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Information on EC 3.5.4.4 - adenosine deaminase and Organism(s) Homo sapiens and UniProt Accession Q9NZK5

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IUBMB Comments
The enzyme, found in a wide variety of microorganisms, plants, invertebrates, and animals, plays a role in purine metabolism.
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This record set is specific for:
Homo sapiens
UNIPROT: Q9NZK5
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
Synonyms
adenosine deaminase, adenosine deaminase 2, adenosine aminohydrolase, adenosine deaminase 1, adaii, pvada, mj1541, ciada, sco4901, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ADA2
isozyme
adenosine deaminase 2
isozyme
ADA2
-
-
Adenosine aminohydrolase
adenosine deaminase
adenosine deaminase 1
adenosine deaminase 2
-
-
LADA
-
-
SADA
-
-
TadA
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
adenosine + H2O = inosine + NH3
show the reaction diagram
reaction mechanism, structure-function relationship of ADA and dipeptidyl peptidase IV
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Deamination
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -
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 hide
9026-93-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
adenosine + H2O
inosine + NH3
show the reaction diagram
2'-deoxyadenosine + H2O
2'-deoxyinosine + NH3
show the reaction diagram
6-chloropurine riboside + H2O
inosine + Cl-
show the reaction diagram
-
-
-
-
?
6-chloropurinriboside + H2O
inosine + Cl-
show the reaction diagram
-
-
-
-
?
6-methoxypurinriboside
?
show the reaction diagram
-
-
-
-
?
adenosine + H2O
inosine + NH3
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
adenosine + H2O
inosine + NH3
show the reaction diagram
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
-
-
?
2'-deoxyadenosine + H2O
2'-deoxyinosine + NH3
show the reaction diagram
adenosine + H2O
inosine + NH3
show the reaction diagram
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
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
coformycin
complete inhibition of ADA2 at 1 mM
erythro-9-(2-hydroxy-3-nonyl)adenine
i.e. EHNA
(+)-erythro-9-(2-hydroxy-3-nonyl)adenine
specific inhibitor of ADA1
1,6-Dihydro-6-(hydroxymethyl)purine riboside
-
-
1-deaza-erythro-9-(2-hydroxy-3-nonyl)adenine
-
i.e. 1-dEHNA
1-deazaadenosine
-
-
2'-deoxycoformycin
2'-deoxyformycin
-
50% inhibition of isozyme ADA2 at 0.09 mM
2,6-diaminopurine
-
-
2,6-diaminopurine sulfate
-
-
2-Aminopurine
-
-
3-deaza-erythro-9-(2-hydroxy-3-nonyl)adenine
-
i.e. 3-dEHNA
3-deazaadenosine
-
-
4-amino-5-imidazole carboxamide-HCl
-
-
4-amino-5-imidazole carboxyamide ribonucleoside
-
-
6-Chloropurine
-
-
6-methylamino riboside
-
-
6-Methylmercaptopurine riboside
-
-
adenosine analogs
-
-
-
aza adenosine analogues
-
-
-
coformycin
cordycepin
-
-
deaza adenosine analogues
-
-
-
Deoxycoformycin
-
-
erythro-9-(2-hydroxy-3-nonyl)-adenine hydrochloride
-
0.45 nM, 50% inhibition
erythro-9-(2-hydroxy-3-nonyl)adenine
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
guanosine
-
-
Inosine
-
-
Iodopurine
-
-
N6-methyladenosine
-
-
p-chloromercuryphenylsulfonate
-
-
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
-
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.034 - 0.07
2'-deoxyadenosine
0.277
6-chloropurinriboside
-
-
0.081
6-methoxypurinriboside
-
-
0.000046 - 2.15
adenosine
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5.35 - 180
adenosine
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
90 - 3880
adenosine
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00045 - 0.0006
1-deaza-erythro-9-(2-hydroxy-3-nonyl)adenine
0.0025 - 0.0029
1-deazaadenosine
0.000025 - 0.000036
3-deaza-erythro-9-(2-hydroxy-3-nonyl)adenine
0.52 - 1
3-deazaadenosine
0.00003 - 0.00006
erythro-9-(2-hydroxy-3-nonyl)adenine
0.018
N6-methyladenosine
-
25°C, 50 mM Tris-HCl buffer, pH 7.4, enzyme concentration 1.5 nM
0.008
purine riboside
-
25°C, 50 mM Tris-HCl buffer, pH 7.4, enzyme concentration 1.5 nM
additional information
additional information
-
inhibition kinetics of the large isozyme
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000027
FR234938
Homo sapiens
-
pH 7.4, 22°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
166
purified isozyme ADA2
0.00000373
-
-
0.004
-
thyroid
0.006
-
kidney
0.007
-
lung
0.008
-
skeletal muscle
0.009
-
liver, cerebellum, spinal cord
0.011
-
cardiac muscle
0.013
-
testis
0.02
-
appendix
0.021
-
adrenal gland
0.023
-
lymph node
0.027
-
pancreas, cerebrum
0.063
-
jejunum
0.072
-
normal B cells
0.089
-
stomach
0.127
-
duodenum
0.128
-
spleen
0.45
-
purified large isozyme from blood serum
0.475
-
T cell line CCRF-HSB-2
0.501
-
T cell line CCRF-CEM
0.65
-
purified large isozyme from pleural fluid
0.78
-
-
0.965
-
T cell line RPMI-8402
1.064
-
T cell line MOLT-4
1.2
-
purified isozyme ADA2
1200
-
erythrocytes
17.4
-
Es
2.2
-
protamine sulfate supernatant
2.7
-
El
260
-
purine riboside Sepharose chromatography
28.49
-
-
5.3
-
type 1
52
-
Q Sepharose chromatography
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 8
-
-
5.5
-
type intermediate
6 - 8
-
-
6.5 - 7.8
-
large isozyme from blood serum
7 - 7.4
-
type small and large
7.5 - 8
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.6 - 8.2
isozyme ADA2
6.5 - 8
-
pH 6.5: about 85% of maximal activity, pH 8.0: about 70% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
assay at
22
-
assay at room temperature
30
-
assay at
37
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
ADA2 is secreted by promonocytic cell lines and blood monocytes differentiated into macrophages and dendritic cells
Manually annotated by BRENDA team
-
isozyme ADA1
Manually annotated by BRENDA team
-
LADA
Manually annotated by BRENDA team
-
isozyme ADA2
Manually annotated by BRENDA team
-
T-cell lymphoma cell line
Manually annotated by BRENDA team
-
peripheral blood
Manually annotated by BRENDA team
-
of peripheral blood
Manually annotated by BRENDA team
-
LADA
Manually annotated by BRENDA team
-
differentiating
Manually annotated by BRENDA team
additional information
-
distribution of isozymes
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
large isozyme LADA
Manually annotated by BRENDA team
-
small subunit SADA
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
isozyme ADA2 but not ADA1 induces T cell-dependent differentiation of monocytes into macrophages and stimulates macrophage proliferation. ADA2 exhibits a growth factor activity and increases proliferation of CD4+ T cells. ADA2 binds to cells via proteoglycans and adenosine receptors
malfunction
-
apoptosis is enhanced in ADAR1-deficient cells following infection with wild type and V knockout measles virus but not following infection with C knockout measles virus or treatment with tumor necrosis factor-alpha or staurosporine
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ADA2_HUMAN
511
1
58934
Swiss-Prot
Secretory Pathway (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
110000
-
isozyme ADA2, gel filtration
114000
-
gel filtration, type intermediate
230000
-
El, gel filtration
298000
30000 - 35000
-
gel filtration
36000
-
gel filtration, type small
36000 - 44000
-
gel filtration, type a
41000
-
SDS-PAGE, calculated value 40754
42000
-
a second band of 300000 Da is detected for the complex of adenosine deaminase 1 with dipeptidyl peptidase IV, non-denaturing PAGE
44000
-
SDS-PAGE and nondenaturing PAGE
47000
-
Es, gel filtration
67000
-
2 * 67000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
monomer
polymer
-
-
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
M155D
mutation reduces kcat
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
conversion of smaller enzyme to intermediate and larger enzyme possible
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 30 days, the enzyme remains stable
-
-20°C, PBS, 50% glycerol
-
-20°C, purified large subunit, 2 months without loss of activity
-
0°C, phosphate buffer, pH 7.0, 2-mercaptoethanol, 1 month, enzyme EI
-
25°C, 1 day, the enzyme remains stable
-
4-8°C, 7 days, the enzyme remains stable
-
4°C, potassium phosphate buffer, pH 7.4, several weeks
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
isozyme ADA2, 138.3fold by immunoglobulin and heparin affinity chromatography in two alternated sequences, and gel filtration
recombinant isozyme ADA2 is purified by heparin affinity column chromatography, Ni-chelate column chromatography, and gel filtration
homogeneity, protamine sulfate treatment, Q Sepharose chromatography, purine riboside-Sepharose chromatography
-
isozyme ADA2 400fold from plasma by ammonium sulfate fractionation, anion exchange chromatography, adsorption chromatography, and gel filtration
-
purification of the soluble large isozyme complexed with dipeptidyl peptidase IV from blood serum and pleural fluid by anion exchange chromatography, gel filtration, and affinity chromatography steps to about 90% purity
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
isozyme ADA2 is expressed in S2 Drosophila cells
enzyme expression in an enzyme-deficient Escherichia coli strain Sphi3834
-
expression in Escherichia coli S Phi 3834
-
the activity of human adenosine deaminase (hADA) expressed in transgenic seeds of three different plant species: pea (Pisum sativum L.), Nicotiana benthamiana L. and tarwi (Lupinus mutabilis Sweet) is compared. All three species are transformed with the same expression vector containing the hADA gene driven by the seed-specific promoter LegA2 with an apoplast targeting pinII signal peptide. During the study, several independent transgenic lines are generated and screened from each plant species and only lines with a single copy of the gene of interest are used for hADA expression analysis. A stable transgenic canola line expressing the ADA protein, under the control of 35S constitutive promoter is used as both as a positive control and for comparative study with the seed specific promoter. The highest activity of the hADA enzyme (U/g seed) is reported in tarwi (4.26 U/g) followed by pea (3.23 U/g) and Nicotiana benthamiana (1.69 U/g)
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
interferon gamma inhibits secretion of ADA2 by macrophages
enzyme activity is lowered in gastric tissues treated with the static magnetic field
-
no change of activity is observed in the enzyme activity of colon tissues treated with the static magnetic field
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
ADA2 is a drug candidate to modulate the immune responses during inflammation and cancer. ADA2 and its inhibitors are drug candidates to activate the immune systems of immunocompromised patients and to treat various types of blood cancers
analysis
-
a capillary electrophoresis method for simultaneous analysis of adenosine deaminase in red blood cells is developed. The method is also successfully applied in the inhibitor screening from traditional Chinese medicines
diagnostics
drug development
-
enzyme inhibitor FR234938 might be effective as an anti-rheumatic and anti-inflammatory drug by modulating the host-defense concentrations of adenosine
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Akedo, H.; Nishihara, H.; Shinkai, K.; Komatsu, K.; Ishikawa, S.
Multiple forms of human adenosine deaminase. 1. Purification and characterization of two molecular species
Biochim. Biophys. Acta
276
257-271
1972
Homo sapiens
Manually annotated by BRENDA team
Osborne, W.R.A.; Spencer, N.
Partial purification and properties of the common inherited forms of adenosine deaminase from human erythrocytes
Biochem. J.
133
117-123
1973
Homo sapiens
Manually annotated by BRENDA team
Van der Weyden, M.B.; Kelley, W.N.
Human adenosine deaminase, Distributions and properties
J. Biol. Chem.
251
5448-5456
1976
Homo sapiens
Manually annotated by BRENDA team
Crabbe, M.J.; Kavanagh, J.P.
The purification and preliminary investigation of fumarase, peroxidase, diamine oxidase and adenosine deaminase from human seminal plasma
Biochem. Soc. Trans.
5
735-737
1977
Homo sapiens
Manually annotated by BRENDA team
Agarwal, R.P.; Parks, R.E.
Adenosine deaminase from human erythrocytes
Methods Enzymol.
67
502-507
1978
Bos taurus, Homo sapiens
-
Manually annotated by BRENDA team
Philips, A.V.; Robbins, D.J.; Coleman, M.S.
Immunoaffinity purification and fluorescence studies of human adenosine deaminase
Biochemistry
26
2893-2903
1987
Homo sapiens
Manually annotated by BRENDA team
Daddona, P.E.; Wiesmann, W.P.; Lambros, C.; Kelley, W.N.; Webster, H.K.
Human malaria parasite adenosine deaminase
J. Biol. Chem.
259
1472-1475
1984
Homo sapiens, Plasmodium falciparum
Manually annotated by BRENDA team
Daddona, P.E.
Human adenosine deaminase: Properties and turnover in cultured T and B lymphoblasts
J. Biol. Chem.
256
12496-12501
1981
Homo sapiens
Manually annotated by BRENDA team
Wiginton, D.A.; Coleman, M.S.; Hutton, J.J.
Purification, characterization and radioimmunoassay of adenosine deaminase from human leukaemic granulocytes
Biochem. J.
195
389-397
1981
Homo sapiens
Manually annotated by BRENDA team
Centelles, J.J.; Franco, R.
Slight differences between adenosine deaminase from different species. An immunochemical study
Arch. Int. Physiol. Biochim.
98
421-431
1990
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Lupidi, G.; Marmocchi, F.; Cristalli, G.
Inhibition studies on membrane adenosine deaminase from human placenta
Biochem. Mol. Biol. Int.
46
1071-1080
1998
Homo sapiens
Manually annotated by BRENDA team
Iwaki-Egawa, S.; Watanabe, Y.
Characterization and purification of adenosine deaminase 1 from human and chicken liver
Comp. Biochem. Physiol. B
133
173-182
2002
Gallus gallus, Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Zavialov, A.V.; Engstroem, A.
Human ADA2 belongs to a new family of growth factors with adenosine deaminase activity
Biochem. J.
391
51-57
2005
Homo sapiens (Q9NZK5), Homo sapiens
Manually annotated by BRENDA team
Iwaki-Egawa, S.; Yamamoto, T.; Watanabe, Y.
Human plasma adenosine deaminase 2 is secreted by activated monocytes
Biol. Chem.
387
319-321
2006
Homo sapiens
Manually annotated by BRENDA team
Kashyap, R.S.; Kainthla, R.P.; Mudaliar, A.V.; Purohit, H.J.; Taori, G.M.; Daginawala, H.F.
Cerebrospinal fluid adenosine deaminase activity: a complimentary tool in the early diagnosis of tuberculous meningitis
Cerebrospinal Fluid Res.
3
5
2006
Homo sapiens
Manually annotated by BRENDA team
Aghaei, M.; Karami-Tehrani, F.; Salami, S.; Atri, M.
Adenosine deaminase activity in the serum and malignant tumors of breast cancer: the assessment of isoenzyme ADA1 and ADA2 activities
Clin. Biochem.
38
887-891
2005
Homo sapiens
Manually annotated by BRENDA team
Hitoglou, S.; Zournatzi, V.; Gougoustamou, D.; Hatzistilianou, M.; Tzafettas, J.
Adenosine deaminase activity and its isoenzyme pattern in women with recurrent spontaneous abortions
Gynecol. Obstet. Invest.
58
126-129
2004
Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Vivekanandhan, S.; Soundararajan, C.C.; Tripathi, M.; Maheshwari, M.C.
Adenosine deaminase and 5'-nucleotidase activities in peripheral blood T cells of multiple sclerosis patients
Neurochem. Res.
30
453-456
2005
Homo sapiens
Manually annotated by BRENDA team
Okur, E.; Inanc, F.; Yildirim, I.; Kilinc, M.; Kilic, M.A.
Malondialdehyde level and adenosine deaminase activity in nasal polyps
Otolaryngol. Head Neck Surg.
134
37-40
2006
Homo sapiens
Manually annotated by BRENDA team
Kuno, M.; Seki, N.; Tsujimoto, S.; Nakanishi, I.; Kinoshita, T.; Nakamura, K.; Terasaka, T.; Nishio, N.; Sato, A.; Fujii, T.
Anti-inflammatory activity of non-nucleoside adenosine deaminase inhibitor FR234938
Eur. J. Pharmacol.
534
241-249
2006
Homo sapiens
Manually annotated by BRENDA team
Sadat Hayatshahi, S.H.; Abdolmaleki, P.; Ghiasi, M.; Safarian, S.
QSARs and activity predicting models for competitive inhibitors of adenosine deaminase
FEBS Lett.
581
506-514
2007
Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Poursharifi, P.; Saghiri, R.; Ebrahimi-Rad, M.; Nazem, H.; Pourpak, Z.; Moin, M.; Shams, S.
Adenosine deaminase in patients with primary immunodeficiency syndromes: The analysis of serum ADA1 and ADA2 activities
Clin. Biochem.
42
1438-1443
2008
Homo sapiens
Manually annotated by BRENDA team
Kisacik, B.; Akdogan, A.; Yilmaz, G.; Karadag, O.; Yilmaz, F.M.; Koklu, S.; Yuksel, O.; Ertenli, A.I.; Kiraz, S.
Serum adenosine deaminase activities during acute attacks and attack-free periods of familial Mediterranean fever
Eur. J. Intern. Med.
20
44-47
2009
Homo sapiens
Manually annotated by BRENDA team
Gracia, E.; Cortes, A.; Meana, J.J.; Garcia-Sevilla, J.; Herhsfield, M.S.; Canela, E.I.; Mallol, J.; Lluis, C.; Franco, R.; Casado, V.
Human adenosine deaminase as an allosteric modulator of human A(1) adenosine receptor: abolishment of negative cooperativity for [H](R)-pia binding to the caudate nucleus
J. Neurochem.
107
161-170
2008
Homo sapiens
Manually annotated by BRENDA team
Zaric, B.; Kuruc, V.; Milovancev, A.; Markovic, M.; Sarcev, T.; Canak, V.; Pavlovic, S.
Differential diagnosis of tuberculous and malignant pleural effusions: what is the role of adenosine deaminase?
Lung
186
233-240
2008
Homo sapiens
Manually annotated by BRENDA team
Tofovic, S.P.; Jackson, E.K.; Rafikova, O.
Adenosine deaminase-adenosine pathway in hemolysis-associated pulmonary hypertension
Med. Hypotheses
72
713-719
2009
Homo sapiens
Manually annotated by BRENDA team
Baba, K.; Hoosen, A.A.; Langeland, N.; Dyrhol-Riise, A.M.
Adenosine deaminase activity is a sensitive marker for the diagnosis of tuberculous pleuritis in patients with very low CD4 counts
PLoS ONE
3
e2788
2008
Homo sapiens
Manually annotated by BRENDA team
Kim, S.H.; Kim, Y.K.; Park, H.W.; Kim, S.H.; Kim, S.H.; Ye, Y.M.; Min, K.U.; Park, H.S.
Adenosine deaminase and adenosine receptor polymorphisms in aspirin-intolerant asthma
Respir. Med.
103
356-363
2009
Homo sapiens (P00813), Homo sapiens
Manually annotated by BRENDA team
Dikensoy, O.; Fakili, F.; Elbek, O.; Uysal, N.
High adenosine deaminase activity in the pleural effusion of a patient with Legionnaires disease
Respirology
13
473-474
2008
Homo sapiens
Manually annotated by BRENDA team
Zavialov, A.V.; Gracia, E.; Glaichenhaus, N.; Franco, R.; Zavialov, A.V.; Lauvau, G.
Human adenosine deaminase 2 induces differentiation of monocytes into macrophages and stimulates proliferation of T helper cells and macrophages
J. Leukoc. Biol.
88
279-290
2010
Homo sapiens (P00813), Homo sapiens (Q9NZK5), Homo sapiens
Manually annotated by BRENDA team
Aghaei, M.; Karami-Tehrani, F.; Salami, S.; Atri, M.
Diagnostic value of adenosine deaminase activity in benign and malignant breast tumors
Arch. Med. Res.
41
14-18
2010
Homo sapiens
Manually annotated by BRENDA team
Durak, Z.E.; Kocao?lu, E.H.; Oztuerk, B.
Static magnetic field inhibits adenosine deaminase activity in cancerous and noncancerous human gastric tissues
Cancer Biother. Radiopharm.
29
162-165
2014
Homo sapiens
Manually annotated by BRENDA team
Lu, J.; Grenache, D.G.
Development of a rapid, microplate-based kinetic assay for measuring adenosine deaminase activity in body fluids
Clin. Chim. Acta
413
1637-1640
2012
Homo sapiens
Manually annotated by BRENDA team
Qi, Y.; Li, Y.; Bao, J.J.
Development of a capillary electrophoresis method for analyzing adenosine deaminase and purine nucleoside phosphorylase and its application in inhibitor screening
Anal. Biochem.
506
31-44
2016
Homo sapiens, Mus musculus (P03958)
Manually annotated by BRENDA team
Jaruwat, A.; Riangrungroj, P.; Ubonprasert, S.; Sae-Ueng, U.; Kuaprasert, B.; Yuthavong, Y.; Leartsakulpanich, U.; Chitnumsub, P.
Crystal structure of Plasmodium falciparum adenosine deaminase reveals a novel binding pocket for inosine
Arch. Biochem. Biophys.
667
6-13
2019
Homo sapiens (P00813), Homo sapiens, Plasmodium falciparum (Q8IJA9), Plasmodium falciparum
Manually annotated by BRENDA team
Parra-Ruiz, J.; Ramos, V.; Duenas, C.; Coronado-Alvarez, N.M.; Cabo-Magadan, R.; Portillo-Tunon, V.; Vinuesa, D.; Munoz-Medina, L.; Hernandez-Quero, J.
Rational application of adenosine deaminase activity in cerebrospinal fluid for the diagnosis of tuberculous meningitis
Infection
43
531-535
2015
Homo sapiens
Manually annotated by BRENDA team
Ruggiero, V.; Cacace, E.; Era, B.; Fais, A.
Soluble adenosine deaminase activity in fibromyalgia syndrome
J. Musculoskelet. Pain
23
79-80
2015
Homo sapiens
-
Manually annotated by BRENDA team
Pirincci, N.; Kaya, T.Y.; Kaba, M.; Ozan, T.; Gecit, I.; Oezveren, H.; Eren, H.; Ceylan, K.
Serum adenosine deaminase, catalase, and carbonic anhydrase activities in patients with renal cell carcinoma
Redox Rep.
22
252-256
2017
Homo sapiens
Manually annotated by BRENDA team
Doshi, K.M.; Loukanina, N.N.; Polowick, P.L.; Holbrook, L.A.
Seed specific expression and analysis of recombinant human adenosine deaminase (hADA) in three host plant species
Transgenic Res.
25
629-637
2016
Homo sapiens (P00813), Homo sapiens
Manually annotated by BRENDA team