UDP-3-O-acil-N-acetilglukozaminska deacetilaza
(преусмерено са UDP-3-O-acil-N-acetilglukozamin deacetilaza)
| UDP-3-O-acil-N-acetilglukozaminska deacetilaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 3.5.1.108 | ||||||||
| Baze podataka | |||||||||
| IntEnz | IntEnz pregled | ||||||||
| BRENDA | BRENDA pristup | ||||||||
| ExPASy | NiceZyme pregled | ||||||||
| KEGG | KEGG pristup | ||||||||
| MetaCyc | metabolički put | ||||||||
| PRIAM | profil | ||||||||
| Strukture PBP | 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
[уреди | уреди извор]- ^ 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
[уреди | уреди извор]- Nicholas C. Price; Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third изд.). USA: Oxford University Press. ISBN 019850229X.
- Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 изд.). 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 изд.). Wiley Classics Library. ISBN 0471303097.
Spoljašnje veze
[уреди | уреди извор]- UDP-3-O-acyl-N-acetylglucosamine+deacetylase на US National Library of Medicine Medical Subject Headings (MeSH)
