| Systematic (IUPAC) name | |
|---|---|
| E. coli L-asparagine amidohydrolase | |
| Clinical data | |
| Trade names | Elspar |
| AHFS/Drugs.com | monograph |
| MedlinePlus | a682046 |
| Pregnancy cat. | C(US) |
| Legal status | POM (UK) |
| Pharmacokinetic data | |
| Half-life | 8-30 hrs |
| Identifiers | |
| CAS number | 9015-68-3 |
| ATC code | L01XX02 |
| DrugBank | BTD00011 |
| UNII | G4FQ3CKY5R |
| KEGG | D02997 |
| Chemical data | |
| Formula | C1377H2208N382O442S17 |
| Mol. mass | 31731.9 g/mol |
| (what is this?) (verify) |
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Asparaginase (EC 3.5.1.1) is an enzyme that catalyzes the hydrolysis of asparagine to aspartic acid. Asparaginases are naturally occurring enzymes expressed and produced by microorganisms. Different types of asparaginases can be used for different industrial and pharmaceutical purposes. The most common use of asparaginases is as a processing aid in the manufacture of food[1]. Marketed under the brand names Acrylaway and PreventASe, asparaginases are used to reduce the formation of acrylamide, a suspected carcinogen, in starchy food products such as snacks and biscuits.
A different asparaginase is marketed as a drug under the brand name Elspar for the treatment of acute lymphoblastic leukemia (ALL)[2] and is also used in some mast cell tumor protocols. [3] Unlike other chemotherapy agents, it can be given as an intramuscular, subcutaneous, or intravenous injection without fear of tissue irritation.
It is usually derived from Escherichia coli. Asparaginase produced by Erwinia chrysanthemi instead is known as crisantaspase (BAN), and is available in the United Kingdom under the trade name Erwinase.[2]
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Aspariginase can be used as a food processing aid to reduce the formation of acrylamide, a suspected carcinogen, in starchy food products. Acrylamide is a chemical compound that is formed in starchy foods when they are baked or fried. During heating the amino acid asparagine, naturally present in starchy foods, is converted into acrylamide in a process called the Maillard reaction. The reaction is responsible for giving baked or fried foods their brown color, crust and toasted flavor.
By adding asparaginase before baking or frying the food, asparagine is converted into another common amino acid, aspartic acid, and ammonium. As a result, asparagine cannot take part in the Maillard reaction, and therefore the formation of acrylamide is significantly reduced. Complete acrylamide removal is probably not possible due to other, minor asparagine-independent formation pathways[1].
As a food processing aid, asparaginases can effectively reduce the level of acrylamide up to 90% in a range of starchy foods without changing the taste and appearance of the end product[4].
The rationale behind asparaginase is that it takes advantage of the fact that ALL leukemic cells are unable to synthesize the non-essential amino acid asparagine, whereas normal cells are able to make their own asparagine; thus leukemic cells require high amount of asparagine. These leukemic cells depend on circulating asparagine. Asparaginase, however, catalyzes the conversion of L-asparagine to aspartic acid and ammonia. This deprives the leukemic cell of circulating asparagine.
The main side effect is an allergic or hypersensitivity reaction; anaphylaxis is a possibility.[2] Asparaginase has also been associated with pancreatitis. Additionally, it can also be associated with a coagulopathy as it decreases protein synthesis, including synthesis of coagulation factors (eg progressive isolated decrease of fibrinogen) and anticoagulant factor (generally antithrombin III; sometimes protein C & S as well), leading to bleeding or thrombotic events such as stroke.
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