Dolihil-P-Glc:Man9GlcNAc2-PP-dolihol alfa-1,3-glukoziltransferaza

Dolihil-P-Glc:Man9GlcNAc2-PP-dolihol alfa-1,3-glukoziltransferaza
Identifikatori
EC broj	2.4.1.267
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

Dolihil-P-Glc:Man9GlcNAc2-PP-dolihol alfa-1,3-glukoziltransferaza (EC 2.4.1.267, ALG6, Dol-P-Glc:Man9GlcNAc2-PP-Dol alfa-1,3-glukoziltransferaza) je enzim sa sistematskim imenom dolihil beta-D-glukozil fosfat:D-Man-alfa-(1->2)-D-Man-alfa-(1->2)-D-Man-alfa-(1->3)-(D-Man-alfa-(1->2)-D-Man-alfa-(1->3)-(D-Man-alfa-(1->2)-D-Man-alfa-(1->6))-D-Man-alfa-(1->6))-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-difosfodolihol alfa-1,3-glukoziltransferaza.^[1]^[2]^[3] Ovaj enzim katalizuje sledeću hemijsku reakciju

dolihil beta-D-glukozil fosfat + D-Man-alfa-(1->2)-D-Man-alfa-(1->2)-D-Man-alfa-(1->3)-[D-Man-alfa-(1->2)-D-Man-alfa-(1->3)-[D-Man-alfa-(1->2)-D-Man-alfa-(1->6)]-D-Man-alfa-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-difosfodolihol

\rightleftharpoons

D-Glc-alfa-(1->3)-D-Man-alfa-(1->2)-D-Man-alfa-(1->2)-D-Man-alfa-(1->3)-[D-Man-alfa-(1->2)-D-Man-alfa-(1->3)-[D-Man-alfa-(1->2)-D-Man-alfa-(1->6)]-D-Man-alfa-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-difosfodolihol + dolihil fosfat

Konsekutivna adicija tri glukozna ostatka posredstvom enzima EC 2.4.1.267, EC 2.4.1.265 (Dol-P-Glc:Glc1Man9GlcNAc2-PP-Dol alfa-1,3-glukoziltransferaza) i EC 2.4.1.256 (Dol-P-Glc:Glc2Man9GlcNAc2-PP-Dol alfa-1,2-glukoziltransferaza) predstavlja finalni korak formiranja lipid-vezanog oligosaharidnog sklopa.

Reference

↑ Reiss, G., te Heesen, S., Zimmerman, J., Robbins, P.W. and Aebi, M. (1996). „Isolation of the ALG6 locus of Saccharomyces cerevisiae required for glucosylation in the N-linked glycosylation pathway”. Glycobiology 6: 493-498. PMID 8877369.
↑ Runge, K.W., Huffaker, T.C. and Robbins, P.W. (1984). „Two yeast mutations in glucosylation steps of the asparagine glycosylation pathway”. J. Biol. Chem. 259: 412-417. PMID 6423630.
↑ Westphal, V., Xiao, M., Kwok, P.Y. and Freeze, H.H. (2003). „Identification of a frequent variant in ALG6, the cause of congenital disorder of glycosylation-Ic”. Hum. Mutat. 22: 420-421. PMID 14517965.

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 Dolichyl-P-Glc:Man9GlcNAc2-PP-dolichol+alpha-1,3-glucosyltransferase

[1] Reiss, G., te Heesen, S., Zimmerman, J., Robbins, P.W. and Aebi, M. (1996). „Isolation of the ALG6 locus of Saccharomyces cerevisiae required for glucosylation in the N-linked glycosylation pathway”. Glycobiology 6: 493-498. PMID 8877369.

[2] Runge, K.W., Huffaker, T.C. and Robbins, P.W. (1984). „Two yeast mutations in glucosylation steps of the asparagine glycosylation pathway”. J. Biol. Chem. 259: 412-417. PMID 6423630.

[3] Westphal, V., Xiao, M., Kwok, P.Y. and Freeze, H.H. (2003). „Identification of a frequent variant in ALG6, the cause of congenital disorder of glycosylation-Ic”. Hum. Mutat. 22: 420-421. PMID 14517965.

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