asparaginase | 3.1.1.- Carboxylic Ester Hydrolases | IUPHAR/BPS Guide to PHARMACOLOGY

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asparaginase

Target not currently curated in GtoImmuPdb

Target id: 2762

Nomenclature: asparaginase

Family: 3.1.1.- Carboxylic Ester Hydrolases

Annotation status:  image of a grey circle Awaiting annotation/under development. Please contact us if you can help with annotation.  » Email us

Gene and Protein Information
Species TM AA Chromosomal Location Gene Symbol Gene Name Reference
Human - 573 14q32.33 ASPG asparaginase
Mouse - 564 12 F1 Aspg asparaginase
Rat - 564 6q32 Aspg asparaginase
Previous and Unofficial Names
60 kDa lysophospholipase | GPA/WT | LPP60 | asparaginase homolog (S. cerevisiae)
Database Links
BRENDA
CATH/Gene3D
Ensembl Gene
Entrez Gene
Human Protein Atlas
KEGG Enzyme
KEGG Gene
RefSeq Nucleotide
RefSeq Protein
UniProtKB
Wikipedia
Enzyme Reaction
EC Number: 3.1.1.5
EC Number: 3.1.1.47
EC Number: 3.5.1.1
General Comments
This protein has multiple functions. It acts as a lysophospholipase, a transacylase, a platelet-activating factor (PAF) acetylhydrolase and an L-asparaginase. L-asparaginase catalyses the deamination of asparagine to aspartic acid and a single ammonium ion. This action decreases circulating free asparagine in plasma.
Synthetic versions of L-asparaginase (e.g. crisantaspase) are used for clinical antineoplastic activity in acute lymphoblastic leukemia (ALL). ALL cells lack endogenous asparagine synthase and so are unable to generate the asparagine that is required to supply the protein synthesis pathway and feed tumour cell proliferation. Advanced combination therapeutic regimens have been developed which can utilise longer acting enzyme formulations such as pegaspargase and calaspargase pegol (Asparlas®) which are pegylated to extend circulating half-life [1-3].

References

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1. Angiolillo AL, Schore RJ, Devidas M, Borowitz MJ, Carroll AJ, Gastier-Foster JM, Heerema NA, Keilani T, Lane AR, Loh ML et al.. (2014) Pharmacokinetic and pharmacodynamic properties of calaspargase pegol Escherichia coli L-asparaginase in the treatment of patients with acute lymphoblastic leukemia: results from Children's Oncology Group Study AALL07P4. J. Clin. Oncol., 32 (34): 3874-82. [PMID:25348002]

2. Ribera JM, Morgades M, Montesinos P, Martino R, Barba P, Soria B, Bermúdez A, Moreno MJ, González-Campos J, Vives S et al.. (2018) Efficacy and safety of native versus pegylated Escherichia coli asparaginase for treatment of adults with high-risk, Philadelphia chromosome-negative acute lymphoblastic leukemia. Leuk. Lymphoma, 59 (7): 1634-1643. [PMID:29165013]

3. Silverman LB, Blonquist TM, Hunt SK, Kay-Green S, Athale UH, Clavell LA, Cole PD, Kelly KM, Laverdiere C, Leclerc J-M et al.. (2016) Randomized Study of Pegasparagase (SS-PEG) and Calaspargase Pegol (SC-PEG) in Pediatric Patients with Newly Diagnosed Acute Lymphoblastic Leukemia or Lymphoblastic Lymphoma: Results of DFCI ALL Consortium Protocol 11-001. Blood, 128: 175.

How to cite this page

3.1.1.- Carboxylic Ester Hydrolases: asparaginase. Last modified on 07/01/2019. Accessed on 19/07/2019. IUPHAR/BPS Guide to PHARMACOLOGY, http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=2762.