Maltase-glucoamylase

MGAM
Available structures
PDB	Human UniProt search: PDBe RCSB
List of PDB id codes
	2QLY, 2QMJ, 3CTT, 3L4T, 3L4U, 3L4V, 3L4W, 3L4X, 3L4Y, 3L4Z, 3TON, 3TOP
Identifiers
Aliases	MGAM, MG, MGA, Maltase-glucoamylase
External IDs	OMIM: 154360; MGI: 1203495; HomoloGene: 130099; GeneCards: MGAM; OMA:MGAM - orthologs
Gene location (Human)
Chr.	Chromosome 7 (human)
End	142,106,747 bp
Gene location (Mouse)
Chr.	Chromosome 6 (mouse)
End	40,746,057 bp
RNA expression pattern
	Top expressed in
	duodenum; ; blood; ; bone marrow cells; ; spleen; ; right lung; ; granulocyte; ; human kidney; ; monocyte; ; gonad; ; renal cortex;
	Top expressed in
	jejunum; ; duodenum; ; ileum; ; Paneth cell; ; epithelium of small intestine; ; colon; ; left colon; ; granulocyte; ; migratory enteric neural crest cell; ; human kidney;
	More reference expression data
	n/a
Gene ontology
Molecular function	hydrolase activity, acting on glycosyl bonds; maltose alpha-glucosidase activity; hydrolase activity, hydrolyzing O-glycosyl compounds; catalytic activity; alpha-1,4-glucosidase activity; hydrolase activity; amylase activity; glucan 1,4-alpha-glucosidase activity; carbohydrate binding; alpha-glucosidase activity;
Cellular component	integral component of membrane; plasma membrane; apical plasma membrane; extracellular exosome; membrane; tertiary granule membrane; ficolin-1-rich granule membrane;
Biological process	polysaccharide digestion; metabolism; starch catabolic process; maltose metabolic process; neutrophil degranulation; carbohydrate metabolic process;
	Sources:Amigo / QuickGO
Orthologs
	8972
	232714
	ENSG00000257335; ENSG00000282607
	ENSMUSG00000068587
	O43451
	n/a
	NM_004668; NM_001365693
	NM_001171003; NM_001368875
	NP_004659; NP_001352622
	n/a
	Wikidata
View/Edit Human	View/Edit Mouse

Maltase-glucoamylase, intestinal is an enzyme that in humans is encoded by the MGAM gene.

Maltase-glucoamylase is an alpha-glucosidase digestive enzyme. It consists of two subunits with differing substrate specificity. Recombinant enzyme studies have shown that its N-terminal catalytic domain has highest activity against maltose, while the C-terminal domain has a broader substrate specificity and activity against glucose oligomers. In the small intestine, this enzyme works in synergy with sucrase-isomaltase and alpha-amylase to digest the full range of dietary starches.