Dolihil-P-Man:Man7GlcNAc2-PP-dolihol alfa-1,6-manoziltransferaza
Dolihil-P-Man:Man7GlcNAc2-PP-dolihol alfa-1,6-manoziltransferaza | |||||||||
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Identifikatori | |||||||||
EC broj | 2.4.1.260 | ||||||||
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-Man:Man7GlcNAc2-PP-dolihol alfa-1,6-manoziltransferaza (EC 2.4.1.260, ALG12, ALG12 manoziltransferaza, ALG12 alfa1,6manoziltransferaza, dolihil-P-manoza:Man7GlcNAc2-PP-dolihil manoziltransferaza, dolihil-P-Man:Man7GlcNAc2-PP-dolihil alfa6-manoziltransferaza, EBS4, Dol-P-Man:Man7GlcNAc2-PP-Dol alfa-1,6-manoziltransferaza) je enzim sa sistematskim imenom dolihil beta-D-manozil 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->6))-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-difosfodolihol alfa-1,6-manoziltransferaza.[1][2][3][4] Ovaj enzim katalizuje sledeću hemijsku reakciju
- dolihil beta-D-manozil 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->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-difosfodolihol 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->6)]-D-Man-alfa-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-difosfodolihol + dolihil fosfat
Tokom formiranja N-glikozilnih veza glikoproteina dolazi do uređivanja sklopa rasprostanjenih oligosaharida sa Glc3Man9GlcNAc2 osnovom na lipidnom nosiocu dolihil difosfatu.
Reference[uredi | uredi kod]
- ↑ Frank, C.G. and Aebi, M. (2005). „ALG9 mannosyltransferase is involved in two different steps of lipid-linked oligosaccharide biosynthesis”. Glycobiology 15: 1156-1163. PMID 15987956.
- ↑ Hong, Z., Jin, H., Fitchette, A.C., Xia, Y., Monk, A.M., Faye, L. and Li, J. (2009). „Mutations of an α1,6 mannosyltransferase inhibit endoplasmic reticulum-associated degradation of defective brassinosteroid receptors in Arabidopsis”. Plant Cell 21: 3792-3802. PMID 20023196.
- ↑ Cipollo, J.F. and Trimble, R.B. (2002). „The Saccharomyces cerevisiae alg12δ mutant reveals a role for the middle-arm α1,2Man- and upper-arm α1,2Manα1,6Man- residues of Glc3Man9GlcNAc2-PP-Dol in regulating glycoprotein glycan processing in the endoplasmic reticulum and Golgi apparatus”. Glycobiology 12: 749-762. PMID 12460943.
- ↑ Grubenmann, C.E., Frank, C.G., Kjaergaard, S., Berger, E.G., Aebi, M. and Hennet, T. (2002). „ALG12 mannosyltransferase defect in congenital disorder of glycosylation type lg”. Hum. Mol. Genet. 11: 2331-2339. PMID 12217961.
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.
- Gerhard Michal, Dietmar Schomburg (2012). Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology (2nd izd.). Wiley. ISBN 0470146842.