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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
Baze podataka
IntEnz	IntEnz pregled
BRENDA	BRENDA pristup
ExPASy	NiceZyme pregled
KEGG	KEGG pristup
MetaCyc	metabolički put
PRIAM	profil
Strukture PBP	RCSB PDB PDBe PDBj PDBsum
PMC
Pretraga
PMC	članci
PubMed	članci
NCBI	proteini

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 изд.). USA: Oxford University Press. ISBN 019850229X.
Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 изд.). 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 изд.). Wiley Classics Library. ISBN 0471303097.
William P. Jencks (1987). Catalysis in Chemistry and Enzymology. Dover Publications. ISBN 0486654605.

Spoljašnje veze

Dolichyl-P-Glc:Man9GlcNAc2-PP-dolichol+alpha-1,3-glucosyltransferase на US National Library of Medicine Medical Subject Headings (MeSH)

[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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