammonium sulfate, 2',5'-ADP-Sepharose
-
recombinant ChuZ from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
-
recombinant GST-tagged full-length HO-1 mutant R254K 54fold and recombinant wild-type enzyme 40fold by thrombin treatment and glutathione affinity chromatography, elution with 1.0% sarkosyl detergent and 2% octyl glucoside, the recombinant wild-type full-length enzyme is not stable during expression and purification due to proteolytic cleavage, overview
recombinant GST-tagged wild-type and mutant HO-2 from Escherichia coli strain BL21(DE3) by glutathione affinity chromatography
recombinant His-tagged HO1 from Escherichia coli by nickel affinity chromatography
recombinant His6-tagged HugZ from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
-
recombinant wild-type and His-tagged enzyme, ion-exchange, gel filtration
-
Triton X-100 + cholate, DEAE-cellulose, hydroxyapatite, Sepharose CL-6B, hydroxyapatite
-
verdoheme-HmuO complex by anion exchange chromatography and gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
293FT cells transiently cotransfected with a vector containing the viral packaging proteins gag and pol, a vector containing env and pMSCV-scrttaM2puro or pRevTRE-hHO1
-
710-bp fragment encoded amino acids of wild-type and mutant HO-1 constructed in the plasmids pET28b(+)-hHO-1(w) and (m), expressed in Escherichia coli BL21 (DE3)
-
adenovirus-mediated HO-1 transfection of Rattus norvegicus primary cardiomyocytes and H9C2 myocytes
-
DNA and amino acid sequence determination and analysis, genetic structure, phylogenetic analysis, functional expression of His-tagged HO1 in Escherichia coli
DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression of GFP-tagged HO1 targeted to chloroplasts. Expression of mature MsHO1 in Escherichia coli
DNA and amino acid sequence determination of wild-type and mutant, full-length and truncated enzymes, expression of the N-terminus of the rat enzyme in human HEK-293 cells, and of FLAG-tagged inactive mutant H25A in 3T3 cells, nuclear translocation of enzyme mutants lacking the C-terminus and of mutant H25A, overview
expressed in Escherichia coli
expression analysis
expression in Escherichia coli
expression in SH-SY5Y cells
expression of C-terminal truncated heme oxygenase-1 and of a heme oxygenase-1 cytochrome P450 reductase fusion protein
-
expression of GST-tagged full-length HO-1 mutant R254K and of GST-tagged wild-type enzyme in Escherichia coli strain DH5alpha
expression of GST-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3), transfection of wild-type HO-1 cDNA or intracellular delivery of pure HO-1 protein into cultured NIH 3T3 cells results in activation of a 15-kb HO-1 promoter independently of HO activity, expression of an catalytically inactive HO-1 also results in promoter activation, HO-1-mediated promoter activation is regulated via the distal enhancers E1 and E2
expression of the kappaB element of the proximal rat HO-1 gene promoter region, -284 to -275, a nuclear target for the NF-kappaB subunit p65/RelA, expression in in RAW264.7 monocytes fused to the luciferase gene. HO-1 promoter activity is induced by p65, an NF-kappaB subunit, which is also termed RelA, and which is a member of the Rel family of proteins and is activated in response to a variety of stimuli
expression of the kappaB element of the proximal rat HO-1 gene promoter region, -284 to -275, a nuclear target for the NF-kappaB subunit p65/RelA, expressionin in RAW264.7 monocytes fused to the luciferase gene
expression of wild-type and His-tagged enzyme in Escherichia coli
-
expression of wild-type heme oxygenase-1 and 2 and heme oxygenase-2 C264A/C281A double mutant in Escherichia coli
-
gene chuZ, ChuZ is highly conserved in 32 clinical isolates. Genotyping, recombinant expression in Escherichia coli strain BL21(DE3)
-
HO-1, DNA and amino acid sequence determination, quantitative expression analysis, overview
HY1, HO3, and HO4 expressed without their predicted chloroplast transit peptides either using a tac promoter-driven N-terminal GST fusion expression system (HY1) or the pET vector system (HO3, HO4) using a T7-promoter and a His-tag fusion. Plasmids pGEX-mHY1, pET24a-mHO3 and pET24a-mHO4 expressed in Escherichia coli BL21 (DE3). Fluorescent protein expression in Nicotiana benthamiana by using Agrobacterium tumefaciens C58C1 pGV2260
-
overexpression in Escherichia coli BL21 (DE3) with a hexa-histidine (6X-His) tag
-
overexpression of GST-tagged wild-type and mutant HO-2 in Escherichia coli strain BL21(DE3)
quantitative enzyme expression analysis
sense and antisense constructs, expression analysis in dendritic cells of different maturation levels, cobalt protoporphyrin leads to overexpression of HO-1, molecular mechanism, overview
truncated HO-1 lacking the 23 C-terminal residues, truncated HO-2 lacking the 23 C-terminal residues in the pBAce expression vector construct transformed into Escherichia coli DH5alpha
-
truncated human HO-1 expression vector, expressed in Escherichia coli strain DH5alpha
-
truncated, soluble version of HO-1 that contains 233 amino acids expressed from plasmid HO1-t233/pBace in Escherichia coli DH5alpha
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
21 h treatment with 0.05-0.2 mM docosahexaenoic acid enhances isoform HO-1 expression through transcriptional regulation in human cancer cells. Docosahexaenoic acid induces Bach1 protein degradation, thereby enhancing the transcriptional factor Nrf2-mediated isoform HO-1 gene transcription
-
apoptotic cell supernatants provoke a biphasic up-regulation of HO-1. Although the first phase of HO-1 induction at 6 h is accomplished by apoptotic cell-derived sphingosine-1-phosphate acting via sphingosine-1-phosphate receptor 1, the second wave of HO-1 induction at 24 h is attributed to autocrine signaling of vascular endothelial growth factor A, whose expression and release are facilitated by sphingosine-1-phosphate
-
cell treatment with Salvia plebeia methanolic extract significantly induces the expression of hemeoxygenase-1
-
expression of Hmox1a, Hmox1b and biliverdin reductase b is significantly induced in zebrafish eleutheroembryos in response to pro-oxidants cadmium, hemin and tert-butylhydroquinone
expression of isoform Hmox2a is significantly reduced in male gill samples in response to the 96 hour cadmium exposure
expression of isoforms Hmox1a, Hmox2a and Hmox2b is significantly induced in male liver tissues in response to 96 hour cadmium exposure (20 microM). Hmox2a and Hmox2b are significantly induced in male brain samples
HO-1 activity is upregulated in response to several therapeutic treatments and is implicated in promoting tumour growth
HO-1 expression is chemically induced by cobalt protoporphyrin-IX in HEK293 T-RExTM Nox4 cells resulting in downregulation of NADPH oxidase Nox4 activity
HO-1 expression is reduced upon differentiation of cytotrophoblasts into extravillous trophoblasts. Knock down of endogenous HO-1 in BeWo cells using retroviral transduction with a miRNA adapted retroviral vector targeting human HO-1 sequence
-
HO-1 induction after hemoglobin treatment is decreased by about half by MEK inhibitors U0126 and SL327, and is completely prevented by the direct ERK inhibitor FR180204
-
HO-1 induction by hemoglobin. In cultures treated with hemoglobin plus dimethylsulfoxide vehicle for 4 h, which is a time point prior to the onset of neuronal lysis, HO-1 expression is increased 2.2fold over control cultures treated with vehicle only
-
HO-1 is induced by inflammation associated both with an anti-inflammatory response and with mitochondrial biogenesis
HO-1 protein expression is strongly induced 24 h after DOX addition in the HTR-8/SVneo cell line
-
HO1 is induced by several stress conditions, e.g. osmotic and salinity stresses, cadmium exposure, H2O2, and hemin treatments
in human acute kidney injury as well as preclinical acute kidney injury models, thed enzyme (HO-1) is robustly induced
lipopolysaccharide downregulates isoform HO-1 in primary human peripheral blood mononuclear cells, CD14+ monocytes, macrophages, dendritic cells, and granulocytes
-
lipopolysaccharide upregulates isoform HO-1 in human monocytic leukemia cell lines. Bach1 is a critical transcriptional repressor of isoform HO-1
-
low concentration of 4-hydroxy hexenal increases heme oxygenase-1 expression through activation of Nrf2 and antioxidative activity in vascular endothelial cells, overview. The induction is abolished by knockout of Nrf2
-
MsHO1 gene expression and protein level are induced significantly by some pro-oxidant compounds, including hemin and nitric oxide donor sodium nitroprusside
Mycobacterium tuberculosis (MTB) infection causes acute oxidative stress, and increases the expression of HO-1, which may in turn facilitate MTB survival and growth due to increased iron availability
pretreatment with hemoglobin induces HO-1 and significantly reduces systemic inflammations associated with plasma concentrations of TNFalpha levels due to intestinal ischemia/reperfusion injury
-
renal HO-1 is induced by angiotensin II, ANG II, when given in high doses
small interfering RNA-mediated knock-down of Nrf-2 significantly inhibits surfactin-induced HO-1 expression. Inhibition of phosphoinositide 3-kinase/Akt and extracellular signal-regulated kinase significantly decreased surfactin-induced HO-1 expression, mechanism of surfactin, overview
-
surfactin, a cyclic lipopeptide produced by Bacillus subtilis, induces HO-1 mRNA and protein expression via activation of Nrf2, and PI3K/Akt and ERK, mechanism of surfactin, overview. Nrf-2 is a redox-sensitive basic-leucine zipper transcription factor
-
systemic enzyme levels are dramatically increased in individuals with active pulmonary and extra-pulmonary tuberculosis and particularly those with bilateral lung lesions and elevated bacillary loads in sputum
-
the enzyme (HO-1) is highly inducible in response to a variety of stimuli, such as oxidative stress, hypoxia, bacterial lipopolysaccharide (LPS), cytokines, and its substrate heme
transcripts can be differentially induced by hemin, paraquat, and NaCl treatments
HO-1 is induced by inflammation associated both with an anti-inflammatory response and with mitochondrial biogenesis
-
HO-1 is induced by inflammation associated both with an anti-inflammatory response and with mitochondrial biogenesis
-
-
renal HO-1 is induced by angiotensin II, ANG II, when given in high doses
-
renal HO-1 is induced by angiotensin II, ANG II, when given in high doses
-
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
drug development
medicine
analysis
glial HO-1 expression might be an early marker of non-hemorrhagic cell injury in the striatum, time course of induction, overview
analysis
live-cell activity assay based on heterologous coexpression in Escherichia coli of heme oxygenase and its mutants and a fluorescent biliverdin biosensor
analysis
live-cell activity assay based on heterologous coexpression in Escherichia coli of heme oxygenase and its mutants and a fluorescent biliverdin biosensor
drug development
-
the enzyme is a potential therapeutic target for antimicrobial drug development, computer-aided drug design and screening, overview
drug development
heme oxygenase has cytoprotective properties and may play a role in several disease states, making it an interesting therapeutic target
medicine
-
cells pretreated with curcumin at 37°C or during a programmed decrease in temperature exhibit increased resistance to oxidative stress-mediated injury, feasibility of modulating HO-1 expression during hydpothermic storage to confer tissues a better protection against damages characteristic of organ transplantation
medicine
-
treatment of streptozotocin-induced diabetic rats with enzyme inhibitor sn protoporphyrin IX. No significant alterations of the enzyme sytem following one week of diabetes. One month of diabetes caused increased oxidative stress in association with 2.5-fold increase in enzyme activity. Sn protoporphyrin IX treatment reduces the number of 8-hydroxy-2deoxyguanosine-positive cardiomycetes and enzyxme activity. Non-diabetic animals treated with hemin exhibit abnormalities similar to diabetic rats
medicine
-
involved in the control of wound healing, heme-induced influx of leukocytes is highly elevated after inhibition of enzyme
medicine
-
outstanding capacity of HO-1-specific CD8+ Tregs to efficiently suppress T cell responses opens new opportunities for therapeutic intervention to modulate immune responses
medicine
-
reduction in HO activity may contribute to the protective effect of MEK and ERK inhibitors against heme-mediated neuronal injury
medicine
-
chronic ethanol feeding induces 5-aminolevulinic acid synthase-1 (ALAS1) mRNA, cytosolic ALAS1 and mature ALAS1 protein levels, but not those of HO-1 in rat livers, which provides novel insights into the effects of chronic ethanol consumption on hepatic heme biosynthesis and porphyrias
medicine
modulation of Nox4 activity via heme oxygenase-1 may represent a promising therapeutic tool in osteoarthritis
medicine
-
the enzyme is a potentially useful parameter for distinguishing active from latent or treated pulmonary tuberculosis
medicine
induction or exogenous overexpression of heme oxygenase HO-1 effectively inhibits Dengue virus DENV replication in DENV-infected Huh-7 cells. This antiviral is attenuated by inhibitor tin protoporphyrin. Biliverdin but not carbon monoxide and ferrous ions, mediates the HO-1-induced anti-DENV effect by non-competitively inhibiting DENV protease. HO-1 induction or its exogenous overexpression, rescues DENV-suppressed antiviral interferon response. HO-1 induction by cobalt protoporphyrin and andrographolide leads to a significant delay in the onset of disease and mortality, and virus load in the infected mice's brains
medicine
Hmox1 protects against amyloid beta toxicity via production of CO. Protection does not arise from inhibition of apoptosis-associated K+ efflux, but rather by inhibition of AMP-dependent protein kinase activation
medicine
activity of heme oxygenase-1 interferes with porcine reproductive and respiratory syndrome virus PRRSV replication. The host cell antiviral effect depends on a heme oxygenase-1-biliverdin/bilrubin-nitric oxide-cGMP/PKG cascade
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Release 2026.1 (March 2026)
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