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Information on EC 3.5.4.4 - adenosine deaminase and Organism(s) Mus musculus and UniProt Accession P03958
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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.
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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: Mus musculus
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
Adenosine aminohydrolase
-
-
-
-
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
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
-
-
?
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
-
the enzyme is important in thymocyte development, especially in late stages, overview
-
-
?
adenosine + H2O
inosine + NH3
the enzyme is crucial for purine metabolism and normal immune competence
-
-
ir
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
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+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
6-fluoro-D,L-tryptophan
adenosine analogue, induces conformational changes inhibiting the enzyme, structural mechanism, overview
adenosine analogues
induce conformational changes inhibiting the enzyme, structural mechanism, overview
-
purine riboside
adenosine analogue, induces conformational changes inhibiting the enzyme, structural mechanism, overview
progesterone
-
progesterone decreases adenosine deaminase levels, adenosine deaminase levels show regional specificity with differences among the cerebral hemispheres, cerebellum, and brainstems structures
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
thermodynamics and kinetics
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
apparent activity difference between healthy and hepatoma mice
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_MOUSE
352
0
39992
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 has (beta/alpha)8-barrel structure with bound zinc
additional information
-
the enzyme has (beta/alpha)8-barrel structure with bound zinc
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
holo- and apo-ADA, hanging drop vapor diffusion method, using 20% (w/v) PEG 3350 and 200 mM ammonium sulfate, pH 4.7 for apo-ADA or 25% (w/v) PEG 6000, 20 mM Tris-HCl and pH 8.5 for holo-ADA
the binding free energies of a series of adenosine deaminase inhibitors are calculated, and the structure-activity relationship is investigated, the inhibitor recognition mechanism of adenosine deaminase and the effect of methyl substitution in inhibitors are discussed on the basis of the analysis of MD trajectories
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
ADA-deficiency in mice inhibits the further differentiation of double positive CD4+CD8+ thymocytes in fetal thymic organ culture, the later stages of thymocyte development are sensitive to a lack of ADA, the block is mediated by a mitochondria-dependent mechanism. ADA-deficient cultures are partially rescued by the pan-caspase inhibitor carbobenzoxy-Val-Ala-Asp-fluoromethyl ketone or by the use of Apaf-1-deficient mice lacking apoptotic protease-activating factor-1, overview
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
adenosine deaminase inhibitors have potential as anti-inflammatory drugs or immunosuppressants
drug development
-
progesterone treatment may prevent epileptic activity by decreasing adenosine deaminase levels
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Schrader, W.P.; West, C.A.; Miczek, A.D.; Norton, E.K.
Characterization of the adenosine deaminase-adenosine deaminase complexing protein binding reaction
J. Biol. Chem.
265
19312-19318
1990
Cavia porcellus, Oryctolagus cuniculus, Homo sapiens, Platyrrhini, Mus musculus
Singh, L.S.; Sharma, R.
Purification and characterization of intestinal adenosine deaminase from mice
Mol. Cell. Biochem.
204
127-134
2000
Mus musculus
Shu, Q.; Frieden, C.
Relation of enzyme activity to local/global stability of murine adenosine deaminase: 19F NMR studies
J. Mol. Biol.
345
599-610
2005
Mus musculus (P03958), Mus musculus
Van De Wiele, C.J.; Joachims, M.L.; Fesler, A.M.; Vaughn, J.G.; Blackburn, M.R.; McGee, S.T.; Thompson, L.F.
Further differentiation of murine double-positive thymocytes is inhibited in adenosine deaminase-deficient murine fetal thymic organ culture
J. Immunol.
176
5925-5933
2006
Mus musculus, Mus musculus C57BL/6
Pence, S.; Erkutlu, I.; Kurtul, N.; Alptekin, M.; Tan, U.
Effects of progesterone on total brain tissue adenosine deaminase activity in experimental epilepsy
Int. J. Neurosci.
119
204-213
2009
Mus musculus
Sibani, S.; Rampakakis, E.; Di Paola, D.; Zannis-Hadjopoulos, M.
Fine mapping and functional activity of the adenosine deaminase origin in murine embryonic fibroblasts
J. Cell. Biochem.
104
773-784
2008
Mus musculus
Kosugi, T.; Nakanishi, I.; Kitaura, K.
Binding free energy calculations of adenosine deaminase inhibitor and the effect of methyl substitution in inhibitors
J. Chem. Inf. Model.
49
615-622
2009
Mus musculus (P03958)
Wu, X.H.; Zou, G.L.; Quan, J.M.; Wu, Y.D.
A theoretical study on the catalytic mechanism of Mus musculus adenosine deaminase
J. Comput. Chem.
31
2238-2247
2010
Mus musculus (P03958), Mus musculus
Niu, W.; Shu, Q.; Chen, Z.; Mathews, S.; Di Cera, E.; Frieden, C.
The role of Zn2+ on the structure and stability of murine adenosine deaminase
J. Phys. Chem. B
114
16156-16165
2010
Mus musculus (P03958), Mus musculus
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