Endoglycosidase H

Mannosyl-glycoprotein endo-β-N-acetylglucosaminidase
Identifiers
EC no.3.2.1.96
CAS no.37278-88-9
Alt. namesEndo-β-N-acetylglucosaminidase H, N,N′-diacetylchitobiosyl β-N-acetylglucosaminidase, mannosyl-glycoprotein endo-β-N-acetylglucosamidase, di-N-acetylchitobiosyl β-N-acetylglucosaminidase, endo-β-acetylglucosaminidase, endo-β-(1→4)-N-acetylglucosaminidase, mannosyl-glycoprotein 1,4-N-acetamidodeoxy-β-D-glycohydrolase, endoglycosidase S, endo-N-acetyl-β-D-glucosaminidase, endo-N-acetyl-β-glucosaminidase, endo-β-N-acetylglucosaminidase D, endo-β-N-acetylglucosaminidase F, endo-β-N-acetylglucosaminidase H, endo-β-N-acetylglucosaminidase L, glycopeptide-D-mannosyl-4-N-(N-acetyl-D-glucosaminyl)2-asparagine 1,4-N-acetyl-β-glucosaminohydrolase, endoglycosidase H
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins

The enzyme mannosyl-glycoprotein endo-β-N-acetylglucosaminidase (endoglycosidase H) (EC 3.2.1.96) has systematic name glycopeptide-D-mannosyl-N4-(N-acetyl-D-glucosaminyl)2-asparagine 1,4-N-acetyl-β-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.

  1. ^ Chien S, Weinburg R, Li S, Li Y (1977). "Endo-β-N-acetylglucosaminidase from fig latex". Biochem. Biophys. Res. Commun. 76: 317–323. doi:10.1016/0006-291x(77)90727-6.
  2. ^ Koide N, Muramatsu T (August 1974). "Endo-β-N-acetylglucosaminidase acting on carbohydrate moieties of glycoproteins. Purification and properties of the enzyme from Diplococcus pneumoniae". The Journal of Biological Chemistry. 249 (15): 4897–904. PMID 4152561.
  3. ^ Pierce RJ, Spik G, Montreuil J (June 1979). "Cytosolic location of an endo-N-acetyl-β-D-glucosaminidase activity in rat liver and kidney". The Biochemical Journal. 180 (3): 673–76. doi:10.1042/bj1800673. PMC 1161109. PMID 486141.
  4. ^ Pierce RJ, Spik G, Montreuil J (January 1980). "Demonstration and cytosolic location of an endo-N-acetyl-β-D-glucosaminidase activity towards an asialo-N-acetyl-lactosaminic-type substrate in rat liver". The Biochemical Journal. 185 (1): 261–4. doi:10.1042/bj1850261. PMC 1161293. PMID 7378051.
  5. ^ 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-β-N-acetylglucosaminidase specificity". The Journal of Biological Chemistry. 250 (21): 8569–75. PMID 389.
  6. ^ Tarentino AL, Plummer TH, Maley F (February 1974). "The release of intact oligosaccharides from specific glycoproteins by endo-β-N-acetylglucosaminidase H". The Journal of Biological Chemistry. 249 (3): 818–24. PMID 4204553.