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 | ||||||||
| |||||||||
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 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.
- ↑ 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.
- 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.