52544
Adenosine deaminase Streptococcus thermophilus, recombinant
recombinant, expressed in E. coli, ≥100 units/mL
Synonym(s):
ADA
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About This Item
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recombinant
expressed in E. coli
form
liquid
specific activity
≥100 units/mL
mol wt
38 kDa
storage temp.
−20°C
General description
Adenosine deaminase is a single polypeptide chain having eight parallel strands of α⁄β barrels. The molecular weight is found to be approximately 38,000 Da. The deep pocket at the COOH-terminal of the β barrel, which contains zinc as the co-factor, serves as the active site. It is ubiquitously found in wide variety of microorganisms, plants, and invertebrates.
Application
Adenosine deaminase was used to study its inhibitory effect on cerebrocortical vasodilatation (brain activation) and hypoxia. It was also used for the comparison of the inhibition by two adenosine analogs, N6-phenylisopropyladenosine and 5′-N-ethylcarboxamideadenosine of glycerol production by adipocytes
Biochem/physiol Actions
Adenosine deaminase is an active enzyme in purine metabolism, which mainly catalyzes the irreversible hydrolytic deamination of adenosine and deoxyadenosine to inosine and deoxyinosine, respectively. It is adequately present in mammalian tissue, and its deficiency leads to combined immunodeficiency disease. It is also present in all mammalian cells that play a key role in differentiation and maturation of lymphoid system.
Unit Definition
One unit will deaminate 1.0 μmole of adenosine to inosine per min at pH 7.5 at 25°C.
Storage Class Code
12 - Non Combustible Liquids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
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C Londos et al.
Proceedings of the National Academy of Sciences of the United States of America, 77(5), 2551-2554 (1980-05-01)
Cell surface adenosine receptors mediate either stimulation or inhibition of adenylate cyclase activity [ATP pyrophosphate-lyase (cyclizing), EC 4.6.1.1], and the receptors that mediate these different responses can be discriminated with selected adenosine analogs. 5'-N-Ethylcarboxamide-adenosine is a more potent agonist at
E Dóra et al.
Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism, 4(3), 447-457 (1984-09-01)
The purpose of this study was to investigate the possible importance of adenosine in cerebrocortical vasodilatation accompanying brain activation (epileptic seizures and direct electrical stimulation) and hypoxia (arterial hypoxia and cyanide poisoning of the brain cortex). In chloralose-anesthetized cats a
G Cristalli et al.
Medicinal research reviews, 21(2), 105-128 (2001-02-27)
Adenosine deaminase (ADA) is an enzyme of the purine metabolism which catalyzes the irreversible deamination of adenosine and deoxyadenosine to inosine and deoxyinosine, respectively. This ubiquitous enzyme has been found in a wide variety of microorganisms, plants, and invertebrates. In
P E Daddona et al.
The Journal of biological chemistry, 252(1), 110-115 (1977-01-10)
Human erythrocyte adenosine deaminase has been purified approximately 800,000-fold to apparent homogeneity using antibody affinity chromatography. The enzyme was shown to be a single polypeptide chain with an estimated molecular weight of approximately 38,000. The three electrophoretic forms of erythrocyte
D K Wilson et al.
Science (New York, N.Y.), 252(5010), 1278-1284 (1991-05-31)
The crystal structure of a murine adenosine deaminase complexed with 6-hydroxyl-1,6-dihydropurine ribonucleoside, a nearly ideal transition-state analog, has been determined and refined at 2.4 angstrom resolution. The structure is folded as an eight-stranded parallel alpha/beta barrel with a deep pocket
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