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Target not currently curated in GtoImmuPdb

Target id: 2627

Nomenclature: maltase-glucoamylase

Family: 3.2.1.- Glycosidases

Gene and Protein Information Click here for help
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 Click here for help
maltase-glucoamylase, intestinal | MGA | maltase-glucoamylase (alpha-glucosidase)
Database Links Click here for help
ChEMBL Target
DrugBank Target
Ensembl Gene
Entrez Gene
Human Protein Atlas
KEGG Enzyme
RefSeq Nucleotide
RefSeq Protein
Enzyme Reaction Click here for help
EC Number:
EC Number:

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

Key to terms and symbols View all chemical structures Click column headers to sort
Ligand Sp. Action Value Parameter Reference
acarbose Small molecule or natural product Approved drug Ligand has a PDB structure Mm Inhibition 7.6 – 8.1 pKi 1
pKi 7.6 – 8.1 (Ki 2.8x10-8 – 9x10-9 M) [1]
Description: Affinity measured across splice variants of mouse MGAM catalytic subunit ctMGAM
miglitol Small molecule or natural product Approved drug Ligand has a PDB structure Mm Inhibition 6.0 – 6.7 pKi 1
pKi 6.0 – 6.7 (Ki 1x10-6 – 2.11x10-7 M) Inhibition across MGAM catalytic subunits [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 6.0 pKi 2
pKi 6.0 (Ki 1x10-6 M) [2]
Description: Inhibition of human recombinant N-terminal subunit of maltase-glucoamylase after 60 mins by glucose oxidase assay
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
Immuno Process:  Inflammation
Immuno Process:  Cellular signalling


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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]

How to cite this page

3.2.1.- Glycosidases: maltase-glucoamylase. Last modified on 13/08/2015. Accessed on 21/05/2024. IUPHAR/BPS Guide to PHARMACOLOGY,