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Sucrase-isomaltase
From Proteopedia
(Difference between revisions)
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Some other key enzymes that capitalize on this characteristic in the small intestine are: glucoamylase (Maltase), lactase, and peptidases. Among these common enzymes however is SI, which is important because it is critically involved in the final stage of carbohydrate digestion. <ref> http://www.uniprot.org/uniprot/P14410</ref> Specifically, this enzyme works by catalyzing the conversion of isomaltose into glucose molecules. Cleaving bonds with water (hydrolysis), SI interacts with glucosidic linkages produced by alpha-amylase. <ref>Maureen Barlow Pugh, ed. (2000). Stedman's Medical Dictionary (27th ed.). Baltimore, Maryland, USA: Lippincott Williams & Wilkins. p. 65. ISBN 978-0-683-40007-6. </ref> | Some other key enzymes that capitalize on this characteristic in the small intestine are: glucoamylase (Maltase), lactase, and peptidases. Among these common enzymes however is SI, which is important because it is critically involved in the final stage of carbohydrate digestion. <ref> http://www.uniprot.org/uniprot/P14410</ref> Specifically, this enzyme works by catalyzing the conversion of isomaltose into glucose molecules. Cleaving bonds with water (hydrolysis), SI interacts with glucosidic linkages produced by alpha-amylase. <ref>Maureen Barlow Pugh, ed. (2000). Stedman's Medical Dictionary (27th ed.). Baltimore, Maryland, USA: Lippincott Williams & Wilkins. p. 65. ISBN 978-0-683-40007-6. </ref> | ||
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== Structure == | == Structure == | ||
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-The gene on which SI processes occur is located on chromosome 3 and is composed of 48 exons. | -The gene on which SI processes occur is located on chromosome 3 and is composed of 48 exons. | ||
</StructureSection> | </StructureSection> | ||
| - | ==3D structures of surase-isomaltase== | ||
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| - | Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | ||
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| - | [[3lpo]] - hSI N-terminal - human<br /> | ||
| - | [[3lpp]] - hSI N-terminal + kotalanol<br /> | ||
| - | [[4m56]] - BsSI + glucose - ''Bacillus subtilis''<br /> | ||
| - | [[4m8u]], [[4maz]], [[4mb1]] - BsSI (mutant)<br /> | ||
== References == | == References == | ||
<references /> | <references /> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Revision as of 08:42, 11 February 2020
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References
- ↑ http://www.siumed.edu/~dking2/erg/gicells.htm
- ↑ http://www.uniprot.org/uniprot/P14410
- ↑ Maureen Barlow Pugh, ed. (2000). Stedman's Medical Dictionary (27th ed.). Baltimore, Maryland, USA: Lippincott Williams & Wilkins. p. 65. ISBN 978-0-683-40007-6.
- ↑ "SI sucrase-isomaltase (alpha-glucosidase) [Homo sapiens (human)] - Gene - NCBI"
- ↑ Naim HY, Sterchi EE, Lentze MJ (1988). "Biosynthesis of the human sucrase-isomaltase complex. Differential O-glycosylation of the sucrase subunit correlates with its position within the enzyme complex". J. Biol. Chem. 263 (15): 7242–53. PMID 3366777
- ↑ http://www.jbc.org/content/254/6/1821.full.pdf
- ↑ http://onlinelibrary.wiley.com/doi/10.1111/j.1432-1033.1977.tb11335.x/epdf
- ↑ http://www.jbc.org/content/251/11/3250.full.pdf
- ↑ http://www.iffgd.org/site/gi-disorders/other/csid
- ↑ Sim L, Willemsma C, Mohan S, Naim HY, Pinto BM, Rose DR (2010). "Structural basis for substrate selectivity in human maltase-glucoamylase and sucrase-isomaltase N-terminal domains". J. Biol. Chem. 285 (23): 17763–70. doi:10.1074/jbc.M109.078980. PMC 2878540. PMID 20356844
