Glikolipid 2-a-manoziltransferaza
Glikolipid 2-a-manoziltransferaza (EC 2.4.1.131, ALG11, ALG11 manoziltransferaza, LEW3 (gen), At2G40190 (gen), gmd3 (gen), protein galaktomananske deficijencije 3, GDP-manoza:glikolipid 1,2-alfa-D-manoziltransferaza, glikolipid 2-alfa-manoziltransferaza, GDP-manoza:glikolipid 2-alfa-D-manoziltransferaza, GDP-Man:Man3GlcNAc2-PP-Dol alfa-1,2-manoziltransferaza) je enzim sa sistematskim imenom GDP-alfa-D-manoza:D-Man-alfa-(1->3)-(D-Man-alfa-(1->6))-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-difosfodolihol 2-alfa-D-manoziltransferaza.[1][2][3] Ovaj enzim katalizuje sledeću hemijsku reakciju
| Glikolipid 2-a-manoziltransferaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 2.4.1.131 | ||||||||
| CAS broj | 74506-43-7 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
- 2 GDP-alfa-D-manoza + D-MaN-alfa-(1->3)-[D-MaN-alfa-(1->6)]-D-MaN-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-difosfodolihol 2 GDP + D-MaN-alfa-(1->2)-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
Pri biosintezi za asparagin vezanih glikoproteina (N-vezanoj proteinskoj glikozilaciji) se koristi za dolihil difosfat vezani glikozilni donor. Njega formira serija za membranu vezanih glikoziltransferaza.
Reference
uredi- ↑ O'Reilly, M.K., Zhang, G. and Imperiali, B. (2006). „In vitro evidence for the dual function of Alg2 and Alg11: essential mannosyltransferases in N-linked glycoprotein biosynthesis”. Biochemistry 45: 9593-9603. PMID 16878994.
- ↑ Absmanner, B., Schmeiser, V., Kampf, M. and Lehle, L. (2010). „Biochemical characterization, membrane association and identification of amino acids essential for the function of Alg11 from Saccharomyces cerevisiae, an α1,2-mannosyltransferase catalysing two sequential glycosylation steps in the formation of the lipid-linked core oligosaccharide”. Biochem. J. 426: 205-217. PMID 19929855.
- ↑ Schutzbach, J.S., Springfield, J.D. and Jensen, J.W. (1980). „The biosynthesis of oligosaccharide-lipids. Formation of an α-1,2-mannosyl-mannose linkage”. J. Biol. Chem. 255: 4170-4175. PMID 6154707.
Literatura
uredi- 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.