UDP-N-acetilglukozamin—lizozomalni-enzim N-acetilglukozaminfosfotransferaza
UDP-N-acetilglukozamin—lizozomalni-enzim N-acetilglukozaminfosfotransferaza | |||||||||
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Identifikatori | |||||||||
EC broj | 2.7.8.17 | ||||||||
CAS broj | 84012-69-1 | ||||||||
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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UDP-N-acetilglukozamin—lizozomalni-enzim N-acetilglukozaminfosfotransferaza (EC 2.7.8.17, N-acetilglukozaminilfosfotransferaza, UDP-N-acetilglukozamin:lizozomalni enzim N-acetilglukozamin-1-fosfotransferaza, UDP-GlcNAc:glikoprotein N-acetilglukozamin-1-fosfotransferaza, uridin difosfoacetilglukozamin-lizozomalni enzim prekurzor acetilglukozamin-1-fosfotransferaza, uridin difosfoacetilglukozamin-glikoprotein acetilglukozamin-1-fosfotransferaza, lizozomalni enzim prekurzor acetilglukozamin-1-fosfotransferaza, N-acetilglukozaminilna fosfotransferaza, UDP-acetilglukozamin:lizozomalni enzim N-acetilglukozamin-1-fosfotransferaza, UDP-GlcNAc:lizozomalni enzim N-acetilglukozamin-1-fosfotransferaza, UDP-N-acetilglukozamin:glikoprotein N-acetilglukozamin-1-fosfotransferaza, UDP-N-acetilglukozamin:glikoprotein N-acetilglukozaminil-1-fosfotransferaza) je enzim sa sistematskim imenom UDP-N-acetil-D-glukozamin:lizozomalni-enzim N-acetilglukozaminfosfotransferaza.[1][2][3][4] Ovaj enzim katalizuje sledeću hemijsku reakciju
- UDP-N-acetil-D-glukozamin + lizozomalni-enzim D-manoza UMP + lizozomalni-enzim N-acetil-D-glukozaminil-fosfo-D-manoza
Neki drugi glikoproteini sa visokim sadržajem manoze mogu da budu akceptori.
Reference[uredi | uredi kod]
- ↑ Reitman, M.L. and Kornfeld, S. (1981). „UDP-N-acetylglucosamine:glycoprotein N-acetylglucosamine-1-phosphotransferase. Proposed enzyme for the phosphorylation of the high mannose oligosaccharide units of lysosomal enzymes”. J. Biol. Chem. 256: 4275-4281. PMID 6452459.
- ↑ Reitman, M.L. and Kornfeld, S. (1981). „Lysosomal enzyme targeting. N-Acetylglucosaminylphosphotransferase selectively phosphorylates native lysosomal enzymes”. J. Biol. Chem. 256: 11977-11980. PMID 6457829.
- ↑ Waheed, A., Hasilik, A. and von Figura, K. (1982). „UDP-N-acetylglucosamine:lysosomal enzyme precursor N-acetylglucosamine-1-phosphotransferase. Partial purification and characterization of the rat liver Golgi enzyme”. J. Biol. Chem. 257: 12322-12331. PMID 6288715.
- ↑ Waheed, A., Pohlmann, R., Hasilik, A. and von Figura, K. (1981). „Subcellular location of two enzymes involved in the synthesis of phosphorylated recognition markers in lysosomal enzymes”. J. Biol. Chem. 256: 4150-4152. PMID 6260788.
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.