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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 | |
Alphafold | Q86U10 (Hs), A0JNU3 (Mm), O88202 (Rn) |
BRENDA | 3.1.1.5, 3.1.1.47, 3.5.1.1 |
CATH/Gene3D | 3.40.50.1170, 3.40.50.40, 1.25.40.20 |
Ensembl Gene | ENSG00000166183 (Hs), ENSMUSG00000037686 (Mm), ENSRNOG00000012843 (Rn) |
Entrez Gene | 374569 (Hs), 104816 (Mm), 246266 (Rn) |
Human Protein Atlas | ENSG00000166183 (Hs) |
KEGG Enzyme | 3.1.1.5, 3.1.1.47, 3.5.1.1 |
KEGG Gene | hsa:374569 (Hs), mmu:104816 (Mm), rno:246266 (Rn) |
Pharos | Q86U10 (Hs) |
RefSeq Nucleotide | NM_001080464 (Hs), NM_001081169 (Mm), NM_144750 (Rn) |
RefSeq Protein | NP_001073933 (Hs), NP_001074638 (Mm), NP_653351 (Rn) |
UniProtKB | Q86U10 (Hs), A0JNU3 (Mm), O88202 (Rn) |
Wikipedia | ASPG (Hs) |
Enzyme Reaction | ||||||||||||
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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]. |
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.
3.1.1.- Carboxylic Ester Hydrolases: asparaginase. Last modified on 07/01/2019. Accessed on 17/01/2025. IUPHAR/BPS Guide to PHARMACOLOGY, https://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=2762.