maltase-glucoamylase | 3.2.1.- Glycosidases | IUPHAR/BPS Guide to PHARMACOLOGY

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Target not currently curated in GtoImmuPdb

Target id: 2627

Nomenclature: maltase-glucoamylase

Family: 3.2.1.- Glycosidases

Annotation status:  image of a grey circle Awaiting annotation/under development. Please contact us if you can help with annotation.  » Email us

Gene and Protein Information
Species TM AA Chromosomal Location Gene Symbol Gene Name Reference
Human - 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
ChEMBL Target
DrugBank Target
Ensembl Gene
Entrez Gene
Human Protein Atlas
KEGG Enzyme
RefSeq Nucleotide
RefSeq Protein
Enzyme Reaction
EC Number:
EC Number:

Download all structure-activity data for this target as a CSV file

Key to terms and symbols View all chemical structures Click column headers to sort
Ligand Sp. Action Value Parameter Reference
acarbose 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 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 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
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


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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 12/07/2020. IUPHAR/BPS Guide to PHARMACOLOGY,