1.14.14.18: heme oxygenase (biliverdin-producing)
This is an abbreviated version!
For detailed information about heme oxygenase (biliverdin-producing), go to the full flat file.
Word Map on EC 1.14.14.18
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1.14.14.18
-
monoxide
-
cytoprotective
-
endothelial
-
necrosis
-
dismutase
-
protoporphyrin
-
erythroid
-
2-related
-
tnf
-
bilirubin
-
artery
-
malondialdehyde
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lipopolysaccharide
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catalase
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hemin
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neuroprotective
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ischemia
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gsh
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lps
-
sod
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anti-oxidant
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mapks
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sirna
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caspase-3
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quinone
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pulmonary
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reperfusion
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lps-induced
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hypoxia
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cyclooxygenase-2
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cox-2
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ferritin
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erk
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nf-e2-related
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anti-apoptotic
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cobalt
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myeloperoxidase
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ischemia-reperfusion
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nrf2-mediated
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pro-oxidant
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kelch-like
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nadph:quinone
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factor-2
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lps-stimulated
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2-like
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erythroid-derived
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oxygenases
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delta-aminolevulinic
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sulforaphane
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hyperbilirubinemia
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medicine
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drug development
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analysis
- 1.14.14.18
- monoxide
-
cytoprotective
- endothelial
- necrosis
- dismutase
- protoporphyrin
-
erythroid
-
2-related
- tnf
- bilirubin
- artery
- malondialdehyde
- lipopolysaccharide
- catalase
- hemin
-
neuroprotective
- ischemia
- gsh
- lps
- sod
-
anti-oxidant
- mapks
- sirna
- caspase-3
- quinone
- pulmonary
-
reperfusion
-
lps-induced
- hypoxia
- cyclooxygenase-2
- cox-2
- ferritin
- erk
-
nf-e2-related
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anti-apoptotic
- cobalt
- myeloperoxidase
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ischemia-reperfusion
-
nrf2-mediated
-
pro-oxidant
-
kelch-like
-
nadph:quinone
-
factor-2
-
lps-stimulated
-
2-like
-
erythroid-derived
- oxygenases
-
delta-aminolevulinic
- sulforaphane
- hyperbilirubinemia
- medicine
- drug development
- analysis
Reaction
+ 3 [reduced NADPH-hemoprotein reductase] + 3 O2 = + + + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O
Synonyms
biliverdin-producing heme oxygenase, ChuS, ChuZ, EC 1.14.99.3, haem oxygenase, heme oxygenase, heme oxygenase 1, heme oxygenase 2, heme oxygenase-1, heme oxygenase-2, HemO, Hmox1, Hmox1a, Hmox1b, Hmox2, Hmox2a, Hmox2b, HmuO, Hmx1, HO, HO-1, HO-2, Ho1, Ho2, Ho3, HO4, HSP32, HugZ, HY1, inducible heme oxygenase-1, More, MsHO1, ORP33 proteins, oxygenase, heme (decyclizing), pbsA1, PigA, proteins, specific or class, ORP33 (oxygen-regulated protein 33,000-mol.-wt.), Syn HO-1, Syn HO-2
ECTree
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Inhibitors
Inhibitors on EC 1.14.14.18 - heme oxygenase (biliverdin-producing)
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(+-)-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
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(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
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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
-
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(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
-
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(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
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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
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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
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(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
-
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(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
-
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(2R,4S)-4-[(3-bromophenylsulfanyl)methyl]-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane hydrochloride
-
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(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
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IC50: 0.02 mM
(2S,4S)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-methyl-1,3-dioxolane
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IC50: 0.012 mM
(2Z)-4-[(4-anilinophenyl)amino]-4-oxobut-2-enoic acid
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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
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IC50: 0.0019 mM
1-((2-(2-(4-chlorophenyl)ethyl)-1,3-dioxolan-2-yl)methyl)-1H-imidazole hydrochloride
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IC50: 0.0043 mM
1-((2-(2-(4-fluorophenyl)ethyl)-1,3-dioxolan-2-yl)methyl)-1H-imidazole hydrochloride
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IC50: 0.0038 mM
1-((2-(2-(4-iodophenyl)ethyl)-1,3-dioxolan-2-yl)methyl)-1H-imidazole hydrochloride
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IC50: 0.0037 mM
1-((2-(2-phenylethyl)-1,3-dioxolan-2-yl)methyl)-1H-imidazole hydrochloride
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IC50: 0.0007 mM
1-(1H-imidazol-1-yl)-4-(4-iodophenyl)-2-butanone hydrochloride
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IC50: 0.00011 mM
1-(4-trifluoromethylbenzyl)-2-(pyrrolidin-1-ylmethyl)-1H-benzimidazole
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1-(naphthalen-2-ylmethyl)-2-(pyrrolidin-1-ylmethyl)-1H-benzimidazole
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2-(4-chlorophenyl)-N'-[(1E)-1H-indol-3-ylmethylidene]acetohydrazide
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binding affinity is 0.0141 mM, complete inhibition
2-(4-chlorophenyl)-N'-[(1Z)-1H-inden-3-ylmethylene]acetohydrazide
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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
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2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-1,3-dithiolane
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IC50: 0.0047 mM
2-[2-(4-fluorophenyl)ethyl]-2-[(1H-imidazol-1-yl) methyl]-1,3-dioxolane
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3-morpholinosydnonimine
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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
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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
-
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
27% inhibition at 0.1 mM
1 mM, potent inhibitor
2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-1,3-dioxolane
-
IC50: 0.004 mM
-
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
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
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
-
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
-
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
-
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
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
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
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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
-
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
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additional information
imidazole-based inhibitor derivatives, overview; imidazole-based inhibitor derivatives, overview
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additional information
imidazole-based inhibitor derivatives, overview; imidazole-based inhibitor derivatives, overview
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additional information
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HO-1-generated hydrogen peroxide leads to a decrease in HO-1 activity
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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
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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
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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
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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
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additional information
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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
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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
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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
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additional information
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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
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imidazole-based inhibitor derivatives, overview; imidazole-based inhibitor derivatives, overview
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additional information
imidazole-based inhibitor derivatives, overview; imidazole-based inhibitor derivatives, overview
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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
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additional information
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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
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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
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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
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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
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additional information
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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
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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
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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
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additional information
synthesis and inhibitory potency on isozyme HO-1 of imidazole-based compounds, molecular docking and modelling, overview
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