Any feedback?
Information on EC 3.5.4.4 - adenosine deaminase and Organism(s) Bos taurus and UniProt Accession P56658
for references in articles please use BRENDA:EC3.5.4.4Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
3.5.4.4 adenosine deaminaseIUBMB Comments
The enzyme, found in a wide variety of microorganisms, plants, invertebrates, and animals, plays a role in purine metabolism.
Specify your search results
Word Map
- 3.5.4.4
- purine
- nucleoside
- lymphocyte
- immunodeficiency
- inosine
- pleural
-
tuberculous
-
deamination
- effusion
- erythrocyte
- phosphorylase
- agonist
- leukemia
- 5'-nucleotidase
- deoxyadenosine
- marrow
- xanthine
- adenylate
- hypoxanthine
- t-cells
-
lymphoid
- ehna
- dipyridamole
-
purinergic
-
hematopoietic
-
exudative
-
lipolysis
- pleurisy
- meningitis
- theophylline
- datp
-
ecto-5\'-nucleotidase
- s-adenosylhomocysteine
- 2-chloroadenosine
- dpcpx
-
autoinflammatory
- pericarditis
-
acid-fast
- deoxycytidine
-
transudate
-
antilipolytic
-
diphosphohydrolase
-
hypoxanthine-guanine
-
adenosine-induced
- ectonucleotidases
-
n6-cyclopentyladenosine
- empyema
- deaminases
- ntpdases
-
purinoceptors
- medicine
- pharmacology
- drug development
- diagnostics
- analysis
The taxonomic range for the selected organisms is: Bos taurus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
adenosine deaminase, adenosine deaminase 2, adenosine aminohydrolase, adenosine deaminase 1, adaii, pvada, mj1541, ciada, sco4901, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ADA
-
-
Adenosine aminohydrolase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
adenosine + H2O = inosine + NH3
reaction mechanism, structure-function relationship of ADA and dipeptidyl peptidase IV
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Deamination
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
adenosine aminohydrolase
The enzyme, found in a wide variety of microorganisms, plants, invertebrates, and animals, plays a role in purine metabolism.
CAS REGISTRY NUMBER
COMMENTARY
9026-93-1
-
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'-O-isopropylidenadenosine + H2O
2',3'-O-isopropylideninosine + NH3
modeling studies
-
-
?
2',3'-O-methoxymethylideneadenosine + H2O
2',3'-O-methoxymethylideneinosine + NH3
modeling studies
-
-
?
2',3'-O-isopropylidene adenosine + H2O
2',3'-O-isopropylidene inosine + NH3
-
-
-
-
?
adenosine + H2O
inosine + NH3
key enzyme involved in the purine metabolism
-
-
?
adenosine + H2O
inosine + NH3
-
-
-
-
?
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
-
-
?
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
adenosine + H2O
inosine + NH3
key enzyme involved in the purine metabolism
-
-
?
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
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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-[(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
-
2,2,2-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
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
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
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
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
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
-
-
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
-
-
8-butoxy-7,8-dihydro-1-p-methoxybenzyl-6H-6,7-dimethylimidazo[4,5-e][1,2,4]triazepine
-
-
additional information
structure-based design, synthesis, and structure-activity relationship studies of non-nucleoside adenosine deaminase inhibitors, overview
-
additional information
the trend of relative activity is directly proportional to helicity and inversely proportional to accessible surface area
-
additional information
-
molecular dynamic simulations of inhibitor-enzyme interaction, overview
-
additional information
-
cytotoxic effects of inhibitors against human breast cancer cell lines MCF-7 and MCF-10A
-
additional information
-
no inhibition of the bovine enzyme by 5'-methylthiocoformycin and 5'-methylthio-2'-deoxycoformycin
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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 inhibitor, overview
-
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
0.0000059
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
0.0000096
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
0.000478
N-[4-[(4-oxo-4,5-dihydro-2H-pyrazolo[3,4-d]pyrimidin-2-yl)methyl]phenyl]-2-phenylacetamide
30°C, pH 7.6
0.000051
N-[4-[(4-oxo-4,5-dihydro-2H-pyrazolo[3,4-d]pyrimidin-2-yl)methyl]phenyl]-4-(trifluoromethyl)benzamide
30°C, pH 7.5
0.0001265
N-[4-[(4-oxo-4,5-dihydro-2H-pyrazolo[3,4-d]pyrimidin-2-yl)methyl]phenyl]benzamide
30°C, pH 7.2
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
0.0106
4-amino-1-(beta-D-ribofuranosyl)-3H-imidazo[4,5-d]pyridazin-7-(6H)-one
-
pH 7.4, 25°C
0.0265
5-carbamimidoyl-1-(beta-D-ribofuranosyl)-1H-imidazole-4-carbohydrazide
-
pH 7.4, 25°C
0.012
7,8-dihydro-1-p-methoxybenzyl-6H-6,7-dimethyl-8-propoxyimidazo[4,5-e][1,2,4]-triazepine
-
pH 7.0, 25°C
0.023
7,8-dihydro-1-p-methoxybenzyl-8-(2-methoxyethoxy)-6H-6,7-dimethylimidazo[4,5-e][1,2,4]triazepine
-
pH 7.0, 25°C
0.093
7,8-dihydro-1-p-methoxybenzyl-8-(3-methylbenzyloxy)-6H-6,7-dimethylimidazo[4,5-e][1,2,4]triazepine
-
pH 7.0, 25°C
0.077
7,8-dihydro-1-p-methoxybenzyl-8-(4-methoxybenzyloxy)-6H-6,7-dimethylimidazo[4,5-e][1,2,4]triazepine
-
pH 7.0, 25°C
0.02
7,8-dihydro-8-ethoxy-1-p-methoxybenzyl-6H-6,7-dimethylimidazo[4,5-e][1,2,4]triazepine
-
pH 7.0, 25°C
0.03
7,8-dihydro-8-isopropoxy-1-p-methoxybenzyl-6H-6,7-dimethylimidazo[4,5-e][1,2,4]triazepine
-
pH 7.0, 25°C
0.024
7,8-dihydro-8-methoxy-1-p-methoxybenzyl-6H-6,7-dimethylimidazo[4,5-e][1,2,4]triazepine
-
pH 7.0, 25°C
0.0514
7-amino-1-(beta-D-ribofuranosyl)-1H-imidazo[4,5-d]pyridazin-4-(5H)-one
-
pH 7.4, 25°C
0.015
8-butoxy-7,8-dihydro-1-p-methoxybenzyl-6H-6,7-dimethylimidazo[4,5-e][1,2,4]triazepine
-
pH 7.0, 25°C
0.0074
1-deazaadenosine
-
pH 7.1, 23°C, after preincubation with diethyl dicarbonate
0.00005
3-deaza-erythro-9-(2-hydroxy-3-nonyl)adenine
-
kidney cortex large isozyme
0.00009
diethyl dicarbonate
-
pH 7.1, 23°C, in presence of 0.022 mM erythro-9-(2-hydroxy-3-nonyl)-adenine
0.00013
diethyl dicarbonate
-
pH 7.1, 23°C, in presence of 0.03 mM erythro-9-(2-hydroxy-3-nonyl)-3-deazaadenine
0.00011
erythro-9-(2-hydroxy-3-nonyl)-3-deazaadenine
-
pH 7.1, 23°C, after preincubation with diethyl dicarbonate
0.00007
erythro-9-(2-hydroxy-3-nonyl)-adenine
-
pH 7.1, 23°C, after preincubation with diethyl dicarbonate
additional information
additional information
-
the adenine moiety of inhibitors does not bind to the histidine residues of the active site His238
-
additional information
additional information
-
inhibition kinetics of the large and the small isozyme
-
additional information
additional information
-
kinetics and thermodynamic effects of inhibitors, QSAR analysis, overview
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.9
enzymatic data, conformational properties and docking scores for adenosine analogue 2,3-O-isopropylidenadenosine, modeling studies
2
enzymatic data, conformational properties and docking scores for adenosine analogue 2,3-O-methoxymethylideneadenosine, modeling studies
0.5
additional information
additional information
no activity with substrate 9H-(1-deoxy-3,4-O-isopropylidene-beta-D-psicofuranosyl)adenine, adenosine deaminase aptly transforms substrates largely modified at the 2- and 3-O-positions, whereas C-modification at the 1-position prevents the adenosine deaminase-catalyzed deamination
additional information
-
the serum adenosine deaminase activity increases significantly in all infected groups compared to control group (adenosine deaminase activity: 5.99 IU/l control group, 27.62 IU/l infected group)
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 8
-
ciADA activity on adenosine at pH values between 6.0 nd 8.0 remains constant and is lower at pH smaller than 6. The activity is not influenced by the presence of isoproylidene moiety in 2,3-O-isopropylidene adenosine within pH 5-8 range.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
activity is determined in cattle experimentally infected by Fasciola hepatica on days 20, 40, 60 and 80 post-infection. A reduction in activity on day 20 post-infection, as well as an increase in adenosine deaminase activity on days 40 and 60 post-infection is observed when compared to the control. Based on these results, it can be conclude that ATP, ADP and AMP hydrolysis and adenosine deamination are altered in platelets of cattle infected by Fasciola hepatica
from Friesian male cattle. Animals infected with Fasciola hepatica show lower enzyme activity on days 40 and 60 post infection compared with the uninfected control. The reduction on seric activity on days 40 and 60 post-inection can contribute to restrict the inflammatory response, and the subsequent cellular damage
from Friesian male cattle. Activity increases on day 100 post-infection (with Fasciola hepatica) contributed to the intense inflammatory process and oxidative damage due to the depletion of adenosine levels, an antiinflammatory molecule
-
reduced enzyme activity is associated with increased membrane fluidity in transformed versus normal fibroblasts
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
adenosine deaminase is important in regulating the concentration of adenine nucleotides, molecules known to be involved on platelet aggregation
metabolism
important enzyme in the purine metabolism. Oxidative stress occurs in cattle experimentally infected by Fasciola hepatica, mainly due to excessive production of reactive oxygen species in the course of fasciolosis, contributing to hepatic damage. Increase in hepatic adenosine deaminase activity may contribute to the inflammatory process
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). ADA_BOVIN
363
0
40919
Swiss-Prot
other Location (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
the enzyme exists as large and small isozymes, SADA and LADA, the latter is formed by the catalytic subunit monomer, the first by SADA complexed with the ADA complexing protein, i.e. the dipeptidyl peptidase IV
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of adenosine deaminase ligated with (+)-erythro-9-(2-hydroxy-3-nonyl)adenine (EHNA), vapor diffusion, sitting drop, 2 M ammonium sulfate, 2% 2-methyl-2, 4-pentanediol, 0.1 M MES buffer, pH 6.0, temperature 293K, , X-ray diffraction structure determination and analysis at 2.52 A resolution, space group P 43 21 2, EHNA induces conformational change of adenosine deaminase to the open form in the crystalline state, structural comparison between the EHNA-ADA complex and the 1-eaza-adenosine-ADA complex
molecular modeling enzyme-inhibitor, docking simulations enzyme-inhibitor, drug design
purified intestinal enzyme complexed with 1-[(R)-1-hydroxy-4-(6-(5-phenylvalerylamino)indol-1-yl)2-butyl]imidazole-4-carboxamide, 1-[(R)-1-hydroxy-4-(6-(3-phenylpropionylamino)indol-1-yl)2-butyl]imidazole-4-carboxamide, or 1-[(R)-4-(6-(3-benzylureido)indol-1-yl)-1-hydroxy-2-butyl]imidazole-4-carboxamide, protein solution is mixed with precipitant solution containing 100 mM MES, pH 6.0, 2.1 ammonium sulfate, and 2.5% v/v PEG 400, X-ray diffraction structure determination and analysis at 2.2 A resolution
commercial enzyme preparation at 20 mg/ml, native enzyme or complexed with inhibitor purine riboside, sitting drop vapour diffusion method, micro-stirring technique over 2 weeks, from 2.2 M ammonium sulfate, 2% 2-methyl-2,4-pentanediol, 0.1 M MES, pH 6.0, 20°C, with reservoir solution containing 20% 2-propanol, 20% PEG 4000, 0.1 M citrate, pH 5.6, X-ray diffraction structure determination and analysis at 1.8 A resolution
-
crystals of the complex of adenosine deaminase with 6-hydroxy-1,6-dihydropurine riboside are grown against reservoirs containing 2.0-2.2 M ammonium sulfate, 2% v/v polyethylene glycol 400 in 0.1 M HEPES buffer, pH 7.5, solved at 2.5 A resolution
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
effects of sodium dodecyl sulfate, dodecyltrimethylammonium bromide, sodium chloride, sodium sulfate, methanol and ethanol, on the structure and activity of adenosine deaminase are investigated by UV-Vis, circular dichroism spectrophotometry and molecular dynamics studies. Relative activity, experimental and computational helix content, total accessible surface area and exposed charged surface area are obtained. The relative activity of adenosine deaminase in the absence and the presence of denaturants is compared with structural results. It is shown that an increase in the surface area and a decrease in the amount of helicity are associated with a decrease in the activity of ADA
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
gel filtration, ion exchange chromatography, adenosine deaminase forms a complex with dipeptidyl peptidase II, during purification, it is noted that dipeptidyl peptidase II (DPPII; EC 3.4.14.2) fractions possesses adenosine deaminase activity at all steps
-
small isozyme from lung and spleen to homogeneity, purification of the soluble large isozyme complexed with dipeptidyl peptidase IV from kidney cortex by anion exchange chromatography, gel filtration, and affinity chromatography steps to about 90% purity
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
-
increased serum adenosine deaminase activity in tropical theileriosis may reflect the involvement of the cellular immune responses
medicine
-
ADA is an adjuvant for a dendritic cell-based vaccine against HIV. ADA potentiates human T-lymphocyte proliferation 4.5fold in co-cultures of HIV-inactivated-pulsed dendritic cells and autologous T cells of HIV-1-infected individuals. ADA enhances cytokine secretion in co-cultures of HIV-pulsed dendritic cells with T cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sim, M.K.; Maguire, M.H.
Studies on adenosine deaminase. 1. Purification and some properties of bovine placental adenosine deaminase
Eur. J. Biochem.
23
17-21
1971
Bos taurus
Rossi, C.A.; Lucacchini, A.
Purification and some properties of calf thymus adenosine deaminase
Biochem. Soc. Trans.
2
1313-1315
1974
Bos taurus
-
Agarwal, R.P.; Parks, R.E.
Adenosine deaminase from human erythrocytes
Methods Enzymol.
67
502-507
1978
Bos taurus, Homo sapiens
-
Lewis, A.S.; McCalla, C.; Murphy, L.
A simple conventional method for the purification of bovine spleen adenosine deaminase in high yield: Physical properties
J. Appl. Biochem.
3
378-386
1981
Bos taurus
-
Kinoshita, T.; Nishio, N.; Sato, A.; Murata, M.
Crystallization and preliminary analysis of bovine adenosine deaminase
Acta Crystallogr. Sect. D
55
2031-2032
1999
Bos taurus
Kinoshita, T.; Nishio, N.; Nakanishi, I.; Sato, A.; Fujii, T.
Structure of bovine adenosine deaminase complexed with 6-hydroxy-1,6-dihydropurine riboside
Acta Crystallogr. Sect. D
59
299-303
2003
Bos taurus
Mardanyan, S.S.; Sharoyan, S.G.; Antonyan, A.A.; Lupidi, G.; Cristalli, G.
Interaction of adenosine deaminase with inhibitors. Chemical modification by diethyl pyrocarbonate
Biochemistry (Moscow)
67
770-777
2002
Bos taurus
Ben-Shooshan, I.; Kessel, A.; Ben-Tal, N.; Cohen-Luria, R.; Parola, A.H.
On the regulatory role of dipeptidyl peptidase IV (:CD26:adenosine deaminase complexing protein) on adenosine deaminase activity
Biochim. Biophys. Acta
1587
21-30
2002
Bos taurus
Castro, C.; Britt, B.M.
Binding thermodynamics of the transition state analogue coformycin and of the ground state analogue 1-deazaadenosine to bovine adenosine deaminase
J. Enzyme Inhib.
16
217-232
2001
Bos taurus
Ataie, G.; Safarian, S.; Divsalar, A.; Saboury, A.A.; Moosavi-Movahedi, A.A.; Ranjbar, B.; Cristalli, G.; Mardanian, S.
Kinetic and structural analysis of the inhibition of adenosine deaminase by acetaminophen
J. Enzyme Inhib. Med. Chem.
19
71-78
2004
Bos taurus
Reayi, A.; Hosmane, R.S.
Inhibition of adenosine deaminase by novel 5:7 fused heterocycles containing the imidazo[4,5-e][1,2,4]triazepine ring system: a structure-activity relationship study
J. Med. Chem.
47
1044-1050
2004
Bos taurus
Sharoyan, S.; Antonyan, A.; Mardanyan, S.; Lupidi, G.; Cristalli, G.
Influence of dipeptidyl peptidase IV on enzymatic properties of adenosine deaminase
Acta Biochim. Pol.
53
539-546
2006
Bos taurus, Homo sapiens
Adachi, H.; Takano, K.; Niino, A.; Matsumura, H.; Kinoshita, T.; Warizaya, M.; Inoue, T.; Mori, Y.; Sasaki, T.
Solution stirring initiates nucleation and improves the quality of adenosine deaminase crystals
Acta Crystallogr. Sect. D
D61
759-762
2005
Bos taurus
Paul, M.K.; Grover, V.; Mukhopadhyay, A.K.
Merits of HPLC-based method over spectrophotometric method for assessing the kinetics and inhibition of mammalian adenosine deaminase
J. Chromatogr. B
822
146-153
2005
Bos taurus, Homo sapiens
Terasaka, T.; Kinoshita, T.; Kuno, M.; Seki, N.; Tanaka, K.; Nakanishi, I.
Structure-based design, synthesis, and structure-activity relationship studies of novel non-nucleoside adenosine deaminase inhibitors
J. Med. Chem.
47
3730-3743
2004
Bos taurus (P56658)
Da Settimo, F.; Primofiore, G.; La Motta, C.; Taliani, S.; Simorini, F.; Marini, A.M.; Mugnaini, L.; Lavecchia, A.; Novellino, E.; Tuscano, D.; Martini, C.
Novel, highly potent adenosine deaminase inhibitors containing the pyrazolo[3,4-d]pyrimidine ring system. Synthesis, structure-activity relationships, and molecular modeling studies
J. Med. Chem.
48
5162-5174
2005
Bos taurus
Tyler, P.C.; Taylor, E.A.; Froehlich, R.F.; Schramm, V.L.
Synthesis of 5-methylthio coformycins: specific inhibitors for malarial adenosine deaminase
J. Am. Chem. Soc.
129
6872-6879
2007
Bos taurus, Homo sapiens, Plasmodium falciparum
Ajloo, D.; Saboury, A.A.; Haghi-Asli, N.; Ataei-Jafarai, G.; Moosavi-Movahedi, A.A.; Ahmadi, M.; Mahnam, K.; Namaki, S.
Kinetic, thermodynamic and statistical studies on the inhibition of adenosine deaminase by aspirin and diclofenac
J. Enzyme Inhib. Med. Chem.
22
395-406
2007
Bos taurus
Alunni, S.; Orru, M.; Ottavi, L.
A study on the inhibition of adenosine deaminase
J. Enzyme Inhib. Med. Chem.
23
182-189
2008
Bos taurus
Ujjinamatada, R.K.; Phatak, P.; Burger, A.M.; Hosmane, R.S.
Inhibition of adenosine deaminase by analogues of adenosine and inosine, incorporating a common heterocyclic base, 4(7)-amino-6(5)H-imidazo[4,5-d]pyridazin-7(4)one
J. Med. Chem.
51
694-698
2008
Bos taurus
Kinoshita, T.; Tada, T.; Nakanishi, I.
Conformational change of adenosine deaminase during ligand-exchange in a crystal
Biochem. Biophys. Res. Commun.
373
53-57
2008
Bos taurus (P56658)
Sharoyan, S.G.; Antonyan, A.A.; Mardanyan, S.S.; Lupidi, G.; Cuccioloni, M.; Angeletti, M.; Cristalli, G.
Complex of dipeptidyl peptidase II with adenosine deaminase
Biochemistry (Moscow)
73
943-949
2008
Bos taurus
Vistoli, G.; Pedretti, A.; Alessandrini, L.; Casati, S.; Ciuffreda, P.; Meroni, G.; Santaniello, E.
Enhanced activity or resistance of adenosine derivatives towards adenosine deaminase-catalyzed deamination: Influence of ribose modifications
Bioorg. Med. Chem. Lett.
19
2877-2879
2009
Bos taurus (P56658)
Ajloo, D.; Taghizadeh, E.; Saboury, A.A.; Bazyari, E.; Mahnam, K.
Effects of surfactant, salt and solvent on the structure and activity of adenosine deaminase: molecular dynamic and spectrophotometric studies
Int. J. Biol. Macromol.
43
151-158
2008
Bos taurus (P56658)
La Motta, C.; Sartini, S.; Mugnaini, L.; Salerno, S.; Simorini, F.; Taliani, S.; Marini, A.M.; Da Settimo, F.; Lavecchia, A.; Novellino, E.; Antonioli, L.; Fornai, M.; Blandizzi, C.; Del Tacca, M.
Exploiting the pyrazolo[3,4-d]pyrimidin-4-one ring system as a useful template to obtain potent adenosine deaminase inhibitors
J. Med. Chem.
52
1681-1692
2009
Bos taurus (P56658), Bos taurus
Alessandrini, L.; Ciuffreda, P.; Pavlovic, R.; Santaniello, E.
Activity of adenosine deaminase and adenylate deaminase on adenosine and 2, 3-isopropylidene adenosine: role of the protecting group at different pH values
Nucleosides Nucleotides Nucleic Acids
27
31-36
2008
Bos taurus
Altug, N.; Yueksek, N.; Agaoglu, Z.T.; Keles, I.
Determination of adenosine deaminase activity in cattle naturally infected with Theileria annulata
Trop. Anim. Health Prod.
40
449-456
2008
Bos taurus
Climent, N.; Martinez-Navio, J.M.; Gil, C.; Garcia, F.; Rovira, C.; Hurtado, C.; Miralles, L.; Gatell, J.M.; Gallart, T.; Mallol, J.; Lluis, C.; Franco, R.
Adenosine deaminase enhances T-cell response elicited by dendritic cells loaded with inactivated HIV
Immunol. Cell Biol.
87
634-639
2009
Bos taurus
Lougiakis, N.; Marakos, P.; Pouli, N.; Fragopoulou, E.; Tenta, R.
Synthesis of new nebularine analogues and their inhibitory activity against adenosine deaminase
Chem. Pharm. Bull.
63
134-142
2015
Bos taurus (P56658)
Zimmermann, S.C.; Sadler, J.M.; ODaniel, P.I.; Kim, N.T.; Seley-Radtke, K.L.
Reverse carbocyclic fleximers: synthesis of a new class of adenosine deaminase inhibitors
Nucleosides Nucleotides Nucleic Acids
32
137-154
2013
Bos taurus (P56658)
Kandalkar, S.R.; Ramaiah, P.A.; Joshi, M.; Wavhal, A.; Waman, Y.; Raje, A.A.; Tambe, A.; Ansari, S.; De, S.; Palle, V.P.; Mookhtiar, K.A.; Deshpande, A.M.; Barawkar, D.A.
Modifications of flexible nonyl chain and nucleobase head group of (+)-erythro-9-(2s-hydroxy-3s-nonyl)adenine [(+)-EHNA] as adenosine deaminase inhibitors
Bioorg. Med. Chem.
25
5799-5819
2017
Bos taurus (P56658)
Arun, K. G.; Sharanya, C.S.; Abhithaj, J.; Sadasivan, C.
Biochemical and computational insights of adenosine deaminase inhibition by Epigallocatechin gallate
Comput. Biol. Chem.
83
107111
2019
Bos taurus (P56658)
Fracasso, M.; Da Silva, A.S.; Baldissera, M.D.; Bottari, N.B.; Gabriel, M.E.; Piva, M.M.; Stedille, F.A.; Christ, R.; Rhoden, L.A.; Henker, L.C.; Moresch, V.M.; Schetinger, M.R.; Mendes, R.E.
Activities of ectonucleotidases and adenosine deaminase in platelets of cattle experimentally infected by Fasciola hepatica
Exp. Parasitol.
176
16-20
2017
Bos taurus (P56658), Bos taurus
Da Silva, A.S.; Baldissera, M.D.; Bottari, N.B.; Gabriel, M.E.; Rhoden, L.A.; Piva, M.M.; Christ, R.; Stedille, F.A.; Gris, A.; Morsch, V.M.; Schetinger, M.R.; Mendes, R.E.
Oxidative stress and changes in adenosine deaminase activity of cattle experimentally infected by Fasciola hepatica
Parasitology
144
520-526
2017
Bos taurus (P56658), Bos taurus
EXTERNAL LINKS (specific for EC-Number 3.5.4.4)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
