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Gene and Protein Information ![]() |
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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 ![]() |
glucosidase | glucosidase, alpha, acid | glucosidase, alpha; acid | glucosidase alpha, acid | lysosomal alpha-glucosidase |
Database Links ![]() |
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Alphafold | P10253 (Hs), P70699 (Mm), Q6P7A9 (Rn) |
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 ![]() |
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Download all structure-activity data for this target as a CSV file
Inhibitors | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Key to terms and symbols | View all chemical structures | Click column headers to sort | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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View species-specific inhibitor tables | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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 | ||
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Clinically-Relevant Mutations and Pathophysiology ![]() |
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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. |
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. He M, Zhai Y, Zhang Y, Xu S, Yu S, Wei Y, Xiao H, Song Y. (2022) Inhibition of α-glucosidase by trilobatin and its mechanism: kinetics, interaction mechanism and molecular docking. Food Funct, 13 (2): 857-866. [PMID:34989743]
4. 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]
5. 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.
3.2.1.- Glycosidases: alpha glucosidase. Last modified on 08/01/2024. Accessed on 06/02/2025. IUPHAR/BPS Guide to PHARMACOLOGY, https://www.guidetoimmunopharmacology.org/GRAC/ObjectDisplayForward?objectId=2611.