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Manozil-glikoprotein endo-beta-N-acetilglukozaminidaza
Identifikatori
EC broj	3.2.1.96
CAS broj	37278-88-9
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB	RCSB PDB PDBe PDBj PDBsum
Pretraga
PMC	articles
PubMed	articles
NCBI Protein	search

Manozil-glikoprotein endo-beta-N-acetilglukozaminidaza (EC 3.2.1.96, N,N'-diacetilhitobiozil beta-N-acetilglukozaminidaza, endo-beta-N-acetilglukozaminidaza, manozil-glikoprotein endo-beta-N-acetilglukozamidaza, di-N-acetilhitobiozil beta-N-acetilglukozaminidaza, endo-beta-acetilglukozaminidaza, endo-beta-(1->4)-N-acetilglukozaminidaza, manozil-glikoprotein 1,4-N-acetamidodezoksi-beta-D-glikohidrolaza, endoglikozidaza S, endo-N-acetil-beta-D-glukozaminidaza, endo-N-acetil-beta-glukozaminidaza, endo-beta-N-acetilglukozaminidaza D, endo-beta-N-acetilglukozaminidaza F, endo-beta-N-acetilglukozaminidaza H, endo-beta-N-acetilglukozaminidaza L, glikopeptid-D-manozil-4-N-(N-acetil-D-glukozaminil)2-asparagin 1,4-N-acetil-beta-glukozaminohidrolaza, endoglikozidaza H) je enzim sa sistematskim imenom glikopeptid-D-manozil-N4-(N-acetil-D-glukozaminil)2-asparagin 1,4-N-acetil-beta-glukosaminohidrolaza.^[1]^[2]^[3]^[4]^[5]^[6] Ovaj enzim katalizuje sledeću hemijsku reakciju

Endohidroliza N,N'-diacetilhitobiozilnih jedinica u visoko-manoznim glikopeptidima i glikoproteinima koji sadrže -[Man(GlcNAc)2]AsN- strukturu. Jedan N-acetil-D-glukozaminski ostatak ostaje vezan za protein; ostatak oligosaharids se odvaja napromenjen

Reference

↑ Chien, S., Weinburg, R., Li, S. and Li, Y. (1977). „Endo-β-N-acetylglucosaminidase from fig latex”. Biochem. Biophys. Res. Commun. 76: 317-323.
↑ Koide, N. and Muramatsu, T. (1974). „Endo-β-N-acetylglucosaminidase acting on carbohydrate moieties of glycoproteins. Purification and properties of the enzyme from Diplococcus pneumoniae”. J. Biol. Chem. 249: 4897-4904. PMID 4152561.
↑ Pierce, R.J., Spik, G. and Montreuil, J. (1979). „Cytosolic location of an endo-N-acetyl-β-D-glucosaminidase activity in rat liver and kidney”. Biochem. J. 180: 673-673. PMID 486141.
↑ Pierce, R.J., Spik, G. and Montreuil, J. (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”. Biochem. J. 185: 261-264. PMID 7378051.
↑ Tai, T., Yamashita, K., Ogata-Arakawa, M., Koide, N., Muramatsu, T., Iwashita, S., Inoue, Y. and Kobata, A. (1975). „Structural studies of two ovalbumin glycopeptides in relation to the endo-β-N-acetylglucosaminidase specificity”. J. Biol. Chem. 250: 8569-8575. PMID 389.
↑ Tarentino, A.L., Plummer, T.H., Jr. and Maley, F. (1974). „The release of intact oligosaccharides from specific glycoproteins by endo-β-N-acetylglucosaminidase H”. J. Biol. Chem. 249: 818-824. PMID 4204553.

Literatura

Nicholas C. Price, Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third izd.). USA: Oxford University Press. ISBN 019850229X.
Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 izd.). Wiley-Interscience. ISBN 0471205036.
Branden C, Tooze J.. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN: 0-8153-2305-0.
Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 izd.). Wiley Classics Library. ISBN 0471303097.
Robert A. Copeland (2013). Evaluation of Enzyme Inhibitors in Drug Discovery: A Guide for Medicinal Chemists and Pharmacologists (2nd izd.). Wiley-Interscience. ISBN 111848813X.
Gerhard Michal, Dietmar Schomburg (2012). Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology (2nd izd.). Wiley. ISBN 0470146842.

Vanjske veze

MeSH Mannosyl-glycoprotein+endo-beta-N-acetylglucosaminidase

[1] Chien, S., Weinburg, R., Li, S. and Li, Y. (1977). „Endo-β-N-acetylglucosaminidase from fig latex”. Biochem. Biophys. Res. Commun. 76: 317-323.

[2] Koide, N. and Muramatsu, T. (1974). „Endo-β-N-acetylglucosaminidase acting on carbohydrate moieties of glycoproteins. Purification and properties of the enzyme from Diplococcus pneumoniae”. J. Biol. Chem. 249: 4897-4904. PMID 4152561.

[3] Pierce, R.J., Spik, G. and Montreuil, J. (1979). „Cytosolic location of an endo-N-acetyl-β-D-glucosaminidase activity in rat liver and kidney”. Biochem. J. 180: 673-673. PMID 486141.

[4] Pierce, R.J., Spik, G. and Montreuil, J. (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”. Biochem. J. 185: 261-264. PMID 7378051.

[5] Tai, T., Yamashita, K., Ogata-Arakawa, M., Koide, N., Muramatsu, T., Iwashita, S., Inoue, Y. and Kobata, A. (1975). „Structural studies of two ovalbumin glycopeptides in relation to the endo-β-N-acetylglucosaminidase specificity”. J. Biol. Chem. 250: 8569-8575. PMID 389.

[6] Tarentino, A.L., Plummer, T.H., Jr. and Maley, F. (1974). „The release of intact oligosaccharides from specific glycoproteins by endo-β-N-acetylglucosaminidase H”. J. Biol. Chem. 249: 818-824. PMID 4204553.

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