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Information on EC 3.5.4.4 - adenosine deaminase
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3.5.4.4 adenosine deaminaseSpecify your search results
Word Map
- 3.5.4.4
- purine
- nucleoside
- lymphocyte
- immunodeficiency
- inosine
- pleural
-
tuberculous
- agonist
-
deamination
- phosphorylase
- effusion
- erythrocyte
- adenylate
- leukemia
- 5'-nucleotidase
- xanthine
-
editing
- ehna
- marrow
- deoxyadenosine
- hypoxanthine
-
lymphoid
- t-cells
- dipyridamole
-
hematopoietic
- theophylline
-
exudative
-
purinergic
-
lipolysis
- meningitis
- pleurisy
- dpcpx
- 2-chloroadenosine
-
ecto-5\'-nucleotidase
- datp
- s-adenosylhomocysteine
- ectonucleotidases
- pericarditis
-
acid-fast
-
n6-cyclopentyladenosine
- lymphopenia
-
adenosine-induced
- ntpdases
- deaminases
-
antilipolytic
-
diphosphohydrolase
- deoxycytidine
-
transudate
- empyema
- drug development
- medicine
- diagnostics
- analysis
-
purinoceptors
- pharmacology
The enzyme appears in viruses and cellular organisms
Synonyms
adenosine deaminase, adenosine deaminase 2, adenosine aminohydrolase, adenosine deaminase 1, adaii, pvada, mj1541, sco4901, ciada, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ADA
ADA1
ADA2
ADAI
ADAII
Adenosine aminohydrolase
adenosine deaminase
adenosine deaminase 1
adenosine deaminase 2
MJ1541
PvADA
ADA
-
-
ADA
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
adenosine + H2O = inosine + NH3
-
-
-
-
adenosine + H2O = inosine + NH3
reaction mechanism, structure-function relationship of ADA and dipeptidyl peptidase IV
-
adenosine + H2O = inosine + NH3
reaction mechanism, structure-function relationship of ADA and dipeptidyl peptidase IV
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
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SYSTEMATIC NAME
IUBMB Comments
adenosine aminohydrolase
-
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CAS REGISTRY NUMBER
COMMENTARY
9026-93-1
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2',3'-deoxyadenosine + H2O
2',3'-deoxyinosine + NH3
-
1.7% of the activity with adenosine
-
?
2',3'-O-isopropylidenadenosine + H2O
2',3'-O-isopropylideninosine + NH3
modeling studies
-
?
2',3'-O-isopropylidene adenosine + H2O
2',3'-O-isopropylidene inosine + NH3
-
-
-
?
2',3'-O-methoxymethylideneadenosine + H2O
2',3'-O-methoxymethylideneinosine + NH3
modeling studies
-
?
2'-deoxyguanosine + H2O
2'-deoxyxanthosine + NH3
-
ADAII shows 41% of the activity with adenosine
-
?
2,6-diaminopurine arabinoside + H2O
arabinoguanosine + NH3
-
-
-
?
2,6-diaminopurine-2',3'-dideoxyriboside + H2O
2',3'-dideoxyguanosine + NH3
-
-
-
?
2,6-diaminopurine-2'-deoxyriboside + H2O
2'-deoxyguanosine + NH3
-
-
-
?
adenosine 3'-monophosphate + H2O
inosine 3'-monophosphate + NH3
56% of the activity of adenine
-
?
formycin A + H2O
2-(hydroxymethyl)-5-(1H-pyrazolo[4,3-d]pyrimidin-3-yl)tetrahydrofuran-3,4-diol + NH3
guanine + H2O
xanthine + NH3
-
ADAII shows 47% of the activity with adenosine
-
?
guanosine + H2O
xanthosine + NH3
-
ADAII shows 75% of the activity with adenosine
-
?
N6-isopentenyladenosine + H2O
?
1.9% of the activity of adenine
-
?
N6-isopentenyladenosine + H2O
inosine + 3-methylbut-3-en-1-amine
1.2% of the activity of adenine
-
?
2',3'-isopropylideneadenosine + H2O
2',3'-isopropylideneinosine + NH3
Micrococcus sodonensis
-
-
-
?
2',3'-isopropylideneadenosine + H2O
2',3'-isopropylideneinosine + NH3
-
-
-
ir
2',3'-isopropylideneadenosine + H2O
2',3'-isopropylideneinosine + NH3
-
-
-
ir
2',3'-isopropylideneadenosine + H2O
2',3'-isopropylideneinosine + NH3
-
-
-
?
2',3'-isopropylideneadenosine + H2O
2',3'-isopropylideneinosine + NH3
-
-
-
?
2'-deoxyadenosine + H2O
2'-deoxyinosine + NH3
-
ADAII shows 88% of the activity with adenosine
-
?
2'-deoxyadenosine + H2O
2'-deoxyinosine + NH3
-
118.9% of the activity with adenosine
-
?
2'-deoxyadenosine + H2O
2'-deoxyinosine + NH3
-
79.2% of the activity with adenosine
-
?
2'-deoxyadenosine + H2O
2'-deoxyinosine + NH3
-
82.8% of the activity with adenosine
-
?
2'-deoxyadenosine + H2O
2'-deoxyinosine + NH3
-
the enzyme plays an important role in the immune system
-
?
3'-deoxyadenosine + H2O
3'-deoxyinosine + NH3
-
2.4% of the activity with adenosine
-
?
5'-methylthioadenosine + H2O
5'-methylthioinosine + NH3
-
-
-
?
5'-methylthioadenosine + H2O
5'-methylthioinosine + NH3
-
-
ir
5'-methylthioadenosine + H2O
5'-methylthioinosine + NH3
adenosine deaminase has a secondary function in recycling methylthiopurines from the polyamine biosynthetic pathway
-
ir
adenine + H2O
hypoxanthine + NH3
-
ADAII shows 70% of the activity with adenosine
-
?
adenosine + H2O
inosine + NH3
30% of the activity of adenine
-
ir
adenosine + H2O
inosine + NH3
-
key enzyme in controlling intra- and extracellular adenosine levels
-
?
adenosine + H2O
inosine + NH3
-
-
-
?
adenosine + H2O
inosine + NH3
key enzyme involved in the purine metabolism
-
?
adenosine + H2O
inosine + NH3
-
-
655265, 667870, 668232, 668751, 670393, 670464, 686745, 687290, 697368, 697735, 699651, 699959, 699972, 733602, 733674
-
?
adenosine + H2O
inosine + NH3
isozyme ADA2 is important in lymphocyte activation, and may be active in sites of inflammation and during hypoxia and in areas of tumor growth with elevated adenosine levels and acidic pH, overview
-
?
adenosine + H2O
inosine + NH3
-
the enzyme activity is correlated with the content in malonaldehyde in nasal polyps and nasal mucosa, overview
-
?
adenosine + H2O
inosine + NH3
-
the enzyme expression and activity is suppressed in normal pregnancy, but not in woman with recurrent spontaneous abortion
-
?
adenosine + H2O
inosine + NH3
-
the enzyme is involved in differentiation and maturation of the lymphoid system, the enzyme activity is decreased in multiple sclerosis patients irrespective of whether patients have relapsing-remitting or chronic progressive multiple sclerosis, overview
-
?
adenosine + H2O
inosine + NH3
-
the enzyme plays an important role in the immune system
-
?
adenosine + H2O
inosine + NH3
-
metabolization of extracellular adenosine leads to exacerbation of inflammation
-
ir
adenosine + H2O
inosine + NH3
-
detailed quantitative structure-activity relationship, QSAR, nonlinear modeling and analysis, descriptor generation and selection, overview
-
?
adenosine + H2O
inosine + NH3
-
metabolization of extracellular adenosine
-
ir
adenosine + H2O
inosine + NH3
-
adenosine deaminase markedly enhances the agonist and antagonist affinity and abolishes the negative cooperativity on agonist binding to human striatial adenosine A1 receptors
-
?
adenosine + H2O
inosine + NH3
the enzyme shows no activity with 5'-methylthioinosine
-
ir
adenosine + H2O
inosine + NH3
-
adenosine deaminase is involved in purine metabolism and is a key enzyme for the control of the cellular levels of adenosine
-
?
adenosine + H2O
inosine + NH3
catalytic efficiency of the enzyme for 5'-deoxyadenosine is 1000fold higher than for S-methyl-5'-thioadenosine, and 10000fold hgher than with S-adenosyl-L-homocysteine or adenosine
-
?
adenosine + H2O
inosine + NH3
catalytic efficiency of the enzyme for 5'-deoxyadenosine is 1000fold higher than for S-methyl-5'-thioadenosine, and 10000fold hgher than with S-adenosyl-L-homocysteine or adenosine
-
?
adenosine + H2O
inosine + NH3
the enzyme is crucial for purine metabolism and normal immune competence
-
ir
adenosine + H2O
inosine + NH3
-
the enzyme is important in thymocyte development, especially in late stages, overview
-
?
adenosine + H2O
inosine + NH3
-
the enzyme is important in thymocyte development, especially in late stages, overview
-
?
adenosine + H2O
inosine + NH3
-
the enzyme is involved in the bile duct-inflammation and fibrosis caused chronic fascioliasis including an atrophy of the liver parenchyma and liver cirrhosis
-
ir
adenosine + H2O
inosine + NH3
-
adenosine deamination is involved in the essential pathway of purine salvage in Plasmodium falciparum, and inhibition of purine salvage results in parasite death
-
?
adenosine + H2O
inosine + NH3
-
-
-
?
adenosine + H2O
inosine + NH3
1.4% of the activity of adenine
-
?
adenosine + H2O
inosine + NH3
2.0% of the activity of adenine
-
?
adenosine 3'-phosphate + H2O
inosine 3'-phosphate + NH3
3.3% of the activity of adenine
-
?
adenosine 3'-phosphate + H2O
inosine 3'-phosphate + NH3
4.5% of the activity of adenine
-
?
adenosine-3'-monophosphate + H2O
IMP-3'-monophosphate + NH3
-
-
-
?
formycin A + H2O
2-(hydroxymethyl)-5-(1H-pyrazolo[4,3-d]pyrimidin-3-yl)tetrahydrofuran-3,4-diol + NH3
-
-
-
?
formycin A + H2O
2-(hydroxymethyl)-5-(1H-pyrazolo[4,3-d]pyrimidin-3-yl)tetrahydrofuran-3,4-diol + NH3
-
-
-
?
viramidine + H2O
ribavirin + NH3
-
the enzyme catalyzes viramidine deamination to ribavirin in vivo as a prodrug conversion to active drug, pharmacokinetic analysis, overview
-
?
viramidine + H2O
ribavirin + NH3
-
substrate and product determination by LC-MS
-
?
additional information
?
-
-
regulatory role of dipeptidyl peptidase IV on adenosine deaminase activity
-
?
additional information
?
-
-
the enzyme may facilitate catalysis via the formation of a stabilizing conformation at the reaction transition state
-
?
additional information
?
-
-
the enzyme is bound and complexed by the cell membraneous dipeptidyl peptidase IV, which is identical to the activated immune cell antigen CD26, playing a role in the immune system, overview
-
?
additional information
?
-
-
substrate specificities of the large and the small isozyme, overview
-
?
additional information
?
-
-
adenosine deaminase inhibition enhances the efficiency of signal transduction and inotropic response mediated by A1 adenosine receptor in hyperthyroid guinea pig atrium via elevated intracellular adenosine levels, overview
-
?
additional information
?
-
-
the enzyme is involved in purine metabolism and plays an important role in the mechanism of the immune system
-
?
additional information
?
-
-
no activity with 3'-deoxyadenosine, 2',3'-deoxyadenosine and 2'-O-methyladenosine
-
?
additional information
?
-
-
activity with 3'-deoxyadenosine, 2',3'-deoxyadenosine and 2'-O-methyladenosine is less than 0.5% of the activity with adenine
-
?
additional information
?
-
-
the large isozyme is bound and complexed by the cell membraneous dipeptidyl peptidase IV, which is identical to the activated immune cell antigen CD26, playing a role in the immune system, overview
-
?
additional information
?
-
-
substrate specificities of the large and the small isozyme, overview
-
?
additional information
?
-
-
Plasmodium gallinaceum ADA does not have significant activity for 5'-methylthioadenosine
-
?
additional information
?
-
-
adenosine modulates the immune system and inhibits inflammation via reduction of cytokine biosynthesis and neutrophil functions, enzyme inhibition reduces inflammation in experimental colitis, overview
-
?
additional information
?
-
-
ADA is associated with the Galphai-3 protein-coupled A1 receptor
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
viramidine + H2O
ribavirin + NH3
-
the enzyme catalyzes viramidine deamination to ribavirin in vivo as a prodrug conversion to active drug, pharmacokinetic analysis, overview
-
-
?
2'-deoxyadenosine + H2O
2'-deoxyinosine + NH3
-
the enzyme plays an important role in the immune system
-
-
?
5'-methylthioadenosine + H2O
5'-methylthioinosine + NH3
adenosine deaminase has a secondary function in recycling methylthiopurines from the polyamine biosynthetic pathway
-
-
ir
adenosine + H2O
inosine + NH3
-
key enzyme in controlling intra- and extracellular adenosine levels
-
-
?
adenosine + H2O
inosine + NH3
key enzyme involved in the purine metabolism
-
-
?
adenosine + H2O
inosine + NH3
-
-
-
-
?
adenosine + H2O
inosine + NH3
isozyme ADA2 is important in lymphocyte activation, and may be active in sites of inflammation and during hypoxia and in areas of tumor growth with elevated adenosine levels and acidic pH, overview
-
-
?
adenosine + H2O
inosine + NH3
-
the enzyme activity is correlated with the content in malonaldehyde in nasal polyps and nasal mucosa, overview
-
-
?
adenosine + H2O
inosine + NH3
-
the enzyme expression and activity is suppressed in normal pregnancy, but not in woman with recurrent spontaneous abortion
-
-
?
adenosine + H2O
inosine + NH3
-
the enzyme is involved in differentiation and maturation of the lymphoid system, the enzyme activity is decreased in multiple sclerosis patients irrespective of whether patients have relapsing-remitting or chronic progressive multiple sclerosis, overview
-
-
?
adenosine + H2O
inosine + NH3
-
the enzyme plays an important role in the immune system
-
-
?
adenosine + H2O
inosine + NH3
-
metabolization of extracellular adenosine leads to exacerbation of inflammation
-
-
ir
adenosine + H2O
inosine + NH3
-
adenosine deaminase is involved in purine metabolism and is a key enzyme for the control of the cellular levels of adenosine
-
-
?
adenosine + H2O
inosine + NH3
the enzyme is crucial for purine metabolism and normal immune competence
-
-
ir
adenosine + H2O
inosine + NH3
-
the enzyme is important in thymocyte development, especially in late stages, overview
-
-
?
adenosine + H2O
inosine + NH3
-
the enzyme is important in thymocyte development, especially in late stages, overview
-
-
?
adenosine + H2O
inosine + NH3
-
the enzyme is involved in the bile duct-inflammation and fibrosis caused chronic fascioliasis including an atrophy of the liver parenchyma and liver cirrhosis
-
-
ir
adenosine + H2O
inosine + NH3
-
adenosine deamination is involved in the essential pathway of purine salvage in Plasmodium falciparum, and inhibition of purine salvage results in parasite death
-
-
?
additional information
?
-
-
regulatory role of dipeptidyl peptidase IV on adenosine deaminase activity
-
-
?
additional information
?
-
-
the enzyme is bound and complexed by the cell membraneous dipeptidyl peptidase IV, which is identical to the activated immune cell antigen CD26, playing a role in the immune system, overview
-
-
?
additional information
?
-
-
adenosine deaminase inhibition enhances the efficiency of signal transduction and inotropic response mediated by A1 adenosine receptor in hyperthyroid guinea pig atrium via elevated intracellular adenosine levels, overview
-
-
?
additional information
?
-
-
the enzyme is involved in purine metabolism and plays an important role in the mechanism of the immune system
-
-
?
additional information
?
-
-
the large isozyme is bound and complexed by the cell membraneous dipeptidyl peptidase IV, which is identical to the activated immune cell antigen CD26, playing a role in the immune system, overview
-
-
?
additional information
?
-
-
adenosine modulates the immune system and inhibits inflammation via reduction of cytokine biosynthesis and neutrophil functions, enzyme inhibition reduces inflammation in experimental colitis, overview
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
the activity found in the enzymes expressed with added Zn(II) and added Fe(II) are 2fold higher than when expressed with Ni(II) or without additional metal
Fe3+
Mg2+
Ni2+
Zn2+
additional information
Ni2+
the activity found in the enzymes expressed with added Zn(II) and added Fe(II) are 2fold higher than when expressed with Ni(II) or without additional metal
Zn2+
the activity found in the enzymes expressed with added Zn(II) and added Fe(II) are 2fold higher than when expressed with Ni(II) or without additional metal
Zn2+
ADA contains a tightly bound Zn2+ which is required for activity, the stability of the protein is decreased significantly in the absence of Zn2+
additional information
-
there are no significant changes in ADA activity in the presence of cadmium acetate, potassium dichromate, lead acetate, zinc chloride, copper sulfate, cobalt chloride, and manganese chloride
additional information
metal-dependent enzyme. The metal can not be removed from the enzyme nor can the nature of the catalytic metal be established. Dialysis of the wild-type enzyme for 3 days against a dipicolinic acid containing buffer fails to show any lowering enzyme activity, again indicating that chelation is not able to remove the bound metal in the active site. The catalytic metal is not removed by EDTA
additional information
-
metal-dependent enzyme. The metal can not be removed from the enzyme nor can the nature of the catalytic metal be established. Dialysis of the wild-type enzyme for 3 days against a dipicolinic acid containing buffer fails to show any lowering enzyme activity, again indicating that chelation is not able to remove the bound metal in the active site. The catalytic metal is not removed by EDTA
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2S,3R)-3-(6-amino-9H-purin-9-yl)-5-[3-(trifluoromethyl)phenyl]pentan-2-ol
comopound shows suitable balance of potency, microsomal stability and demonstrates better pharmacokinetic properties as compared to (+)-erythro-9-(2-hydroxy-3-nonyl)adenine
(2S,3R)-3-(6-amino-9H-purin-9-yl)-5-[4-(trifluoromethyl)phenyl]pentan-2-ol
comopound shows suitable balance of potency, microsomal stability and demonstrates better pharmacokinetic properties as compared to (+)-erythro-9-(2-hydroxy-3-nonyl)adenine
1-(4-benzylphenyl)-3-[4-[(4-oxo-4,5-dihydro-2H-pyrazolo[3,4-d]pyrimidin-2-yl)methyl]phenyl]urea
-
1-(4-fluorophenyl)-3-[4-[(4-oxo-4,5-dihydro-2H-pyrazolo[3,4-d]pyrimidin-2-yl)methyl]phenyl]urea
-
1-(4-methoxyphenyl)-3-[4-[(4-oxo-4,5-dihydro-2H-pyrazolo[3,4-d]pyrimidin-2-yl)methyl]phenyl]urea
-
1-benzyl-3-[4-[(4-oxo-4,5-dihydro-2H-pyrazolo[3,4-d]pyrimidin-2-yl)methyl]phenyl]urea
-
1-[(1R)-1-(hydroxymethyl)-3-(6-[[(1-methyl-1H-benzimidazol-2-yl)acetyl]amino]-1H-indol-1-yl)propyl]-1H-imidazole-4-carboxamide
-
1-[(1R)-1-(hydroxymethyl)-3-naphthalen-1-ylpropyl]-1H-imidazole-4-carboxamide
-
1-[(1R)-3-[6-(acetylamino)-1H-indol-1-yl]-1-(hydroxymethyl)propyl]-1H-imidazole-4-carboxamide
-
1-[(1R)-3-[6-(hexanoylamino)-1H-indol-1-yl]-1-(hydroxymethyl)propyl]-1H-imidazole-4-carboxamide
-
1-[(1R,2S)-2-hydroxy-1-(2-naphthalen-1-ylethyl)propyl]-1H-imidazole-4-carboxamide
-
1-[(2S,3R)-2,3-dihydroxycyclopentyl]-5-(1,3-thiazol-5-yl)pyrimidine-2,4(1H,3H)-dione
28% inhibition at 0.1 mM
1-[(2S,3R)-2,3-dihydroxycyclopentyl]-5-(furan-2-yl)pyrimidine-2,4(1H,3H)-dione
35% inhibition at 0.1 mM
1-[(2S,3R)-2,3-dihydroxycyclopentyl]-5-(thiophen-2-yl)pyrimidine-2,4(1H,3H)-dione
36% inhibition at 0.1 mM
1-[(3R,4S)-4-hydroxy-1-[3-(trifluoromethyl)phenyl]pentan-3-yl]-1H-imidazole-4-carboxamide
comopound shows suitable balance of potency, microsomal stability and demonstrates better pharmacokinetic properties as compared to (+)-erythro-9-(2-hydroxy-3-nonyl)adenine
1-[(4R,5S)-4,5-dihydroxycyclopent-2-en-1-yl]-5-(1,3-thiazol-5-yl)pyrimidine-2,4(1H,3H)-dione
49% inhibition at 0.1 mM
1-[(4R,5S)-4,5-dihydroxycyclopent-2-en-1-yl]-5-(furan-2-yl)pyrimidine-2,4(1H,3H)-dione
55% inhibition at 0.1 mM
1-[(4R,5S)-4,5-dihydroxycyclopent-2-en-1-yl]-5-(thiophen-2-yl)pyrimidine-2,4(1H,3H)-dione
48% inhibition at 0.1 mM
1-[(R)-1-hydroxy-4-(1-methyl-5-(3-phenylpropoxy)indol-3-yl)-2-butyl]imidazole-4-carboxamide
-
1-[(R)-1-hydroxy-4-(5-(3-phenylpropoxy)indol-1-yl)-2-butyl]imidazole-4-carboxamide
-
1-[(R)-1-hydroxy-4-(6-(3-(1-methylbenzimidazol-2-yl)propionylamino)indol-1-yl)-2-butyl]imidazole-4-carboxamide
-
1-[(R)-1-hydroxy-4-(6-(3-(3-pyridyl)propionylamino)indol-1-yl)-2-butyl]imidazole-4-carboxamide
-
1-[(R)-1-hydroxy-4-(6-(3-(4-methoxyphenyl)propionylamino)indol-1-yl)-1-hydroxy-2-butyl]imidazole-4-carboxamide
-
1-[(R)-1-hydroxy-4-(6-(3-(4-methylphenyl)propionylamino)indol-1-yl)-2-butyl]imidazole-4-carboxamide
-
1-[(R)-1-hydroxy-4-(6-(3-phenylpropionylamino)indol-1-yl)-2-butyl]imidazole-4-carboxamide
-
1-[(R)-1-hydroxy-4-(6-(3-phenylpropoxy)indol-1-yl)-2-butyl]imidazole-4-carboxamide
-
1-[(R)-1-hydroxy-4-(6-(4-(4-methylphenyl)butyrylamino)indol-1-yl)-2-butyl]imidazole-4-carboxamide
-
1-[(R)-1-hydroxy-4-(6-(4-phenylbutoxy)indol-1-yl)-2-butyl]imidazole-4-carboxamide
-
1-[(R)-1-hydroxy-4-(6-(4-phenylbutyrylamino)indol-1-yl)-2-butyl]imidazole-4-carboxamide
-
1-[(R)-1-hydroxy-4-(6-(5-phenylvalerylamino)indol-1-yl)-2-butyl]imidazole-4-carboxamide
-
1-[(R)-1-hydroxy-4-(6-(6-phenylhexanoylamino)indol-1-yl)-2-butyl]imidazole-4-carboxamide
-
1-[(R)-4-(5-(3-(4-chlorophenyl)propoxyl)-1-methylindol-3-yl)-1-hydroxy-2-butyl]imidazole-4-carboxamide
-
1-[(R)-4-(5-hexyloxy-1-methylindol-3-yl)-1-hydroxy-2-butyl]imidazole-4-carboxamide
-
1-[(R)-4-(5-hexyloxyindol-1-yl)-1-hydroxy-2-butyl]imidazole-4-carboxamide
-
1-[(R)-4-(6-(3-(4-chlorophenyl)propoxy)indol-1-yl)-1-hydroxy-2-butyl]imidazole-4-carboxamide
-
1-[(R)-4-(6-(3-benzylureido)indol-1-yl)-1-hydroxy-2-butyl]imidazole-4-carboxamide
-
1-[(R)-4-(6-acetylaminoindol-1-yl)-1-hydroxy-2-butyl]imidazole-4-carboxamide
-
1-[(R)-4-(6-hexanoylaminoindol-1-yl)-1-hydroxy-2-butyl]imidazole-4-carboxamide
-
1-[(R)-4-(6-hexyloxyindol-1-yl)-1-hydroxy-2-butyl]imidazole-4-carboxamide
-
1-[4-(dimethylamino)phenyl]-3-[4-[(4-oxo-4,5-dihydro-2H-pyrazolo[3,4-d]pyrimidin-2-yl)methyl]phenyl]urea
-
1-[4-[(4-oxo-4,5-dihydro-2H-pyrazolo[3,4-d]pyrimidin-2-yl)methyl]phenyl]-3-(4-phenoxyphenyl)urea
-
1-[4-[(4-oxo-4,5-dihydro-2H-pyrazolo[3,4-d]pyrimidin-2-yl)methyl]phenyl]-3-phenylurea
-
1-[4-[(4-oxo-4,5-dihydro-2H-pyrazolo[3,4-d]pyrimidin-2-yl)methyl]phenyl]-3-[4-(trifluoromethyl)phenyl]urea
-
2'-deoxy-4-amino-1-(beta-D-ribofuranosyl)-3H-imidazo[4,5-d]pyridazin-7-(6H)-one
-
-
2'-deoxy-7-amino-1-(beta-D-ribofuranosyl)-1H-imidazo[4,5-d]pyridazin-4-(5H)-one
-
-
2,2,2-trifluoro-N-[7-chloro-5-methyl-3-(2,3,5-tri-O-acetyl-beta-D-ribofuranosyl)-3H-imidazo[4,5-b]pyridin-6-yl]-acetamide
20% inhibition at 0.4 mM
2,2,2-trifluoro-N-[7-chloro-5-methyl-3-(beta-D-ribofuranosyl)-3H-imidazo[4,5-b]pyridin-6-yl]acetamide
23% inhibition at 0.4 mM
4-fluoro-N-[4-[(4-oxo-4,5-dihydro-2H-pyrazolo[3,4-d]pyrimidin-2-yl)methyl]phenyl]benzamide
-
4-methoxy-N-[4-[(4-oxo-4,5-dihydro-2H-pyrazolo[3,4-d]pyrimidin-2-yl)methyl]phenyl]benzamide
-
5-(beta-D-ribofuranosyl)-1H,5H-imidazo[4,5-b]pyrazolo[3,4-e]pyridine
25% inhibition at 0.4 mM
5-methyl-3-(2,3,5-tri-O-acetyl-beta-D-ribofuranosyl)-3H-imidazo[4,5-b]pyridin-6-amine
19% inhibition at 0.4 mM
5-methyl-3-(beta-D-ribofuranosyl)-3H-imidazo[4,5-b]pyridin-6-amine
6% inhibition at 0.4 mM
5-methyl-6-nitro-3-(2,3,5-tri-O-acetyl-beta-D-ribofuranosyl)-3H-imidazo[4,5-b]pyridine
31% inhibition at 0.4 mM
5-methyl-6-nitro-3-(beta-D-ribofuranosyl)-3H-imidazo[4,5-b]pyridine
25% inhibition at 0.4 mM
6-fluoro-D,L-tryptophan
adenosine analogue, induces conformational changes inhibiting the enzyme, structural mechanism, overview
7,8-dihydro-1-p-methoxybenzyl-6H-6,7-dimethyl-8-propoxyimidazo[4,5-e][1,2,4]-triazepine
-
-
7,8-dihydro-1-p-methoxybenzyl-8-(2-methoxyethoxy)-6H-6,7-dimethylimidazo[4,5-e][1,2,4]triazepine
-
-
7,8-dihydro-1-p-methoxybenzyl-8-(3-methylbenzyloxy)-6H-6,7-dimethylimidazo[4,5-e][1,2,4]triazepine
-
-
7,8-dihydro-1-p-methoxybenzyl-8-(4-methoxybenzyloxy)-6H-6,7-dimethylimidazo[4,5-e][1,2,4]triazepine
-
-
7,8-dihydro-8-ethoxy-1-p-methoxybenzyl-6H-6,7-dimethylimidazo[4,5-e][1,2,4]triazepine
-
-
7,8-dihydro-8-isopropoxy-1-p-methoxybenzyl-6H-6,7-dimethylimidazo[4,5-e][1,2,4]triazepine
-
-
7,8-dihydro-8-methoxy-1-p-methoxybenzyl-6H-6,7-dimethylimidazo[4,5-e][1,2,4]triazepine
-
-
7-(beta-D-ribofuranosyl)-1H,7H-imidazo[4,5-b]pyrazolo[3,4-e]pyridine
7% inhibition at 0.4 mM
7-chloro-5-methyl-3-(beta-D-ribofuranosyl)-3H-imidazo[4,5-b]pyridin-6-amine
15% inhibition at 0.4 mM
8-butoxy-7,8-dihydro-1-p-methoxybenzyl-6H-6,7-dimethylimidazo[4,5-e][1,2,4]triazepine
-
-
adenosine analogues
induce conformational changes inhibiting the enzyme, structural mechanism, overview
-
aspirin
-
significantly decreases adenosine deaminase activity, the half-life of adenosine will be lengthened as a consequence of decreased adenosine deaminase activity
caffeic acid phenethyl ester
-
reduces the enzyme activity in vivo, suppresses the induction of the enzyme by cisplatin in vivo
dodecyltrimethylammonium bromide
at low concentrations (approximately 0.1 mM), enzyme activity decreases, it increases at a slightly higher concentration (about 0.2 mM), and finally decreases again (about 0.3 mM), CD spectra of adenosine deaminase and DTAB, determination of helix content, MD calculations
epigallocatechin gallate
most abundant and biologically active ?avonoid present in green tea, strong competitive inhibitory activity
ethanol
CD spectra of adenosine deaminase and EtOH, determination of helix content, MD calculations
FR234938
-
i.e. 1-((1R,2S)-2-hydroxy-1-(2-(1-naphthyl)ethyl)propyl)1H-imidazole-4-carboxamine, a non-nucleoside inhibitor, the inhibition is blocked by an A2a adenosine receptor antagonist
HgCl2
-
inhibition of ADA activity is observed in the soluble fraction at 0.005-0.25 mM HgCl2 (84.6-92.6% respectively), whereas inhibition occurs at 0.005-0.25 mM in membrane fractions (20.9-26% respectively). The inhibition is partially or fully abolished by 0.5 mM dithiothreitol or EDTA
indole-3-acetic acid
-
the plant hormone decreases enzyme activity in hearts, but not in kidney and muscle
isosorbide mononitrate
-
significantly decreases adenosine deaminase activity, the half-life of adenosine will be lengthened as a consequence of decreased adenosine deaminase activity
kinetin
-
the plant hormone decreases enzyme activity in hearts, but not in kidney and muscle
methylmercury
-
concentration 0.1, 1.0, 20 M, inhibits adenosine deaminase activity in 7- and 60-day-old rats in a concentration-dependent manner, glutathione (50 microM) and dithiothreitol (50 microM) prevent the reduction of adenosine deaminase activity both in cerebral cortex and hippocampus, garlic alcoholic extract (100 microg/ml) abolishes the reduction of adenosine deaminase
metoprolol
-
significantly decreases adenosine deaminase activity, the half-life of adenosine will be lengthened as a consequence of decreased adenosine deaminase activity
N-[4-[(4-oxo-4,5-dihydro-2H-pyrazolo[3,4-d]pyrimidin-2-yl)methyl]phenyl]-2-phenylacetamide
-
N-[4-[(4-oxo-4,5-dihydro-2H-pyrazolo[3,4-d]pyrimidin-2-yl)methyl]phenyl]-4-(trifluoromethyl)benzamide
-
N-[4-[(4-oxo-4,5-dihydro-2H-pyrazolo[3,4-d]pyrimidin-2-yl)methyl]phenyl]benzamide
-
Na2SO4
CD spectra of adenosine deaminase and Na2SO4, determination of helix content, MD calculations, discussion of effects
progesterone
-
progesterone decreases adenosine deaminase levels, adenosine deaminase levels show regional specificity with differences among the cerebral hemispheres, cerebellum, and brainstems structures
simvastatin
-
inhibits ADA1 activity by 46.7%; significantly decreases adenosine deaminase activity, the half-life of adenosine will be lengthened as a consequence of decreased ADA activity
Sodium dodecyl sulfate
at low concentrations (approximately 0.1 mM) enzyme activity decreases, it increases at a slightly higher concentration (about 0.4 mM), and finally decreases again (about 0.55 mM), CD spectra of adenosine deaminase and SDS, determination of helix content, MD calculations
(+)-erythro-9-(2-hydroxy-3-nonyl)adenine
specific inhibitor of ADA1
2'-deoxycoformycin
-
a natural product transition state analogue inhibitor
5'-methylthiocoformycin
-
specific transition state analogue inhibitor of Plasmodium ADA
5'-methylthiocoformycin
-
specific transition state analogue inhibitor of Plasmodium ADA
5'-methylthiocoformycin
-
specific transition state analogue inhibitor of Plasmodium ADA, 5'-methylthiocoformycin is a subnanomolar inhibitor of Plasmodium falciparum ADA and demonstrates more than 20000fold selectivity relative to human ADA
5'-methylthiocoformycin
-
poor inhibitor of Plasmodium gallinaceum ADA
5'-methylthiocoformycin
-
specific transition state analogue inhibitor of Plasmodium ADA
5'-methylthiocoformycin
-
specific transition state analogue inhibitor of Plasmodium ADA
corticosterone
inhibits the adenosine deaminase activity in an age- and region-specific manner
erythro-9-(2-hydroxy-3-nonyl)-adenine
-
0.1 mM concentration, ADA2 is practically unaffected; 0.1 mM concentration, complete and reversible inhibition
erythro-9-(2-hydroxy-3-nonyl)adenine
-
i.e. EHNA, specific for isozyme ADA1, no inhibition of isozyme ADA2
erythro-9-(2-hydroxy-3-nonyl)adenine
-
ADA-specific inhibitor, almost complete inhibition at 0.00005 mM
pentostatin
-
i.e. (8R)-3-[(2R,4S,5R)-4-hydroxy-5-(hydroxymethyl)tetrahydro-2-furanyl]-3,6,7,8-tetrahydroimidazo[4,5-d][1,3]diazepin-8-ol
purine riboside
adenosine analogue, induces conformational changes inhibiting the enzyme, structural mechanism, overview
Zn2+
-
decrease of 31.3% on adenosine deamination in membranes is observed in the presence of 5 mM Zn2+
additional information
structure-based design, synthesis, and structure-activity relationship studies of non-nucleoside adenosine deaminase inhibitors, overview
-
additional information
-
molecular dynamic simulations of inhibitor-enzyme interaction, overview
-
additional information
-
no inhibition of the bovine enzyme by 5'-methylthiocoformycin and 5'-methylthio-2'-deoxycoformycin
-
additional information
-
cytotoxic effects of inhibitors against human breast cancer cell lines MCF-7 and MCF-10A
-
additional information
the trend of relative activity is directly proportional to helicity and inversely proportional to accessible surface area
-
additional information
-
no inhibition by erythro-9-(2-hydroxy-3-nonyl)-adenine hydrochloride
-
additional information
-
no inhibition of the human enzyme by 5'-methylthiocoformycin and 5'-methylthio-2'-deoxycoformycin
-
additional information
-
strong inhibition by the traditional Chinese medicines Rhizoma Chuanxiong and Angelica sinensis
-
additional information
loss of activity precedes the global secondary and tertiary structure transition when the enzyme is exposed to denaturant, structural mechanism, overview
-
additional information
-
loss of activity precedes the global secondary and tertiary structure transition when the enzyme is exposed to denaturant, structural mechanism, overview
-
additional information
-
ADA1 activity is not changed significantly by aspirin, metoprolol, isosorbide mononitrate, and molsidominemolsidomine; molsidomine does not influence plasma adenosine deaminase activity significantly
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cisplatin
-
cisplatin intoxification increases the enzyme activity in vivo, supressable by caffeic acid phenethyl ester
dibutyryl-cAMP
causes a significant increase in the activity level of adenosine deaminase depending on the regions of the gastrointestinal tract
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0044
5'-methylthioadenosine
-
wild type enzyme, in 100 mM Tris-HCl buffer (pH 8.0), temperature not specified in the publication
0.0087
5'-methylthioadenosine
-
wild type enzyme, in 100 mM Tris-HCl buffer (pH 8.0), temperature not specified in the publication
0.0095
5'-methylthioadenosine
-
wild type enzyme, in 100 mM Tris-HCl buffer (pH 8.0), temperature not specified in the publication
0.022
5'-methylthioadenosine
-
wild type enzyme, in 100 mM Tris-HCl buffer (pH 8.0), temperature not specified in the publication
0.0306
5'-methylthioadenosine
pH 8.0, temperature not specified in the publication, wild-type enzyme
0.04461
5'-methylthioadenosine
pH 8.0, temperature not specified in the publication, mutant enzyme C27Q/L227I
0.05256
5'-methylthioadenosine
pH 8.0, temperature not specified in the publication, mutant enzyme L179H
0.115
5'-methylthioadenosine
-
wild type enzyme, in 100 mM Tris-HCl buffer (pH 8.0), temperature not specified in the publication
0.20034
5'-methylthioadenosine
pH 8.0, temperature not specified in the publication, mutant enzyme T174A
0.22422
5'-methylthioadenosine
pH 8.0, temperature not specified in the publication, mutant enzyme D176A/L179A
0.25326
5'-methylthioadenosine
pH 8.0, temperature not specified in the publication, mutant enzyme D176M
0.26747
5'-methylthioadenosine
pH 8.0, temperature not specified in the publication, mutant enzyme T174I
0.28928
5'-methylthioadenosine
pH 8.0, temperature not specified in the publication, mutant enzyme D176A
0.37605
5'-methylthioadenosine
pH 8.0, temperature not specified in the publication, mutant enzyme F136L
0.00943
adenosine
pH 8.0, temperature not specified in the publication, mutant enzyme T174I
0.01728
adenosine
pH 8.0, temperature not specified in the publication, mutant enzyme, wild-type enzyme (refolded)
0.01784
adenosine
pH 8.0, temperature not specified in the publication, wild-type enzyme
0.02064
adenosine
pH 8.0, temperature not specified in the publication, wild-type enzyme
0.02113
adenosine
pH 8.0, temperature not specified in the publication, mutant enzyme L179H
0.02344
adenosine
pH 8.0, temperature not specified in the publication, mutant enzyme C27Q/L227I
0.026
adenosine
-
25°C, 50 mM Tris-HCl buffer, pH 7.4, enzyme concentration 1.5 nM
0.032
adenosine
-
wild type enzyme, in 100 mM Tris-HCl buffer (pH 8.0), temperature not specified in the publication
0.03874
adenosine
pH 8.0, temperature not specified in the publication, mutant enzyme M155A
0.04203
adenosine
pH 8.0, temperature not specified in the publication, mutant enzyme T174A
0.05641
adenosine
pH 8.0, temperature not specified in the publication, mutant enzyme M155A (refolded)
0.057
adenosine
-
wild type enzyme, in 100 mM Tris-HCl buffer (pH 8.0), temperature not specified in the publication
0.06
adenosine
-
wild type enzyme, in 100 mM Tris-HCl buffer (pH 8.0), temperature not specified in the publication
0.072
adenosine
pH and temperature not specified in the publication, mutant enzyme Y136R
0.083
adenosine
-
mutant enzyme D172E, in 100 mM Tris-HCl buffer (pH 8.0), temperature not specified in the publication
0.087
adenosine
-
wild type enzyme, in 100 mM Tris-HCl buffer (pH 8.0), temperature not specified in the publication
0.088
adenosine
-
wild type enzyme, in 100 mM Tris-HCl buffer (pH 8.0), temperature not specified in the publication
0.104
adenosine
-
mutant enzyme D172A, in 100 mM Tris-HCl buffer (pH 8.0), temperature not specified in the publication
0.12
adenosine
-
wild type enzyme, in 100 mM Tris-HCl buffer (pH 8.0), temperature not specified in the publication
0.12628
adenosine
pH 8.0, temperature not specified in the publication, mutant enzyme D176A
0.15
adenosine
pH and temperature not specified in the publication, wild-type enzyme
0.15
adenosine
pH and temperature not specified in the publication, mutant enzyme E150R
0.15897
adenosine
pH 8.0, temperature not specified in the publication, mutant enzyme D176A/L179A
0.29961
adenosine
pH 8.0, temperature not specified in the publication, mutant enzyme D176M
0.32206
adenosine
pH 8.0, temperature not specified in the publication, mutant enzyme F136L
additional information
additional information
thermodynamics and kinetics
-
additional information
additional information
-
isozymes ADA1 and ADA2 are kinetically distinct
-
additional information
additional information
-
kinetics of the large and the small isozyme
-
additional information
additional information
-
kinetics of the large and the small isozyme
-
additional information
additional information
-
optimization of a spectrometric kinetic measurement method pure enzyme, kinetics in presence of substrate, product and inhibtior, overview
-
additional information
additional information
-
optimization of a spectrometric kinetic measurement method using Hut78 cell extract, kinetics in presence of substrate, product and inhibtior, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.13
5'-methylthioadenosine
-
wild type enzyme, in 100 mM Tris-HCl buffer (pH 8.0), temperature not specified in the publication
0.31
5'-methylthioadenosine
-
wild type enzyme, in 100 mM Tris-HCl buffer (pH 8.0), temperature not specified in the publication
0.33
5'-methylthioadenosine
pH 8.0, temperature not specified in the publication, mutant enzyme T174I
0.35
5'-methylthioadenosine
-
wild type enzyme, in 100 mM Tris-HCl buffer (pH 8.0), temperature not specified in the publication
0.51
5'-methylthioadenosine
-
wild type enzyme, in 100 mM Tris-HCl buffer (pH 8.0), temperature not specified in the publication
0.69
5'-methylthioadenosine
pH 8.0, temperature not specified in the publication, mutant enzyme F136L
1.75
5'-methylthioadenosine
pH 8.0, temperature not specified in the publication, mutant enzyme D176A/L179A
1.78
5'-methylthioadenosine
pH 8.0, temperature not specified in the publication, mutant enzyme D176M
4.48
5'-methylthioadenosine
pH 8.0, temperature not specified in the publication, mutant enzyme T174A
5.49
5'-methylthioadenosine
pH 8.0, temperature not specified in the publication, mutant enzyme D176A
5.8
5'-methylthioadenosine
-
wild type enzyme, in 100 mM Tris-HCl buffer (pH 8.0), temperature not specified in the publication
12.17
5'-methylthioadenosine
pH 8.0, temperature not specified in the publication, mutant enzyme C27Q/L227I
13.92
5'-methylthioadenosine
pH 8.0, temperature not specified in the publication, wild-type enzyme
14.07
5'-methylthioadenosine
pH 8.0, temperature not specified in the publication, mutant enzyme L179H
0.31
adenosine
pH 8.0, temperature not specified in the publication, mutant enzyme D176A/L179A
0.97
adenosine
pH 8.0, temperature not specified in the publication, mutant enzyme D176M
1.31
adenosine
pH 8.0, temperature not specified in the publication, mutant enzyme F136L
1.8
adenosine
-
wild type enzyme, in 100 mM Tris-HCl buffer (pH 8.0), temperature not specified in the publication
1.9
adenosine
-
wild type enzyme, in 100 mM Tris-HCl buffer (pH 8.0), temperature not specified in the publication
2.42
adenosine
pH 8.0, temperature not specified in the publication, mutant enzyme T174I
4.1
adenosine
pH 8.0, temperature not specified in the publication, wild-type enzyme
4.41
adenosine
pH 8.0, temperature not specified in the publication, mutant enzyme L179H
4.7
adenosine
-
wild type enzyme, in 100 mM Tris-HCl buffer (pH 8.0), temperature not specified in the publication
5.3
adenosine
-
wild type enzyme, in 100 mM Tris-HCl buffer (pH 8.0), temperature not specified in the publication
5.35
adenosine
pH 8.0, temperature not specified in the publication, mutant enzyme M155A (refolded)
5.59
adenosine
pH 8.0, temperature not specified in the publication, mutant enzyme D176A
5.6
adenosine
-
wild type enzyme, in 100 mM Tris-HCl buffer (pH 8.0), temperature not specified in the publication
6.16
adenosine
pH 8.0, temperature not specified in the publication, mutant enzyme C27Q/L227I
6.8
adenosine
-
wild type enzyme, in 100 mM Tris-HCl buffer (pH 8.0), temperature not specified in the publication
7.45
adenosine
pH 8.0, temperature not specified in the publication, mutant enzyme T174A
12.9
adenosine
-
mutant enzyme D172E, in 100 mM Tris-HCl buffer (pH 8.0), temperature not specified in the publication
14
adenosine
-
mutant enzyme D172A, in 100 mM Tris-HCl buffer (pH 8.0), temperature not specified in the publication
28.69
adenosine
pH 8.0, temperature not specified in the publication, mutant enzyme M155A
40.71
adenosine
pH 8.0, temperature not specified in the publication, mutant enzyme, wild-type enzyme (refolded)
80.04
adenosine
pH 8.0, temperature not specified in the publication, wild-type enzyme
110
adenosine
pH and temperature not specified in the publication, wild-type enzyme
110
adenosine
pH and temperature not specified in the publication, mutant enzyme E150R
140
adenosine
pH and temperature not specified in the publication, mutant enzyme Y136R
180
adenosine
-
25°C, 50 mM Tris-HCl buffer, pH 7.4, enzyme concentration 1.5 nM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1
5'-methylthioadenosine
pH 8.0, temperature not specified in the publication, mutant enzyme T174I
2
5'-methylthioadenosine
pH 8.0, temperature not specified in the publication, mutant enzyme F136L
7
5'-methylthioadenosine
pH 8.0, temperature not specified in the publication, mutant enzyme D176M
8
5'-methylthioadenosine
pH 8.0, temperature not specified in the publication, mutant enzyme D176A/L179A
14
5'-methylthioadenosine
-
wild type enzyme, in 100 mM Tris-HCl buffer (pH 8.0), temperature not specified in the publication
20
5'-methylthioadenosine
pH 8.0, temperature not specified in the publication, mutant enzyme D176A
20
5'-methylthioadenosine
pH 8.0, temperature not specified in the publication, mutant enzyme T174A
23
5'-methylthioadenosine
-
wild type enzyme, in 100 mM Tris-HCl buffer (pH 8.0), temperature not specified in the publication
36
5'-methylthioadenosine
-
wild type enzyme, in 100 mM Tris-HCl buffer (pH 8.0), temperature not specified in the publication
50
5'-methylthioadenosine
-
wild type enzyme, in 100 mM Tris-HCl buffer (pH 8.0), temperature not specified in the publication
79
5'-methylthioadenosine
-
wild type enzyme, in 100 mM Tris-HCl buffer (pH 8.0), temperature not specified in the publication
270
5'-methylthioadenosine
pH 8.0, temperature not specified in the publication, mutant enzyme C27Q/L227I
270
5'-methylthioadenosine
pH 8.0, temperature not specified in the publication, mutant enzyme L179H
450
5'-methylthioadenosine
pH 8.0, temperature not specified in the publication, wild-type enzyme
2
adenosine
pH 8.0, temperature not specified in the publication, mutant enzyme D176A/L179A
3
adenosine
pH 8.0, temperature not specified in the publication, mutant enzyme D176M
4
adenosine
pH 8.0, temperature not specified in the publication, mutant enzyme F136L
30
adenosine
-
wild type enzyme, in 100 mM Tris-HCl buffer (pH 8.0), temperature not specified in the publication
40
adenosine
pH 8.0, temperature not specified in the publication, mutant enzyme D176A
57
adenosine
-
wild type enzyme, in 100 mM Tris-HCl buffer (pH 8.0), temperature not specified in the publication
59
adenosine
-
wild type enzyme, in 100 mM Tris-HCl buffer (pH 8.0), temperature not specified in the publication
61
adenosine
-
wild type enzyme, in 100 mM Tris-HCl buffer (pH 8.0), temperature not specified in the publication
64
adenosine
-
wild type enzyme, in 100 mM Tris-HCl buffer (pH 8.0), temperature not specified in the publication
82
adenosine
-
wild type enzyme, in 100 mM Tris-HCl buffer (pH 8.0), temperature not specified in the publication
90
adenosine
pH 8.0, temperature not specified in the publication, mutant enzyme M155A (refolded)
130
adenosine
-
mutant enzyme D172A, in 100 mM Tris-HCl buffer (pH 8.0), temperature not specified in the publication
150
adenosine
-
mutant enzyme D172E, in 100 mM Tris-HCl buffer (pH 8.0), temperature not specified in the publication
180
adenosine
pH 8.0, temperature not specified in the publication, mutant enzyme T174A
210
adenosine
pH 8.0, temperature not specified in the publication, mutant enzyme L179H
230
adenosine
pH 8.0, temperature not specified in the publication, wild-type enzyme
260
adenosine
pH 8.0, temperature not specified in the publication, mutant enzyme C27Q/L227I
260
adenosine
pH 8.0, temperature not specified in the publication, mutant enzyme T174I
740
adenosine
pH 8.0, temperature not specified in the publication, mutant enzyme M155A
750
adenosine
pH and temperature not specified in the publication, wild-type enzyme
750
adenosine
pH and temperature not specified in the publication, mutant enzyme E150R
2360
adenosine
pH 8.0, temperature not specified in the publication, mutant enzyme, wild-type enzyme (refolded)
2900
adenosine
pH and temperature not specified in the publication, mutant enzyme Y136R
3880
adenosine
pH 8.0, temperature not specified in the publication, wild-type enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0000022
(+)-erythro-9-(2-hydroxy-3-nonyl)adenine
pH 7.0, temperature not specified in the publication
0.00000011
(2S,3R)-3-(6-amino-9H-purin-9-yl)-5-[3-(trifluoromethyl)phenyl]pentan-2-ol
pH 7.0, temperature not specified in the publication
0.0000052
(2S,3R)-3-(6-amino-9H-purin-9-yl)-5-[4-(trifluoromethyl)phenyl]pentan-2-ol
pH 7.0, temperature not specified in the publication
0.00186
1-(4-benzylphenyl)-3-[4-[(4-oxo-4,5-dihydro-2H-pyrazolo[3,4-d]pyrimidin-2-yl)methyl]phenyl]urea
30°C, pH 7.12
0.0000115
1-(4-fluorophenyl)-3-[4-[(4-oxo-4,5-dihydro-2H-pyrazolo[3,4-d]pyrimidin-2-yl)methyl]phenyl]urea
30°C, pH 7.9
0.0002827
1-(4-methoxyphenyl)-3-[4-[(4-oxo-4,5-dihydro-2H-pyrazolo[3,4-d]pyrimidin-2-yl)methyl]phenyl]urea
30°C, pH 7.8
0.000857
1-benzyl-3-[4-[(4-oxo-4,5-dihydro-2H-pyrazolo[3,4-d]pyrimidin-2-yl)methyl]phenyl]urea
30°C, pH 7.14
0.000077
1-[(1R)-1-(hydroxymethyl)-3-(6-[[(1-methyl-1H-benzimidazol-2-yl)acetyl]amino]-1H-indol-1-yl)propyl]-1H-imidazole-4-carboxamide
-
0.0068
1-[(1R)-1-(hydroxymethyl)-3-naphthalen-1-ylpropyl]-1H-imidazole-4-carboxamide
-
0.059
1-[(1R)-1-(hydroxymethyl)-3-phenylpropyl]-1H-imidazole-4-carboxamide
-
0.013
1-[(1R)-3-[6-(acetylamino)-1H-indol-1-yl]-1-(hydroxymethyl)propyl]-1H-imidazole-4-carboxamide
-
0.00024
1-[(1R)-3-[6-(hexanoylamino)-1H-indol-1-yl]-1-(hydroxymethyl)propyl]-1H-imidazole-4-carboxamide
-
0.00011
1-[(1R,2S)-2-hydroxy-1-(2-naphthalen-1-ylethyl)propyl]-1H-imidazole-4-carboxamide
-
0.0000059
1-[(3R,4S)-4-hydroxy-1-[3-(trifluoromethyl)phenyl]pentan-3-yl]-1H-imidazole-4-carboxamide
pH 7.0, temperature not specified in the publication
0.000026
1-[(R)-1-hydroxy-4-(1-methyl-5-(3-phenylpropoxy)indol-3-yl)-2-butyl]imidazole-4-carboxamide
-
0.0019
1-[(R)-1-hydroxy-4-(5-(3-phenylpropoxy)indol-1-yl)-2-butyl]imidazole-4-carboxamide
-
0.000011
1-[(R)-1-hydroxy-4-(6-(3-(1-methylbenzimidazol-2-yl)propionylamino)indol-1-yl)-2-butyl]imidazole-4-carboxamide
-
0.000017
1-[(R)-1-hydroxy-4-(6-(3-(3-pyridyl)propionylamino)indol-1-yl)-2-butyl]imidazole-4-carboxamide
-
0.000057
1-[(R)-1-hydroxy-4-(6-(3-(4-methoxyphenyl)propionylamino)indol-1-yl)-1-hydroxy-2-butyl]imidazole-4-carboxamide
-
0.000038
1-[(R)-1-hydroxy-4-(6-(3-(4-methylphenyl)propionylamino)indol-1-yl)-2-butyl]imidazole-4-carboxamide
-
0.00003
1-[(R)-1-hydroxy-4-(6-(3-phenylpropionylamino)indol-1-yl)-2-butyl]imidazole-4-carboxamide
-
0.000017
1-[(R)-1-hydroxy-4-(6-(3-phenylpropoxy)indol-1-yl)-2-butyl]imidazole-4-carboxamide
-
0.000034
1-[(R)-1-hydroxy-4-(6-(4-(4-methylphenyl)butyrylamino)indol-1-yl)-2-butyl]imidazole-4-carboxamide
-
0.000012
1-[(R)-1-hydroxy-4-(6-(4-phenylbutoxy)indol-1-yl)-2-butyl]imidazole-4-carboxamide
-
0.000016
1-[(R)-1-hydroxy-4-(6-(4-phenylbutyrylamino)indol-1-yl)-2-butyl]imidazole-4-carboxamide
-
0.0000077
1-[(R)-1-hydroxy-4-(6-(5-phenylvalerylamino)indol-1-yl)-2-butyl]imidazole-4-carboxamide
-
0.000091
1-[(R)-1-hydroxy-4-(6-(6-phenylhexanoylamino)indol-1-yl)-2-butyl]imidazole-4-carboxamide
-
0.0000049
1-[(R)-4-(5-(3-(4-chlorophenyl)propoxyl)-1-methylindol-3-yl)-1-hydroxy-2-butyl]imidazole-4-carboxamide
-
0.000013
1-[(R)-4-(5-hexyloxy-1-methylindol-3-yl)-1-hydroxy-2-butyl]imidazole-4-carboxamide
-
0.0062
1-[(R)-4-(5-hexyloxyindol-1-yl)-1-hydroxy-2-butyl]imidazole-4-carboxamide
-
0.000013
1-[(R)-4-(6-(3-(4-chlorophenyl)propoxy)indol-1-yl)-1-hydroxy-2-butyl]imidazole-4-carboxamide
-
0.0000075
1-[(R)-4-(6-(3-benzylureido)indol-1-yl)-1-hydroxy-2-butyl]imidazole-4-carboxamide
-
0.0013
1-[(R)-4-(6-acetylaminoindol-1-yl)-1-hydroxy-2-butyl]imidazole-4-carboxamide
-
0.00024
1-[(R)-4-(6-butoxyindol-1-yl)-1-hydroxy-2-butyl]imidazole-4-carboxamide
-
0.000024
1-[(R)-4-(6-hexanoylaminoindol-1-yl)-1-hydroxy-2-butyl]imidazole-4-carboxamide
-
0.000055
1-[(R)-4-(6-hexyloxyindol-1-yl)-1-hydroxy-2-butyl]imidazole-4-carboxamide
-
0.0000201
1-[4-(dimethylamino)phenyl]-3-[4-[(4-oxo-4,5-dihydro-2H-pyrazolo[3,4-d]pyrimidin-2-yl)methyl]phenyl]urea
30°C, pH 7.11
0.00108
1-[4-[(4-oxo-4,5-dihydro-2H-pyrazolo[3,4-d]pyrimidin-2-yl)methyl]phenyl]-3-(4-phenoxyphenyl)urea
30°C, pH 7.13
0.0000242
1-[4-[(4-oxo-4,5-dihydro-2H-pyrazolo[3,4-d]pyrimidin-2-yl)methyl]phenyl]-3-phenylurea
30°C, pH 7.7
0.0000016
1-[4-[(4-oxo-4,5-dihydro-2H-pyrazolo[3,4-d]pyrimidin-2-yl)methyl]phenyl]-3-[4-(trifluoromethyl)phenyl]urea
30°C, pH 7.10
0.0121
2'-deoxy-4-amino-1-(beta-D-ribofuranosyl)-3H-imidazo[4,5-d]pyridazin-7-(6H)-one
-
pH 7.4, 25°C
0.052
2'-deoxy-7-amino-1-(beta-D-ribofuranosyl)-1H-imidazo[4,5-d]pyridazin-4-(5H)-one
-
pH 7.4, 25°C
0.0000034
2'-deoxycoformycin
-
37°C, pH not specified in the publication
0.0106
4-amino-1-(beta-D-ribofuranosyl)-3H-imidazo[4,5-d]pyridazin-7-(6H)-one
-
pH 7.4, 25°C
0.0000096
4-fluoro-N-[4-[(4-oxo-4,5-dihydro-2H-pyrazolo[3,4-d]pyrimidin-2-yl)methyl]phenyl]benzamide
30°C, pH 7.4
0.0001556
4-methoxy-N-[4-[(4-oxo-4,5-dihydro-2H-pyrazolo[3,4-d]pyrimidin-2-yl)methyl]phenyl]benzamide
30°C, pH 7.3