Maltase-glucoamylase

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

Maltase-glucoamylase (alpha-glucosidase)
PDB rendering based on 2qly.
Available structures PDB 2QLY, 2QMJ, 3CTT, 3L4T, 3L4U, 3L4V, 3L4W, 3L4X, 3L4Y, 3L4Z
Identifiers
Symbols	MGAM; MG; MGA
External IDs	OMIM: 154360 MGI: 1203495 HomoloGene: 88555 GeneCards: MGAM Gene
EC number	3.2.1.3
Gene Ontology Molecular function • catalytic activity • glucan 1,4-alpha-glucosidase activity • hydrolase activity, hydrolyzing O-glycosyl compounds • alpha-glucosidase activity • carbohydrate binding • maltose alpha-glucosidase activity Cellular component • plasma membrane • integral to membrane • apical plasma membrane Biological process • carbohydrate metabolic process • starch catabolic process • polysaccharide digestion Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	8972	232714
Ensembl	ENSG00000179087	ENSMUSG00000068587
UniProt	O43451	Q6XK23
RefSeq (mRNA)	NM_004668	NM_001171003.1
RefSeq (protein)	NP_004659	NP_001164474.1
Location (UCSC)	Chr 7: 141.61 – 141.81 Mb	Chr 6: 40.58 – 40.72 Mb
PubMed search	[1]	[2]

Maltase-glucoamylase, intestinal is an enzyme that in humans is encoded by the MGAM gene.^[1][2]

Maltase-glucoamylase is a saccharide digestive enzyme. It is existed mainly in mucosa and its function is to hydrolyze maltose, beta-limit dextrins and some kind of cyclodextrins.

See also

• Alpha-glucosidase
• Maltase

References

1. ^ "Entrez Gene: maltase-glucoamylase (alpha-glucosidase)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8972. 
2. ^ 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. 

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. 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. 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 
• 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.