Dolihil-P-Glc:Glc1Man9GlcNAc2-PP-dolihol alfa-1,3-glukoziltransferaza
| Dolihil-P-Glc:Glc1Man9GlcNAc2-PP-dolihol alfa-1,3-glukoziltransferaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 2.4.1.265 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
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Dolihil-P-Glc:Glc1Man9GlcNAc2-PP-dolihol alfa-1,3-glukoziltransferaza (EC 2.4.1.265, ALG8, Dol-P-Glc:Glc1Man9GlcNAc2-PP-Dol alfa-1,3-glukoziltransferaza) je enzim sa sistematskim imenom dolihil beta-D-glukozil fosfat: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 alfa-1,3-glukoziltransferaza.[1][2][3] Ovaj enzim katalizuje sledeću hemijsku reakciju
- dolihil beta-D-glukozil fosfat + 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 D-Glc-alfa-(1->3)-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 (dolihil-P-Glc:Man9GlcNAc2-PP-dolihol alfa-1,3-glukoziltransferaza), EC 2.4.1.265 i EC 2.4.1.256 (dolihil-P-Glc:Glc2Man9GlcNAc2-PP-dolihol alfa-1,2-glukoziltransferaza) predstavlja finalni korak formiranja lipid-vezanog oligosaharidnog sklopa.
Reference[uredi | uredi kod]
- ↑ Stagljar, I., te Heesen, S. and Aebi, M. (1994). „New phenotype of mutations deficient in glucosylation of the lipid-linked oligosaccharide: cloning of the ALG8 locus”. Proc. Natl. Acad. Sci. USA 91: 5977-5981. PMID 8016100.
- ↑ Runge, K.W. and Robbins, P.W. (1986). „A new yeast mutation in the glucosylation steps of the asparagine-linked glycosylation pathway. Formation of a novel asparagine-linked oligosaccharide containing two glucose residues”. J. Biol. Chem. 261: 15582-15590. PMID 3536907.
- ↑ Chantret, I., Dancourt, J., Dupre, T., Delenda, C., Bucher, S., Vuillaumier-Barrot, S., Ogier de Baulny, H., Peletan, C., Danos, O., Seta, N., Durand, G., Oriol, R., Codogno, P. and Moore, S.E. (2003). „A deficiency in dolichyl-P-glucose:Glc1Man9GlcNAc2-PP-dolichyl α3-glucosyltransferase defines a new subtype of congenital disorders of glycosylation”. J. Biol. Chem. 278: 9962-9971. PMID 12480927.
Literatura[uredi | uredi kod]
- 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.
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