Maltase-glucoamylase

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

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) Band 7q34 Start 141,907,813 bp End 142,106,747 bp
Gene location (Mouse) Chr. Chromosome 6 (mouse) Band 6|6 B1 Start 40,605,765 bp End 40,746,057 bp
RNA expression pattern Bgee Human Mouse (ortholog) 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 BioGPS 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 Species Human Mouse Entrez 8972 232714 Ensembl ENSG00000257335 ENSG00000282607 ENSMUSG00000068587 UniProt O43451 n/a RefSeq (mRNA) NM_004668 NM_001365693 NM_001171003 NM_001368875 RefSeq (protein) NP_004659 NP_001352622 n/a Location (UCSC) Chr 7: 141.91 – 142.11 Mb Chr 6: 40.61 – 40.75 Mb PubMed search
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.

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. Bibcode:2003PNAS..100.1432N. 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. Bibcode:2003Natur.424..157H. 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. doi:10.1002/j.1460-2075.1987.tb02592.x. 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. Bibcode:2002PNAS...9916899M. 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.

External links

• PDBe-KB provides an overview of all the structure information available in the PDB for Human Maltase-glucoamylase, intestinal