[{"@context":"http:\/\/schema.org\/","@type":"BlogPosting","@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/endoglycosidase-h-wikipedia\/#BlogPosting","mainEntityOfPage":"https:\/\/wiki.edu.vn\/en\/wiki24\/endoglycosidase-h-wikipedia\/","headline":"Endoglycosidase H – Wikipedia","name":"Endoglycosidase H – Wikipedia","description":"From Wikipedia, the free encyclopedia Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase EC no. 3.2.1.96 CAS no. 37278-88-9 Alt. names Endo-\u03b2-N-acetylglucosaminidase H, N,N’-diacetylchitobiosyl beta-N-acetylglucosaminidase, mannosyl-glycoprotein","datePublished":"2019-08-11","dateModified":"2019-08-11","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:\/\/en.wikipedia.org\/wiki\/Special:CentralAutoLogin\/start?type=1x1","url":"https:\/\/en.wikipedia.org\/wiki\/Special:CentralAutoLogin\/start?type=1x1","height":"1","width":"1"},"url":"https:\/\/wiki.edu.vn\/en\/wiki24\/endoglycosidase-h-wikipedia\/","wordCount":2965,"articleBody":"From Wikipedia, the free encyclopediaMannosyl-glycoprotein endo-beta-N-acetylglucosaminidaseEC no.3.2.1.96CAS no.37278-88-9 Alt. namesEndo-\u03b2-N-acetylglucosaminidase H, N,N’-diacetylchitobiosyl beta-N-acetylglucosaminidase, mannosyl-glycoprotein endo-beta-N-acetylglucosamidase, di-N-acetylchitobiosyl beta-N-acetylglucosaminidase, endo-beta-acetylglucosaminidase, endo-beta-(1->4)-N-acetylglucosaminidase, mannosyl-glycoprotein 1,4-N-acetamidodeoxy-beta-D-glycohydrolase, endoglycosidase S, endo-N-acetyl-beta-D-glucosaminidase, endo-N-acetyl-beta-glucosaminidase, endo-beta-N-acetylglucosaminidase D, endo-beta-N-acetylglucosaminidase F, endo-beta-N-acetylglucosaminidase H, endo-beta-N-acetylglucosaminidase L, glycopeptide-D-mannosyl-4-N-(N-acetyl-D-glucosaminyl)2-asparagine 1,4-N-acetyl-beta-glucosaminohydrolase, endoglycosidase HIntEnzIntEnz viewBRENDABRENDA entryExPASyNiceZyme viewKEGGKEGG entryMetaCycmetabolic pathwayPRIAMprofilePDB structuresRCSB PDB PDBe PDBsumThe enzyme endoglycosidase H (EC 3.2.1.96) is an enzyme with systematic name glycopeptide-D-mannosyl-N4-(N-acetyl-D-glucosaminyl)2-asparagine 1,4-N-acetyl-beta-glucosaminohydrolase.[1][2][3][4][5][6] It is a highly specific endoglycosidase which cleaves asparagine-linked mannose rich oligosaccharides, but not highly processed complex oligosaccharides from glycoproteins.  It is used for research purposes to deglycosylate glycoproteins and to monitor intracellular protein trafficking through the secretory pathway.Table of ContentsStructure and activity[edit]Biochemical applications[edit]References[edit]External links[edit]Close enzymes[edit]Structure and activity[edit]Endoglycosidase H is isolated from Streptomyces plicatus or Streptomyces griseus.Its molecular weight is 29 000 Daltons. The primary structure was described by Robbins et al. in 1984.[7]Endoglycosidase H cleaves the bond in the diacetylchitobiose core of theoligosaccharide between two N-acetylglucosamine (GlcNAc) subunits directly proximal to the asparagine residue, generating a truncated sugar molecule with one N-acetylglucosamine residue remaining on the asparagine.[8]It deglycosylates mannose glycoproteins, but the extent and rate of the deglycosylation depends to a high degree on the nature of the glycoproteins.The deglycosylation rate can be increased by denaturation of the glycoproteins (e.g., by carboxymethylation, sulfitolysis or by heating in the presence of sodium dodecyl sulfate).The addition of 0.1 M 2-mercaptoethanol highly increases enzyme activity against glycoproteins containing inter- or intra-molecular disulfide bridges, unlike detergents like Triton X-100, n-Octylglucoside, or zwitterionic detergents.[9]Biochemical applications[edit]Endoglycosidase H (Endo H) is commonly used by cell biologists to monitor posttranslational modification in the Golgi apparatus.  Most proteins destined for the cell surface are translated by ribosomes into the rough endoplasmic reticulum (ER) and translocated into the Golgi.  Upon entering the ER a molecule containing 14 sugar subunits is linked en bloc to an asparagine in a selective manner by the enzyme oligosaccharyl transferase.  It is this oligosaccharide molecule which is modified by a series of enzymes as the protein moves through the different compartments of the Golgi apparatus.  Endoglycosidase H is able to cleave each structure of this oligosaccharide as it is processed until the enzyme Golgi alpha-mannosidase II removes two mannose subunits.  Since all later oligosaccharide structures are resistant to Endo H cleavage the enzyme is widely used to report the extent of oligosaccharide processing a protein of interest has undergone.[10]References[edit]^ Chien S, Weinburg R, Li S, Li Y (1977). “Endo-\u03b2-N-acetylglucosaminidase from fig latex”. Biochem. Biophys. Res. Commun. 76: 317\u2013323. doi:10.1016\/0006-291x(77)90727-6.^ Koide N, Muramatsu T (August 1974). “Endo-beta-N-acetylglucosaminidase acting on carbohydrate moieties of glycoproteins. Purification and properties of the enzyme from Diplococcus pneumoniae”. The Journal of Biological Chemistry. 249 (15): 4897\u2013904. PMID\u00a04152561.^ Pierce RJ, Spik G, Montreuil J (June 1979). “Cytosolic location of an endo-N-acetyl-beta-D-glucosaminidase activity in rat liver and kidney”. The Biochemical Journal. 180 (3): 673\u201376. doi:10.1042\/bj1800673. PMC\u00a01161109. PMID\u00a0486141.^ Pierce RJ, Spik G, Montreuil J (January 1980). “Demonstration and cytosolic location of an endo-N-acetyl-beta-D-glucosaminidase activity towards an asialo-N-acetyl-lactosaminic-type substrate in rat liver”. The Biochemical Journal. 185 (1): 261\u20134. doi:10.1042\/bj1850261. PMC\u00a01161293. PMID\u00a07378051.^ Tai T, Yamashita K, Ogata-Arakawa M, Koide N, Muramatsu T, Iwashita S, Inoue Y, Kobata A (November 1975). “Structural studies of two ovalbumin glycopeptides in relation to the endo-beta-N-acetylglucosaminidase specificity”. The Journal of Biological Chemistry. 250 (21): 8569\u201375. PMID\u00a0389.^ Tarentino AL, Plummer TH, Maley F (February 1974). “The release of intact oligosaccharides from specific glycoproteins by endo-beta-N-acetylglucosaminidase H”. The Journal of Biological Chemistry. 249 (3): 818\u201324. PMID\u00a04204553.^ Robbins PW, Trimble RB, Wirth DF, Hering C, Maley F, Maley GF, Das R, Gibson BW, Royal N, Biemann K (June 1984). “Primary structure of the Streptomyces enzyme endo-beta-N-acetylglucosaminidase H”. The Journal of Biological Chemistry. 259 (12): 7577\u201383. PMID\u00a06429133.^ Endoglycosidase H, North Star^ Trimble RB, Maley F (September 1984). “Optimizing hydrolysis of N-linked high-mannose oligosaccharides by endo-beta-N-acetylglucosaminidase H”. Analytical Biochemistry. 141 (2): 515\u201322. doi:10.1016\/0003-2697(84)90080-0. PMID\u00a06437277.^ Alberts B (2002). Molecular Biology of the Cell (4th\u00a0ed.). New York: Garland. ISBN\u00a0978-0-8153-4072-0.External links[edit]Close enzymes[edit]Endoglycosidases F and D, cleave Glc-NacPNGase F (Peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine_amidase)  "},{"@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\/endoglycosidase-h-wikipedia\/#breadcrumbitem","name":"Endoglycosidase H – Wikipedia"}}]}]