麦芽糖酶-葡糖淀粉酶：修订间差异

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
终止	142,106,747 bp
基因位置（小鼠）
染色体	小鼠6号染色体
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
	8972
	232714
	ENSG00000257335; ENSG00000282607
	ENSMUSG00000068587
	O43451
	无数据
	NM_004668; NM_001365693
	NM_001171003; NM_001368875
	NP_004659; NP_001352622
	无数据
	維基數據
檢視/編輯人類	檢視/編輯小鼠

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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。^[6]^[7]

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。^[8] 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.
Takeshita F, Ishii KJ, Kobiyama K, et al. TRAF4 acts as a silencer in TLR-mediated signaling through the association with TRAF6 and TRIF.. Eur. J. Immunol. 2005, 35 (8): 2477–85. PMID 16052631. doi:10.1002/eji.200526151.
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.
Danielsen EM. Tyrosine sulfation, a post-translational modification of microvillar enzymes in the small intestinal enterocyte.. EMBO J. 1987, 6 (10): 2891–6. PMC 553723 . PMID 3121301.
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.

参考文献

^ 對Maltase-glucoamylase起作用的藥物；在維基數據上查看/編輯參考.
^ ^2.0 ^2.1 ^2.2 GRCh38: Ensembl release 89: ENSG00000257335、ENSG00000282607 - Ensembl, May 2017
^ ^3.0 ^3.1 ^3.2 GRCm38: Ensembl release 89: ENSMUSG00000068587 - Ensembl, May 2017
^ Human PubMed Reference:. National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Mouse PubMed Reference:. National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Entrez Gene: maltase-glucoamylase (alpha-glucosidase).
^ Nichols BL, Eldering J, Avery S, Hahn D, Quaroni A, Sterchi E. Human small intestinal maltase-glucoamylase cDNA cloning. Homology to sucrase-isomaltase. J. Biol. Chem. January 1998, 273 (5): 3076–81. PMID 9446624. doi:10.1074/jbc.273.5.3076.
^ Luminal starch substrate "brake" on maltase-glucoamylase activity is located within the glucoamylase subunit. J. Nutr. 2008, 138 (4): 685–92. PMID 18356321.

[1] 對Maltase-glucoamylase起作用的藥物；在維基數據上查看/編輯參考.

[refGRCh38Ensembl-2] 2.0 ^2.1 ^2.2 GRCh38: Ensembl release 89: ENSG00000257335、ENSG00000282607 - Ensembl, May 2017

[refGRCm38Ensembl-3] 3.0 ^3.1 ^3.2 GRCm38: Ensembl release 89: ENSMUSG00000068587 - Ensembl, May 2017

[4] Human PubMed Reference:. National Center for Biotechnology Information, U.S. National Library of Medicine.

[5] Mouse PubMed Reference:. National Center for Biotechnology Information, U.S. National Library of Medicine.

[entrez-6] Entrez Gene: maltase-glucoamylase (alpha-glucosidase).

[pmid9446624-7] Nichols BL, Eldering J, Avery S, Hahn D, Quaroni A, Sterchi E. Human small intestinal maltase-glucoamylase cDNA cloning. Homology to sucrase-isomaltase. J. Biol. Chem. January 1998, 273 (5): 3076–81. PMID 9446624. doi:10.1074/jbc.273.5.3076.

[pmid18356321-8] Luminal starch substrate "brake" on maltase-glucoamylase activity is located within the glucoamylase subunit. J. Nutr. 2008, 138 (4): 685–92. PMID 18356321.

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@@ 第14行： / 第14行： @@
 *{{cite journal|title=The DNA sequence of human chromosome 7.|journal=Nature|issue=6945|doi=10.1038/nature01782|year=2003|volume=424|pages=157–64|pmid=12853948|vauthors=Hillier LW, Fulton RS, Fulton LA, etal}}
 *{{cite journal|title=Tyrosine sulfation, a post-translational modification of microvillar enzymes in the small intestinal enterocyte.|url=https://archive.org/details/sim_embo-journal_1987-10_6_10/page/2891|author=Danielsen EM|journal=EMBO J.|issue=10|doi=|year=1987|volume=6|pages=2891–6|pmc=553723|pmid=3121301}}
-*{{cite journal|title=A novel mutation of the GAA gene in a Finnish late-onset Pompe disease patient: clinical phenotype and follow-up with enzyme replacement therapy.|journal=Muscle Nerve|issue=1|doi=10.1002/mus.21291|year=2009|volume=40|pages=143–8|pmid=19472353|vauthors=Korpela MP, Paetau A, Löfberg MI, etal}}
+*{{cite journal|title=A novel mutation of the GAA gene in a Finnish late-onset Pompe disease patient: clinical phenotype and follow-up with enzyme replacement therapy.|url=https://archive.org/details/sim_muscle-nerve_2009-07_40_1/page/143|journal=Muscle Nerve|issue=1|doi=10.1002/mus.21291|year=2009|volume=40|pages=143–8|pmid=19472353|vauthors=Korpela MP, Paetau A, Löfberg MI, etal}}
 *{{cite journal|title=Human intestinal maltase-glucoamylase: crystal structure of the N-terminal catalytic subunit and basis of inhibition and substrate specificity.|journal=J. Mol. Biol.|issue=3|doi=10.1016/j.jmb.2007.10.069|year=2008|volume=375|pages=782–92|pmid=18036614|vauthors=Sim L, Quezada-Calvillo R, Sterchi EE, etal}}
 *{{cite journal|title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.|journal=Proc. Natl. Acad. Sci. U.S.A.|issue=26|doi=10.1073/pnas.242603899|year=2002|volume=99|pages=16899–903|pmc=139241|pmid=12477932|vauthors=Strausberg RL, Feingold EA, Grouse LH, etal}}