maltase-glucoamylase

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

   GtoImmuPdb view: OFF :     Currently no data for maltase-glucoamylase in GtoImmuPdb

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
BRENDA
ChEMBL Target
DrugBank Target
Ensembl Gene
Entrez Gene
GenitoUrinary Development Molecular Anatomy Project
Human Protein Atlas
KEGG Enzyme
KEGG Gene
OMIM
RefSeq Nucleotide
RefSeq Protein
SynPHARM
UniProtKB
Wikipedia
Enzyme Reaction
EC Number: 3.2.1.20
EC Number: 3.2.1.3

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
Ligand Sp. Action Affinity Units 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.

References

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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 23/10/2017. IUPHAR/BPS Guide to PHARMACOLOGY, http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=2627.