UDP-3-O-acil-N-acetilglukozaminska deacetilaza
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| UDP-3-O-acil-N-acetilglukozaminska deacetilaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 3.5.1.108 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
UDP-3-O-acil-N-acetilglukozaminska deacetilaza (EC 3.5.1.108, LpxC protein, LpxC enzim, LpxC deacetilaza, deacetilaza LpxC, UDP-3-O-acil-GlcNAc deacetilaza, UDP-3-O-((R)-3-hidroksimiristoil)-N-acetilglukozaminska deacetilaza, UDP-(3-O-acil)-N-acetilglukozaminska deacetilaza, UDP-3-O-(R-3-hidroksimiristoil)-N-acetilglukozaminsla deacetilaza, UDP-(3-O-(R-3-hidroksimiristoil))-N-acetilglukozaminsla deacetilaza) je enzim sa sistematskim imenom UDP-3-O-((3R)-3-hidroksimiristoil)-N-acetilglukozamin amidohidrolaza.[1][2][3][4][5][6] Ovaj enzim katalizuje sledeću hemijsku reakciju
- UDP-3-O-[(3R)-3-hidroksimiristoil]-N-acetilglukozamin + H2O UDP-3-O-[(3R)-3-hidroksimiristoil]-D-glukozamin + acetat
Ovaj enzim sadrži cink.
Reference[uredi | uredi kod]
- ↑ Hernick, M., Gennadios, H.A., Whittington, D.A., Rusche, K.M., Christianson, D.W. and Fierke, C.A. (2005). „UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase functions through a general acid-base catalyst pair mechanism”. J. Biol. Chem. 280: 16969-16978. PMID 15705580.
- ↑ Jackman, J.E., Raetz, C.R. and Fierke, C.A. (1999). „UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase of Escherichia coli is a zinc metalloenzyme”. Biochemistry 38: 1902-1911. PMID 10026271.
- ↑ Hyland, S.A., Eveland, S.S. and Anderson, M.S. (1997). „Cloning, expression, and purification of UDP-3-O-acyl-GlcNAc deacetylase from Pseudomonas aeruginosa: a metalloamidase of the lipid A biosynthesis pathway”. J. Bacteriol. 179: 2029-2037. PMID 9068651.
- ↑ Wang, W., Maniar, M., Jain, R., Jacobs, J., Trias, J. and Yuan, Z. (2001). „A fluorescence-based homogeneous assay for measuring activity of UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase”. Anal. Biochem. 290: 338-346. PMID 11237337.
- ↑ Whittington, D.A., Rusche, K.M., Shin, H., Fierke, C.A. and Christianson, D.W. (2003). „Crystal structure of LpxC, a zinc-dependent deacetylase essential for endotoxin biosynthesis”. Proc. Natl. Acad. Sci. USA 100: 8146-8150. PMID 12819349.
- ↑ Mochalkin, I., Knafels, J.D. and Lightle, S. (2008). „Crystal structure of LpxC from Pseudomonas aeruginosa complexed with the potent BB-78485 inhibitor”. Protein Sci. 17: 450-457. PMID 18287278.
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.