[{"@context":"http:\/\/schema.org\/","@type":"BlogPosting","@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/mannosyl-oligosaccharide-glucosidase-wikipedia\/#BlogPosting","mainEntityOfPage":"https:\/\/wiki.edu.vn\/en\/wiki24\/mannosyl-oligosaccharide-glucosidase-wikipedia\/","headline":"Mannosyl-oligosaccharide glucosidase – Wikipedia","name":"Mannosyl-oligosaccharide glucosidase – Wikipedia","description":"before-content-x4 From Wikipedia, the free encyclopedia after-content-x4 Class of enzymes Mannosyl-oligosaccharide glucosidase (MOGS) (EC 3.2.1.106, processing alpha-glucosidase I, Glc3Man9NAc2 oligosaccharide","datePublished":"2015-11-24","dateModified":"2015-11-24","author":{"@type":"Person","@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/author\/lordneo\/#Person","name":"lordneo","url":"https:\/\/wiki.edu.vn\/en\/wiki24\/author\/lordneo\/","image":{"@type":"ImageObject","@id":"https:\/\/secure.gravatar.com\/avatar\/c9645c498c9701c88b89b8537773dd7c?s=96&d=mm&r=g","url":"https:\/\/secure.gravatar.com\/avatar\/c9645c498c9701c88b89b8537773dd7c?s=96&d=mm&r=g","height":96,"width":96}},"publisher":{"@type":"Organization","name":"Enzyklop\u00e4die","logo":{"@type":"ImageObject","@id":"https:\/\/wiki.edu.vn\/wiki4\/wp-content\/uploads\/2023\/08\/download.jpg","url":"https:\/\/wiki.edu.vn\/wiki4\/wp-content\/uploads\/2023\/08\/download.jpg","width":600,"height":60}},"image":{"@type":"ImageObject","@id":"https:\/\/upload.wikimedia.org\/wikipedia\/commons\/thumb\/a\/af\/MOGS_substrate.png\/325px-MOGS_substrate.png","url":"https:\/\/upload.wikimedia.org\/wikipedia\/commons\/thumb\/a\/af\/MOGS_substrate.png\/325px-MOGS_substrate.png","height":"268","width":"325"},"url":"https:\/\/wiki.edu.vn\/en\/wiki24\/mannosyl-oligosaccharide-glucosidase-wikipedia\/","about":["Wiki"],"wordCount":2832,"articleBody":"     (adsbygoogle = window.adsbygoogle || []).push({});before-content-x4From Wikipedia, the free encyclopedia       (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4Class of enzymesMannosyl-oligosaccharide glucosidase (MOGS) (EC 3.2.1.106, processing alpha-glucosidase I, Glc3Man9NAc2 oligosaccharide glucosidase, trimming glucosidase I, GCS1) is an enzyme with systematic name mannosyl-oligosaccharide glucohydrolase.[1][2][3][4][5] MOGS is a transmembrane protein found in the membrane of the endoplasmic reticulum of eukaryotic cells.  Biologically, it functions within the N-glycosylation pathway.       (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4Table of ContentsEnzyme mechanism[edit]Substrate Specificity[edit]References[edit]External links[edit]Enzyme mechanism[edit]MOGS is a glycoside hydrolase enzyme, belonging to Family 63 as classified within the Carbohydrate-Active Enzyme database.[6]This enzyme catalyses the following chemical reaction:       (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4Exohydrolysis of the non-reducing terminal glucose residue in the mannosyl-oligosaccharide glycan Glc3Man9GlcNAc2This reaction is the first trimming step in the N-glycosylation pathway.  Prior to this, the glycan was co-translationally attached to a nascent protein by the oligosaccharyltransferase complex.  MOGS removes the terminal glucose residue, leaving the glycoprotein linked to Glc2Man9GlcNAc2, which can then serve as a substrate for glucosidase II.Substrate Specificity[edit]MOGS is highly specific to the oligosaccharide in its biological substrate in the N-glycosylation pathway.  Eukaryotic MOGS does not cleave simple substrates such as p-nitrophenyl glucose, and it also shows no activity to the \u03b1(1\u21923) linkage present at the terminus of Glc1-2Man9GlcNAc2.[7][8][9]  Furthermore, the minimum substrate is the glucotriose molecule (Glc-\u03b1(1\u21922)-Glc-\u03b1(1\u21923)-Glc), linked as in its native Glc3Man9GlcNAc2 substrate.   Kojibiose, the disaccharide Glc-\u03b1(1\u21922)-Glc, acts as a weak inhibitor on plant, animal, and yeast MOGS.[8][10][11][12]MOGS also acts to lesser extent on the corresponding glycolipids and glycopeptides.References[edit]^ Elting JJ, Chen WW, Lennarz WJ (March 1980). “Characterization of a glucosidase involved in an initial step in the processing of oligosaccharide chains”. The Journal of Biological Chemistry. 255 (6): 2325\u201331. PMID\u00a07358674.^ Grinna LS, Robbins PW (September 1979). “Glycoprotein biosynthesis. Rat liver microsomal glucosidases which process oligosaccharides”. The Journal of Biological Chemistry. 254 (18): 8814\u20138. PMID\u00a0479161.^ Kilker RD, Saunier B, Tkacz JS, Herscovics A (May 1981). “Partial purification from Saccharomyces cerevisiae of a soluble glucosidase which removes the terminal glucose from the oligosaccharide Glc3Man9GlcNAc2”. The Journal of Biological Chemistry. 256 (10): 5299\u2013603. PMID\u00a07014569.^ Grinna LS, Robbins PW (March 1980). “Substrate specificities of rat liver microsomal glucosidases which process glycoproteins”. The Journal of Biological Chemistry. 255 (6): 2255\u20138. PMID\u00a07358666.^ Michael JM, Kornfeld S (January 1980). “Partial purification and characterization of the glucosidases involved in the processing of asparagine-linked oligosaccharides”. Archives of Biochemistry and Biophysics. 199 (1): 249\u201358. doi:10.1016\/0003-9861(80)90278-7. PMID\u00a07356331.^ “CAZy – GH63”. www.cazy.org. Retrieved 2016-04-05.^ Vijay IK, Shailubhai K, Dong-Yu B, Pratta MA, Saxena S (1988-04-01). “Studies on the biosynthesis and regulation of asparagine-linked glycoproteins in the lactating mammary gland”. Indian Journal of Biochemistry & Biophysics. 25 (1\u20132): 127\u201332. PMID\u00a02846425.^ a b Dhanawansa R, Faridmoayer A, van der Merwe G, Li YX, Scaman CH (March 2002). “Overexpression, purification, and partial characterization of Saccharomyces cerevisiae processing alpha glucosidase I”. Glycobiology. 12 (3): 229\u201334. doi:10.1016\/0014-5793(86)80982-6. PMID\u00a011971867.^ Shailubhai K, Saxena ES, Balapure AK, Vijay IK (June 1990). “Developmental regulation of glucosidase I, an enzyme involved in the processing of asparagine-linked glycoproteins in rat mammary gland”. The Journal of Biological Chemistry. 265 (17): 9701\u20136. PMID\u00a02190984.^ Zeng YC, Elbein AD (July 1998). “Purification to homogeneity and properties of plant glucosidase I”. Archives of Biochemistry and Biophysics. 355 (1): 26\u201334. doi:10.1006\/abbi.1998.0717. PMID\u00a09647663.^ Schweden J, Borgmann C, Legler G, Bause E (July 1986). “Characterization of calf liver glucosidase I and its inhibition by basic sugar analogs”. Archives of Biochemistry and Biophysics. 248 (1): 335\u201340. doi:10.1016\/0003-9861(86)90429-7. PMID\u00a02942110.^ Ugalde RA, Staneloni RJ, Leloir LF (December 1980). “Microsomal glucosidases of rat liver. Partial purification and inhibition by disaccharides”. European Journal of Biochemistry. 113 (1): 97\u2013103. doi:10.1111\/j.1432-1033.1980.tb06144.x. PMID\u00a07460954.External links[edit]       (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4"},{"@context":"http:\/\/schema.org\/","@type":"BreadcrumbList","itemListElement":[{"@type":"ListItem","position":1,"item":{"@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/#breadcrumbitem","name":"Enzyklop\u00e4die"}},{"@type":"ListItem","position":2,"item":{"@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/mannosyl-oligosaccharide-glucosidase-wikipedia\/#breadcrumbitem","name":"Mannosyl-oligosaccharide glucosidase – Wikipedia"}}]}]