Maltase-glucoamylase

"MGAM" redirects here. For other uses, see MGAM (disambiguation).

VALUE_ERROR (nil)
Identifiers
Aliases
External IDs	GeneCards: [1]
Orthologs
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a
Wikidata
View/Edit Human

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.

See also

• Alpha-glucosidase
• Maltase

Further reading

• Nichols BL, Avery S, Sen P, et al. (2003). "The maltase-glucoamylase gene: common ancestry to sucrase-isomaltase with complementary starch digestion activities". Proc. Natl. Acad. Sci. U.S.A. 100 (3): 1432–7. doi:10.1073/pnas.0237170100. PMC 298790. PMID 12547908.
• 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. PMID 16052631.
• Hillier LW, Fulton RS, Fulton LA, et al. (2003). "The DNA sequence of human chromosome 7". Nature. 424 (6945): 157–64. doi:10.1038/nature01782. PMID 12853948.
• Danielsen EM (1987). "Tyrosine sulfation, a post-translational modification of microvillar enzymes in the small intestinal enterocyte". EMBO J. 6 (10): 2891–6. PMC 553723. PMID 3121301.
• 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 Nerve. 40 (1): 143–8. doi:10.1002/mus.21291. PMID 19472353.
• 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. PMID 18036614.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2002). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Naim HY, Sterchi EE, Lentze MJ (1988). "Structure, biosynthesis, and glycosylation of human small intestinal maltase-glucoamylase". J. Biol. Chem. 263 (36): 19709–17. PMID 3143729.
• 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. PMID 17485087.
• 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. PMID 18377903.