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Gene and Protein Information | ||||||
Species | TM | AA | Chromosomal Location | Gene Symbol | Gene Name | Reference |
Human | 1 | 1857 | 7q34 | MGAM | maltase-glucoamylase | |
Mouse | - | 1827 | 6 B1 | Mgam | maltase-glucoamylase | |
Rat | - | - | 4q22 | Mgam | maltase-glucoamylase |
Previous and Unofficial Names |
maltase-glucoamylase, intestinal | MGA | maltase-glucoamylase (alpha-glucosidase) |
Database Links | |
Alphafold | O43451 (Hs) |
BRENDA | 3.2.1.20, 3.2.1.3 |
ChEMBL Target | CHEMBL2074 (Hs) |
DrugBank Target | O43451 (Hs) |
Ensembl Gene | ENSG00000257335 (Hs), ENSMUSG00000068587 (Mm) |
Entrez Gene | 8972 (Hs), 232714 (Mm), 312272 (Rn) |
Human Protein Atlas | ENSG00000257335 (Hs) |
KEGG Enzyme | 3.2.1.20, 3.2.1.3 |
KEGG Gene | hsa:8972 (Hs), mmu:232714 (Mm), rno:312272 (Rn) |
OMIM | 154360 (Hs) |
Pharos | O43451 (Hs) |
RefSeq Nucleotide | NM_004668 (Hs), NM_001171003 (Mm) |
RefSeq Protein | NP_004659 (Hs), NP_001164474 (Mm) |
SynPHARM | 79525 (in complex with miglitol) |
UniProtKB | O43451 (Hs) |
Wikipedia | MGAM (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 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Miglitol may also inhibit the lysosomal alpha-glucosidase (GAA) enzyme. Human maltase-glucoamylase is likely to be the primary molecular target of acarbose. |
Immuno Process Associations | ||
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1. Jones K, Sim L, Mohan S, Kumarasamy J, Liu H, Avery S, Naim HY, Quezada-Calvillo R, Nichols BL, Pinto BM et al.. (2011) Mapping the intestinal alpha-glucogenic enzyme specificities of starch digesting maltase-glucoamylase and sucrase-isomaltase. Bioorg Med Chem, 19 (13): 3929-34. [PMID:21669536]
2. Mohan S, Sim L, Rose DR, Pinto BM. (2010) Probing the active-site requirements of human intestinal N-terminal maltase-glucoamylase: Synthesis and enzyme inhibitory activities of a six-membered ring nitrogen analogue of kotalanol and its de-O-sulfonated derivative. Bioorg Med Chem, 18 (22): 7794-8. [PMID:20970346]
3.2.1.- Glycosidases: maltase-glucoamylase. Last modified on 13/08/2015. Accessed on 21/01/2025. IUPHAR/BPS Guide to PHARMACOLOGY, https://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=2627.