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discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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MetaCyc Reaction: 3.2.1.96

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions
Reactions Classified By Substrate Small-Molecule Reactions

EC Number: 3.2.1.96

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

Mass balance status: Undetermined; a substrate lacks a chemical formula

Enzyme Commission Primary Name: mannosyl-glycoprotein endo-β-N-acetylglucosaminidase

Enzyme Commission Synonyms: N,N'-diacetylchitobiosyl β-N-acetylglucosaminidase, endo-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

Enzyme Commission Summary:
This enzyme catalyzes endohydrolysis of the N,N'-diacetylchitobiosyl unit in high-mannose glycopeptides and glycoproteins containing the -[Man(GlcNAc)2]Asn- structure. One N-acetyl-D-glucosamine residue remains attached to the protein; the rest of the oligosaccharide is released intact.

A group of related enzymes.

Citations: [Koide74, Pierce79, Pierce80, Tai75, Tarentino74, Chien77]

Relationship Links: BRENDA:EC:3.2.1.96 , ENZYME:EC:3.2.1.96 , IUBMB-ExplorEnz:EC:3.2.1.96 , UniProt:RELATED-TO:P04067 , UniProt:RELATED-TO:P13670 , UniProt:RELATED-TO:P49610 , UniProt:RELATED-TO:Q9CFI4 , UniProt:RELATED-TO:Q9R5G5


References

Chien77: Chien, S., Weinburg, R., Li, S., Li, Y. (1977). "Endo-beta-N-acetylglucosaminidase from fig latex." Biochem. Biophys. Res. Commun.

Koide74: Koide N, Muramatsu T (1974). "Endo-beta-N-acetylglucosaminidase acting on carbohydrate moieties of glycoproteins. Purification and properties of the enzyme from Diplococcus pneumoniae." J Biol Chem 249(15);4897-904. PMID: 4152561

Pierce79: Pierce RJ, Spik G, Montreuil J (1979). "Cytosolic location of an endo-N-acetyl-beta-D-glucosaminidase activity in rat liver and kidney." Biochem J 180(3);673-76. PMID: 486141

Pierce80: Pierce RJ, Spik G, Montreuil J (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." Biochem J 185(1);261-4. PMID: 7378051

Tai75: Tai T, Yamashita K, Ogata-Arakawa M, Koide N, Muramatsu T, Iwashita S, Inoue Y, Kobata A (1975). "Structural studies of two ovalbumin glycopeptides in relation to the endo-beta-N-acetylglucosaminidase specificity." J Biol Chem 250(21);8569-75. PMID: 389

Tarentino74: Tarentino AL, Plummer TH, Maley F (1974). "The release of intact oligosaccharides from specific glycoproteins by endo-beta-N-acetylglucosaminidase H." J Biol Chem 249(3);818-24. PMID: 4204553


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Fri Dec 19, 2014, biocyc14.