スクラーゼ・イソマルターゼ
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出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2013/11/24 15:43:11」(JST)
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sucrase-isomaltase (alpha-glucosidase) |
Identifiers |
Symbol |
SI |
Entrez |
6476 |
HUGO |
10856 |
OMIM |
609845 |
RefSeq |
NM_001041 |
UniProt |
P14410 |
Other data |
EC number |
3.2.1.10 |
Locus |
Chr. 3 q25.2-26.2 |
Sucrase-isomaltase (EC 3.2.1.10, oligo-1,6-glucosidase, limit dextrinase, isomaltase, exo-oligo-1,6-glucosidase, dextrin 6alpha-glucanohydrolase, alpha-limit dextrinase, dextrin 6-glucanohydrolase, oligosaccharide alpha-1,6-glucohydrolase) is a glucosidase enzyme with system name oligosaccharide 6-alpha-glucohydrolase.[1][2][3] This enzyme catalyses the following chemical reaction
- Hydrolysis of (1->6)-alpha-D-glucosidic linkages in some oligosaccharides produced from starch and glycogen by enzyme EC 3.2.1.1.
A deficiency is responsible for sucrose intolerance.
References[edit]
- ^ Hauri, H.-P., Quaroni, A. and Isselbacher, K.J. (1979). "Biogenesis of intestinal plasma membrane: posttranslational route and cleavage of sucrase-isomaltase". Proc. Natl. Acad. Sci. USA 76: 5183–5186. PMID 291933.
- ^ Sjöström, H., Norén, O., Christiansen, L., Wacker, H. and Semenza, G. (1980). "A fully active, two-active-site, single-chain sucrase-isomaltase from pig small intestine. Implications for the biosynthesis of a mammalian integral stalked membrane protein". J. Biol. Chem. 255: 11332–11338. PMID 7002920.
- ^ Rodriguez, I.R., Taravel, F.R. and Whelan, W.J. (1984). "Characterization and function of pig intestinal sucrase-isomaltase and its separate subunits". Eur. J. Biochem. 143: 575–582. PMID 6479163.
See also[edit]
- sucrase
- isomaltase
- brush border
External links[edit]
- Structure and evolution of the mammalian maltase-glucoamylase and sucrase-isomaltase
- Sucrase-isomaltase complex at the US National Library of Medicine Medical Subject Headings (MeSH)
Hydrolase: sugar hydrolases (EC 3.2)
|
|
3.2.1: Glycoside hydrolases |
Disaccharidase |
- Sucrase/Sucrase-isomaltase/Invertase
- Maltase
- Trehalase
- Lactase
|
|
Glucosidases |
- Cellulase
- Alpha-glucosidase
- Acid
- Neutral AB
- Neutral C
- Beta-glucosidase
- Debranching enzyme
|
|
Other |
- Amylase
- Chitinase
- Lysozyme
- Neuraminidase
- NEU1
- NEU2
- NEU3
- NEU4
- Bacterial neuraminidase
- Viral neuraminidase
- Galactosidases
- alpha-Mannosidase
- Glucuronidase
- Hyaluronidase
- Pullulanase
- Glucosylceramidase
- Galactosylceramidase
- Alpha-N-acetylgalactosaminidase
- Alpha-N-acetylglucosaminidase
- Fucosidase
- Hexosaminidase
- Iduronidase
- Maltase-glucoamylase
- Heparanase
|
|
|
3.2.2: Hydrolysing
N-Glycosyl compounds |
- DNA glycosylases: Oxoguanine glycosylase
|
|
- B
- enzm
- 1.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 10
- 11
- 13
- 14
- 15-18
- 2.1
- 3.1
- 4.1
- 5.1
- 6.1-3
|
|
|
|
Enzymes: multienzyme complexes
|
|
Photosynthesis |
Photosynthetic reaction center complex proteins · Photosystem (I, II)
|
|
Dehydrogenase |
Pyruvate dehydrogenase complex (E1, E2, E3) · Oxoglutarate dehydrogenase (OGDH, DLST, DLD) · Branched-chain alpha-keto acid dehydrogenase complex (BCKDHA, BCKDHB, DBT, DLD)
|
|
Other |
CAD (Carbamoyl phosphate synthase II, Aspartate carbamoyltransferase, Dihydroorotase) · Cholesterol side-chain cleavage enzyme · Cytochrome b6f complex · Electron transport chain · Fatty acid synthetase complex · Glycine decarboxylase complex · Mitochondrial trifunctional protein (HADHA, HADHB) · Phosphoenolpyruvate sugar phosphotransferase system · Polyketide synthase · Sucrase-isomaltase complex · Tryptophan synthase
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UpToDate Contents
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English Journal
- Design and Synthesis of Labystegines, Hybrid Iminosugars from LAB and Calystegine, as Inhibitors of Intestinal α-Glucosidases: Binding Conformation and Interaction for ntSI.
- Kato A1, Zhang ZL2, Wang HY2, Jia YM2, Yu CY2, Kinami K1, Hirokami Y1, Tsuji Y1, Adachi I1, Nash RJ3, Fleet GW4,5, Koseki J6, Nakagome I6, Hirono S6.
- The Journal of organic chemistry.J Org Chem.2015 May 1;80(9):4501-15. doi: 10.1021/acs.joc.5b00342. Epub 2015 Apr 13.
- This paper identifies the required configuration and orientation of α-glucosidase inhibitors, miglitol, α-1-C-butyl-DNJ, and α-1-C-butyl-LAB for binding to ntSI (isomaltase). Molecular dynamics (MD) calculations suggested that the flexibility around the keyhole of ntSI is lower than that of ctSI
- PMID 25843107
- Dietary phenolic compounds selectively inhibit the individual subunits of maltase-glucoamylase and sucrase-isomaltase with the potential of modulating glucose release.
- Simsek M1, Quezada-Calvillo R2,3, Ferruzzi MG1, Nichols BL3, Hamaker BR1.
- Journal of agricultural and food chemistry.J Agric Food Chem.2015 Apr 22;63(15):3873-9. doi: 10.1021/jf505425d. Epub 2015 Apr 13.
- In this study, it was hypothesized that dietary phenolic compounds selectively inhibit the individual C- and N-terminal (Ct, Nt) subunits of the two small intestinal α-glucosidases, maltase-glucoamylase (MGAM) and sucrase-isomaltase (SI), for a modulated glycemic carbohydrate digestion. The inhibit
- PMID 25816913
- Generation of enterocyte-like cells with pharmacokinetic functions from human induced pluripotent stem cells using small-molecule compounds.
- Iwao T1, Kodama N1, Kondo Y1, Kabeya T1, Nakamura K1, Horikawa T1, Niwa T1, Kurose K1, Matsunaga T2.
- Drug metabolism and disposition: the biological fate of chemicals.Drug Metab Dispos.2015 Apr;43(4):603-10. doi: 10.1124/dmd.114.062604. Epub 2015 Feb 3.
- The small intestine plays an important role in all aspects of pharmacokinetics, but there is no system for the comprehensive evaluation of small-intestinal pharmacokinetics, including drug metabolism and absorption. In this study, we aimed to construct an intestinal pharmacokinetics evaluation syste
- PMID 25650381
Japanese Journal
- Different sucrose-isomaltase response of Caco-2 cells to glucose and maltose suggests dietary maltose sensing
- Jejunal Induction of SI and SGLT1 Genes in Rats by High-Starch/Low-Fat Diet Is Associated with Histone Acetylation and Binding of GCN5 on the Genes
- Journal of nutritional science and vitaminology 57(2), 162-169, 2011-04-01
- NAID 10030028908
- クロマチンリモデリング因子による小腸吸収細胞遺伝子発現誘導機構
- 日本栄養・食糧学会誌 : Nippon eiy◆U014D◆ shokury◆U014D◆ gakkaishi = Journal of Japanese Society of Nutrition and Food Science 62(6), 281-290, 2009-12-10
- NAID 10026248595
Related Links
- Congenital sucrase-isomaltase deficiency is a disorder that affects a person's ability to digest certain sugars. People with this condition cannot break down the sugars sucrose and maltose. Sucrose (a sugar found in ...
- This gene encodes a sucrase-isomaltase enzyme that is expressed in the intestinal brush border. The encoded protein is synthesized as a precursor protein that is cleaved by pancreatic proteases into two enzymatic subunits ...
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- 関
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[★]
スクラーゼ・ソマルターゼ欠損症
[★]
イソマルターゼ
- 関
- oligo-1,6-glucosidase