3lpp
From Proteopedia
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===Crystal complex of N-terminal sucrase-isomaltase with kotalanol=== | ===Crystal complex of N-terminal sucrase-isomaltase with kotalanol=== | ||
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==Disease== | ==Disease== | ||
| - | + | [[http://www.uniprot.org/uniprot/SUIS_HUMAN SUIS_HUMAN]] Congenital sucrase-isomaltase deficiency. Defects in SI are the cause of congenital sucrase-isomaltase deficiency (CSID) [MIM:[http://omim.org/entry/222900 222900]]; also known as disaccharide intolerance I. CSID is an autosomal recessive intestinal disorder that is clinically characterized by fermentative diarrhea, abdominal pain, and cramps upon ingestion of sugar. The symptoms are the consequence of absent or drastically reduced enzymatic activities of sucrase and isomaltase. The prevalence of CSID is 0.02 % in individuals of European descent and appears to be much higher in Greenland, Alaskan, and Canadian native people. CSID arises due to post-translational perturbations in the intracellular transport, polarized sorting, aberrant processing, and defective function of SI.<ref>PMID:8609217</ref> <ref>PMID:10903344</ref> <ref>PMID:11340066</ref> <ref>PMID:14724820</ref> <ref>PMID:16329100</ref> | |
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| + | ==Function== | ||
| + | [[http://www.uniprot.org/uniprot/SUIS_HUMAN SUIS_HUMAN]] Plays an important role in the final stage of carbohydrate digestion. Isomaltase activity is specific for both alpha-1,4- and alpha-1,6-oligosaccharides.<ref>PMID:20356844</ref> | ||
==About this Structure== | ==About this Structure== | ||
| - | + | [[3lpp]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LPP OCA]. | |
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:020356844</ref><references group="xtra"/><references/> |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Oligo-1,6-glucosidase]] | [[Category: Oligo-1,6-glucosidase]] | ||
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[[Category: Membrane]] | [[Category: Membrane]] | ||
[[Category: Multifunctional enzyme]] | [[Category: Multifunctional enzyme]] | ||
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[[Category: Signal-anchor]] | [[Category: Signal-anchor]] | ||
[[Category: Sulfation]] | [[Category: Sulfation]] | ||
[[Category: Transmembrane]] | [[Category: Transmembrane]] | ||
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 21 08:30:21 2010'' | ||
Revision as of 23:11, 10 April 2013
Contents |
Crystal complex of N-terminal sucrase-isomaltase with kotalanol
Template:ABSTRACT PUBMED 20356844
Disease
[SUIS_HUMAN] Congenital sucrase-isomaltase deficiency. Defects in SI are the cause of congenital sucrase-isomaltase deficiency (CSID) [MIM:222900]; also known as disaccharide intolerance I. CSID is an autosomal recessive intestinal disorder that is clinically characterized by fermentative diarrhea, abdominal pain, and cramps upon ingestion of sugar. The symptoms are the consequence of absent or drastically reduced enzymatic activities of sucrase and isomaltase. The prevalence of CSID is 0.02 % in individuals of European descent and appears to be much higher in Greenland, Alaskan, and Canadian native people. CSID arises due to post-translational perturbations in the intracellular transport, polarized sorting, aberrant processing, and defective function of SI.[1] [2] [3] [4] [5]
Function
[SUIS_HUMAN] Plays an important role in the final stage of carbohydrate digestion. Isomaltase activity is specific for both alpha-1,4- and alpha-1,6-oligosaccharides.[6]
About this Structure
3lpp is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Sim L, Willemsma C, Mohan S, Naim HY, Pinto BM, Rose DR. Structural basis for substrate selectivity in human maltase-glucoamylase and sucrase-isomaltase N-terminal domains. J Biol Chem. 2010 Jun 4;285(23):17763-70. Epub 2010 Mar 31. PMID:20356844 doi:10.1074/jbc.M109.078980
- ↑ Ouwendijk J, Moolenaar CE, Peters WJ, Hollenberg CP, Ginsel LA, Fransen JA, Naim HY. Congenital sucrase-isomaltase deficiency. Identification of a glutamine to proline substitution that leads to a transport block of sucrase-isomaltase in a pre-Golgi compartment. J Clin Invest. 1996 Feb 1;97(3):633-41. PMID:8609217 doi:http://dx.doi.org/10.1172/JCI118459
- ↑ Jacob R, Zimmer KP, Schmitz J, Naim HY. Congenital sucrase-isomaltase deficiency arising from cleavage and secretion of a mutant form of the enzyme. J Clin Invest. 2000 Jul;106(2):281-7. PMID:10903344 doi:10.1172/JCI9677
- ↑ Spodsberg N, Jacob R, Alfalah M, Zimmer KP, Naim HY. Molecular basis of aberrant apical protein transport in an intestinal enzyme disorder. J Biol Chem. 2001 Jun 29;276(26):23506-10. Epub 2001 May 4. PMID:11340066 doi:10.1074/jbc.C100219200
- ↑ Ritz V, Alfalah M, Zimmer KP, Schmitz J, Jacob R, Naim HY. Congenital sucrase-isomaltase deficiency because of an accumulation of the mutant enzyme in the endoplasmic reticulum. Gastroenterology. 2003 Dec;125(6):1678-85. PMID:14724820
- ↑ Sander P, Alfalah M, Keiser M, Korponay-Szabo I, Kovacs JB, Leeb T, Naim HY. Novel mutations in the human sucrase-isomaltase gene (SI) that cause congenital carbohydrate malabsorption. Hum Mutat. 2006 Jan;27(1):119. PMID:16329100 doi:10.1002/humu.9392
- ↑ Sim L, Willemsma C, Mohan S, Naim HY, Pinto BM, Rose DR. Structural basis for substrate selectivity in human maltase-glucoamylase and sucrase-isomaltase N-terminal domains. J Biol Chem. 2010 Jun 4;285(23):17763-70. Epub 2010 Mar 31. PMID:20356844 doi:10.1074/jbc.M109.078980
Categories: Homo sapiens | Oligo-1,6-glucosidase | Rose, D R. | Sim, L. | Alpha-glucosidase | Cell membrane | Disease mutation | Disulfide bond | Glycoprotein | Glycosidase | Glycoside hydrolase family 31 | Hydrolase | Isomaltase | Membrane | Multifunctional enzyme | Signal-anchor | Sulfation | Transmembrane
