Adenosine Deaminase Chemical Properties

storage temp. 

2-8°C

solubility 

Buffered aqueous glycerol solution

form 

solution (clear)

color 

pale yellow

biological source

bovine spleen

Water Solubility 

water: miscible

Specific Activity

150-200units/mg protein

Safety Information

Safety Statements 

23-24/25

WGK Germany 

3

F 

10

HS Code 

35079090

Storage Class

10 - Combustible liquids

MSDS

• Language:English Provider:SigmaAldrich

Adenosine Deaminase Usage And Synthesis

Description

Adenosine deaminase (ADA) is a purine catabolic enzyme ubiquitous in mammalian tissue which catalyzes deamination of both adenosine and 2'-deoxyadenosine to inosine and 2'-deoxyinosine respectively. ADA is a class of nucleoside catabolic enzymes with significant links to the body's cellular immune system, comprising a group of thiol-containing hydrolases. ADA plays a pivotal role in purine nucleotide catabolism, catalysing the degradation of adenosine nucleosides into inosine nucleosides. These inosine nucleosides are subsequently phosphorylated by nucleoside phosphorylase into inosine, which is ultimately oxidised into the metabolic product uric acid.

ADA is widely distributed throughout the body, with the highest levels found in the thymus, spleen, and other lymphoid tissues. It is also present in the liver, kidneys, skeletal muscle, and lungs. In peripheral blood, lymphocytes and monocytes show the highest enzymatic activity. The activity in red blood cells and granulocytes is 40–70 times greater than that in serum, with T lymphocytes exhibiting higher activity than B lymphocytes.
Gel electrophoresis can distinguish between the ADA1, ADA2, and ADA2‑1 subtypes, whose phenotypes are controlled by the ADA1 and ADA2 alleles on chromosome 20. Typing can generally be performed using three-month-old blood spots. Among the Han Chinese population in China, ADA1 accounts for about 95% of cases, while among ethnic minorities it constitutes approximately 84%. The ability to distinguish individual ADA subtypes remains relatively limited.

Chemical Properties

White amorphous powder

Uses

Adenosine deaminase is useful in various molecular biology assays, such as glycerol release assays . Adenosine deaminase is a potential target for treatments of combined immunodeficiency disease.

Uses

Adenosine deaminase has been used to pre-treat primary Kupffer cells.

Biological Functions

Adenosine deaminase(EC 3.5.4.4), found in a wide variety of microorganisms, plants, invertebrates, and animals, plays a role in purine metabolism.

General Description

Molecular weight: 32.5-33 kDa

pI: 4.85

Biochem/physiol Actions

Adenosine deaminase is a purine catabolic enzyme which catalyzes the deamination of adenosine and 2′-deoxyadenosine with approximately equal specificity. It is ubiquitous in mammalian tissue, and deficiency in adenosine deaminase has been associated with severe combined immunodeficiency disease.

References

[1] KURATA N. [Adenosine deaminase].[J]. Nihon rinsho. Japanese journal of clinical medicine, 1995, 53 5: 1178-1183. 
[2] N. SPENCER   HARRY H  D A HOPKINSON. Adenosine deaminase polymorphism in man[J]. Annals of Human Genetics, 1968, 32 1: 9-14. DOI:10.1111/j.1469-1809.1968.tb00044.x. 
[3] D A CARSON   J E S  J Kaye. Lymphospecific toxicity in adenosine deaminase deficiency and purine nucleoside phosphorylase deficiency: possible role of nucleoside kinase(s).[J]. Proceedings of the National Academy of Sciences of the United States of America, 1977, 74 12: 5677-5681. DOI:10.1073/pnas.74.12.5677. 
[4] QIU-LI LIANG. Diagnostic accuracy of adenosine deaminase in tuberculous pleurisy: A meta-analysis[J]. Respiratory medicine, 2008, 102 5: Pages 744-754. DOI:10.1016/j.rmed.2007.12.007. 
[5] J. UNGERER. Serum adenosine deaminase: isoenzymes and diagnostic application.[J]. Clinical chemistry, 1992, 99 1: 1322-1326. DOI:10.1093/CLINCHEM/38.7.1322. 
[6] LIQIAO HAN . Optimization of an enzyme-coupling method by spectrophotometer for serum adenosine deaminase: As a candidate reference method[J]. Analytical biochemistry, 2019, 587: Article 113462. DOI:10.1016/j.ab.2019.113462.

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