MGAM
Domain
The N-terminal maltase domain (ntMGAM) mainly hydrolyzes short length oligomaltoses having two to four glucose residues.
The C-terminal glucoamylase domain (ctMGAM) acts on longer maltoside substrates having four to seven glucose residues.
Function
Alpha-(1,4) exo-glucosidase involved in breakdown of dietary starch oligosaccharides in small intestine. Cleaves the non-reducing alpha-(1,4)-linked glucose residue in linear dextrins with retention of anomeric center stereochemistry (PubMed:12547908, PubMed:18036614, PubMed:18356321, PubMed:22058037, PubMed:27480812). Mainly hydrolyzes short length oligomaltoses having two to seven glucose residues (PubMed:12547908, PubMed:18036614, PubMed:18356321, PubMed:22058037, PubMed:27480812). Can cleave alpha-(1,2), alpha-(1,3) and alpha-(1,6) glycosidic linkages with lower efficiency, whereas beta glycosidic linkages are usually not hydrolyzed (PubMed:27480812).
Pathway
Carbohydrate degradation.
Post-translational modifications
N- and O-glycosylated.
Does not undergo intracellular or extracellular proteolytic cleavage.
Sulfated.
Sequence Similarities
Belongs to the glycosyl hydrolase 31 family.
Tissue Specificity
Broadly expressed. Highly expressed in small intestine. Expressed in granulocytes.
Cellular localization
- Apical cell membrane
- Single-pass type II membrane protein
- Brush border.
Alternative names
MGA, MGAML, MGAM, Maltase-glucoamylase