麦芽糖酶-葡糖淀粉酶

麦芽糖酶-葡糖淀粉酶（英語：Maltase-glucoamylase）是一种由人体 MGAM 基因编码的酶。

麦芽糖酶-葡糖淀粉酶
已知的結構 PDB 直系同源搜索: PDBe RCSB PDBID列表 2QLY、​2QMJ、​3CTT、​3L4T、​3L4U、​3L4V、​3L4W、​3L4X、​3L4Y、​3L4Z、​3TON、​3TOP
識別號
别名	MGAM；, MG, MGA, Maltase-glucoamylase
外部ID	OMIM：154360 MGI：1203495 HomoloGene：130099 GeneCards：MGAM
為以下藥物的標靶
米格列醇
基因位置（人类） 染色体 7號染色體 基因座 7q34 起始 141,907,813 bp 终止 142,106,747 bp
基因位置（小鼠） 染色体 小鼠6号染色体 基因座 6|6 B1 起始 40,605,765 bp 终止 40,746,057 bp
基因本體 分子功能 • hydrolase activity, acting on glycosyl bonds • maltose alpha-glucosidase activity • hydrolase activity, hydrolyzing O-glycosyl compounds • 催化活性 • alpha-1,4-glucosidase activity • 水解酶活性 • amylase activity • glucan 1,4-alpha-glucosidase activity • carbohydrate binding • alpha-glucosidase activity 細胞組分 • integral component of membrane • 细胞膜 • apical plasma membrane • 外排體 • 膜 • tertiary granule membrane • ficolin-1-rich granule membrane 生物學過程 • polysaccharide digestion • 代謝 • starch catabolic process • maltose metabolic process • neutrophil degranulation • 碳水化合物代謝 Sources:Amigo / QuickGO
直系同源
物種	人類	小鼠
Entrez	8972	232714
Ensembl	ENSG00000257335 ​ENSG00000282607	ENSMUSG00000068587
UniProt	O43451	无数据
mRNA​序列	NM_004668 ​NM_001365693	NM_001171003 ​NM_001368875
蛋白序列	NP_004659 ​NP_001352622	无数据
基因位置​（UCSC）	Chr 7: 141.91 – 142.11 Mb	Chr 6: 40.61 – 40.75 Mb
PubMed​查找
維基數據
檢視/編輯人類 檢視/編輯小鼠

麦芽糖酶-葡糖淀粉酶是α-葡糖苷酶消化酶。它由两个具有不同底物特异性的亚基组成。 重组酶研究表明，其N-末端催化结构域对麦芽糖具有最高活性，而C-末端结构域具有更广泛的底物特异性和对葡萄糖寡聚体的活性。 在小肠中，这种酶与蔗糖-异麦芽糖酶和α-淀粉酶协同作用，以消化各种淀粉。

延伸阅读

• Nichols BL, Avery S, Sen P, et al. The maltase-glucoamylase gene: common ancestry to sucrase-isomaltase with complementary starch digestion activities.. Proc. Natl. Acad. Sci. U.S.A. 2003, 100 (3): 1432–7. PMC 298790 . PMID 12547908. doi:10.1073/pnas.0237170100. 
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• Hillier LW, Fulton RS, Fulton LA, et al. The DNA sequence of human chromosome 7.. Nature. 2003, 424 (6945): 157–64. PMID 12853948. doi:10.1038/nature01782. 
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• Korpela MP, Paetau A, Löfberg MI, et al. 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. 2009, 40 (1): 143–8. PMID 19472353. doi:10.1002/mus.21291. 
• Sim L, Quezada-Calvillo R, Sterchi EE, et al. Human intestinal maltase-glucoamylase: crystal structure of the N-terminal catalytic subunit and basis of inhibition and substrate specificity.. J. Mol. Biol. 2008, 375 (3): 782–92. PMID 18036614. doi:10.1016/j.jmb.2007.10.069. 
• Strausberg RL, Feingold EA, Grouse LH, et al. Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.. Proc. Natl. Acad. Sci. U.S.A. 2002, 99 (26): 16899–903. PMC 139241 . PMID 12477932. doi:10.1073/pnas.242603899. 
• Naim HY, Sterchi EE, Lentze MJ. Structure, biosynthesis, and glycosylation of human small intestinal maltase-glucoamylase.. J. Biol. Chem. 1988, 263 (36): 19709–17. PMID 3143729. 
• Ao Z, Quezada-Calvillo R, Sim L, et al. Evidence of native starch degradation with human small intestinal maltase-glucoamylase (recombinant).. FEBS Lett. 2007, 581 (13): 2381–8. PMID 17485087. doi:10.1016/j.febslet.2007.04.035. 
• Tuğrul S, Kutlu T, Pekin O, et al. Clinical, endocrine, and metabolic effects of acarbose, an alpha-glucosidase inhibitor, in overweight and nonoverweight patients with polycystic ovarian syndrome.. Fertil. Steril. 2008, 90 (4): 1144–8. PMID 18377903. doi:10.1016/j.fertnstert.2007.07.1326.