Maltase-glucoamylase, intestinal is an enzyme that in humans is encoded by the MGAMgene.
Maltase-glucoamylase is 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.
Takeshita F, Ishii KJ, Kobiyama K, et al. (2005). "TRAF4 acts as a silencer in TLR-mediated signaling through the association with TRAF6 and TRIF.". Eur. J. Immunol.35 (8): 2477–85. doi:10.1002/eji.200526151. PMID16052631.
Korpela MP, Paetau A, Löfberg MI, et al. (2009). "A novel mutation of the GAA gene in a Finnish late-onset Pompe disease patient: clinical phenotype and follow-up with enzyme replacement therapy.". Muscle Nerve40 (1): 143–8. doi:10.1002/mus.21291. PMID19472353.
Sim L, Quezada-Calvillo R, Sterchi EE, et al. (2008). "Human intestinal maltase-glucoamylase: crystal structure of the N-terminal catalytic subunit and basis of inhibition and substrate specificity.". J. Mol. Biol.375 (3): 782–92. doi:10.1016/j.jmb.2007.10.069. PMID18036614.
Naim HY, Sterchi EE, Lentze MJ (1988). "Structure, biosynthesis, and glycosylation of human small intestinal maltase-glucoamylase.". J. Biol. Chem.263 (36): 19709–17. PMID3143729.
Ao Z, Quezada-Calvillo R, Sim L, et al. (2007). "Evidence of native starch degradation with human small intestinal maltase-glucoamylase (recombinant).". FEBS Lett.581 (13): 2381–8. doi:10.1016/j.febslet.2007.04.035. PMID17485087.
Tuğrul S, Kutlu T, Pekin O, et al. (2008). "Clinical, endocrine, and metabolic effects of acarbose, an alpha-glucosidase inhibitor, in overweight and nonoverweight patients with polycystic ovarian syndrome.". Fertil. Steril.90 (4): 1144–8. doi:10.1016/j.fertnstert.2007.07.1326. PMID18377903.