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alpha glucosidase

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Target not currently curated in GtoImmuPdb

Target id: 2611

Nomenclature: alpha glucosidase

Family: 3.2.1.- Glycosidases

Contents:

Gene and Protein Information Click here for help
Species TM AA Chromosomal Location Gene Symbol Gene Name Reference
Human - 952 17q25.3 GAA alpha glucosidase
Mouse - 953 11 83.35 cM Gaa glucosidase, alpha, acid
Rat - 953 10q32.3 Gaa alpha glucosidase
Previous and Unofficial Names Click here for help
glucosidase | glucosidase, alpha, acid | glucosidase, alpha; acid | glucosidase alpha, acid | lysosomal alpha-glucosidase
Database Links Click here for help
Alphafold P10253 (Hs)
BRENDA 3.2.1.20
ChEMBL Target CHEMBL2608 (Hs), CHEMBL1667668 (Mm), CHEMBL3513 (Rn)
DrugBank Target P10253 (Hs)
Ensembl Gene ENSG00000171298 (Hs), ENSMUSG00000025579 (Mm), ENSRNOG00000047656 (Rn)
Entrez Gene 2548 (Hs), 14387 (Mm), 367562 (Rn)
Human Protein Atlas ENSG00000171298 (Hs)
KEGG Enzyme 3.2.1.20
KEGG Gene hsa:2548 (Hs), mmu:14387 (Mm), rno:367562 (Rn)
OMIM 606800 (Hs)
Orphanet ORPHA121987 (Hs)
Pharos P10253 (Hs)
RefSeq Nucleotide NM_000152 (Hs), NM_008064 (Mm), NM_199118 (Rn)
RefSeq Protein NP_000143 (Hs), NP_032090 (Mm), NP_954549 (Rn)
UniProtKB P10253 (Hs), P70699 (Mm), Q6P7A9 (Rn)
Wikipedia GAA (Hs)
Enzyme Reaction Click here for help
EC Number: 3.2.1.20

Download all structure-activity data for this target as a CSV file go icon to follow link

Inhibitors
Key to terms and symbols View all chemical structures Click column headers to sort
Ligand Sp. Action Value Parameter Reference
1-deoxynojirimycin Small molecule or natural product Ligand has a PDB structure Hs Inhibition 6.8 pKi 4
⤷ pKi 6.8 (Ki 1.5x10-7 M) [4]
migalastat Small molecule or natural product Approved drug Ligand has a PDB structure Hs Binding 7.4 pIC50 1
⤷ pIC50 7.4 (IC50 4x10-8 M) [1]
miglitol Small molecule or natural product Approved drug Primary target of this compound Click here for species-specific activity table Ligand has a PDB structure Hs Inhibition 6.5 pIC50 3
⤷ pIC50 6.5 (IC50 3.5x10-7 M) [3]
Inhibitor Comments
1-deoxynojirimycin also inhibits the related enzyme, α-glucosidase neutral AB (GANAB; Q14697) with an IC50 value of 1300nM [2].
Immuno Process Associations
Immuno Process:  Inflammation
GO Annotations:  Associated to 1 GO processes
GO:0043312 neutrophil degranulation TAS
Immuno Process:  Cellular signalling
GO Annotations:  Associated to 1 GO processes
GO:0043312 neutrophil degranulation TAS
Clinically-Relevant Mutations and Pathophysiology Click here for help
Disease:  Glycogen storage disease II; GSD2
Synonyms: Glycogen storage disease due to acid maltase deficiency [Orphanet: ORPHA365]
Glycogen storage disease due to acid maltase deficiency, adult onset [Orphanet: ORPHA308604]
Glycogen storage disease due to acid maltase deficiency, infantile onset [Orphanet: ORPHA308552]
Glycogen storage disease due to acid maltase deficiency, juvenile onset [Orphanet: ORPHA308573]
Pompe disease
Disease Ontology: DOID:2752
OMIM: 232300
Orphanet: ORPHA308604, ORPHA365, ORPHA308552, ORPHA308573
Role:  Pompe disease is a progressive and debilitating muscle disorder. It is caused by deficiency of functional lysosomal acid alpha-glucosidase (GAA) which leads to accummulation of glucose in muscle cells, that causes irreversible cell damage. The most deleterious effects are due to wasting of the muscles required for respiratory function and mobility.
Comments:  Recombinant alpha glucosidase agents are used as enzyme replacement therapies to treat Pompe disease. Approved agents include Lumizyme® (alglucosidase alfa; 2010) and Nexviazyme® (avalglucosidase alfa-ngpt; 2021).
General Comments
GAA is one member of the α-glucosidase family of enzymes which break down starch and disaccharides to glucose. α-glucosidase inhibitors are used as adjuncts to help regulate glucose levels in patients with type 2 diabetes mellitus.

References

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1. Asano N, Ishii S, Kizu H, Ikeda K, Yasuda K, Kato A, Martin OR, Fan JQ. (2000) In vitro inhibition and intracellular enhancement of lysosomal alpha-galactosidase A activity in Fabry lymphoblasts by 1-deoxygalactonojirimycin and its derivatives. Eur J Biochem, 267 (13): 4179-86. [PMID:10866822]

2. Asano N, Oseki K, Kizu H, Matsui K. (1994) Nitrogen-in-the-ring pyranoses and furanoses: structural basis of inhibition of mammalian glycosidases. J Med Chem, 37 (22): 3701-6. [PMID:7966130]

3. Kuriyama C, Kamiyama O, Ikeda K, Sanae F, Kato A, Adachi I, Imahori T, Takahata H, Okamoto T, Asano N. (2008) In vitro inhibition of glycogen-degrading enzymes and glycosidases by six-membered sugar mimics and their evaluation in cell cultures. Bioorg Med Chem, 16 (15): 7330-6. [PMID:18595718]

4. Lesur B, Ducep J-B, Lalloz M-N, Ehrhard A, Danzin C. (1997) New deoxynojirimycin derivatives as potent inhibitors of intestinal α-glucohydrolases. Bioorg Med Chem Lett, 7 (3): 355-360.

How to cite this page

3.2.1.- Glycosidases: alpha glucosidase. Last modified on 09/08/2021. Accessed on 18/09/2021. IUPHAR/BPS Guide to PHARMACOLOGY, http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=2611.