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Maltase-glucoamylase
Introduction
Maltase-glucoamylase, intestinal is an enzyme that in humans is encoded by the MGAM gene.[1][2]
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.[3] In the small intestine, this enzyme works in synergy with sucrase-isomaltase and alpha-amylase to digest the full range of dietary starches.
References
References
- ↑ “Entrez Gene: maltase-glucoamylase (alpha-glucosidase)”.
- ↑ Nichols BL, Eldering J, Avery S, Hahn D, Quaroni A, Sterchi E (January 1998). “Human small intestinal maltase-glucoamylase cDNA cloning. Homology to sucrase-isomaltase”. J. Biol. Chem. 273 (5): 3076–81. doi:10.1074/jbc.273.5.3076. PMID 9446624.
- ↑ Quezada-Calvillo R, Sim L, Ao Z, Hamaker BR, Quaroni A, Brayer GD, Sterchi EE, Robayo-Torres CC, Rose DR, Nichols BL (2008). “Luminal starch substrate “brake” on maltase-glucoamylase activity is located within the glucoamylase subunit”. J. Nutr. 138 (4): 685–92. PMID 18356321.
Further reading
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.
- TuÄŸrul 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.