UDP-3-O-(3-hidroksimiristoil)glukozamin N-aciltransferaza
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| UDP-3-O-(3-hidroksimiristoil)glukozamin N-aciltransferaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 2.3.1.191 | ||||||||
| 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-3-O-(3-hidroksimiristoil)glukozamin N-aciltransferaza (EC 2.3.1.191, UDP-3-O-acil-glukozaminska N-aciltransferaza, UDP-3-O-(R-3-hidroksimiristoil)-glukozaminska N-aciltransferaza, aciltransferaza LpxD, acil-ACP:UDP-3-O-(3-hidroksiacil)-GlcN N-aciltransferaza, firA (gen), lpxD (gen)) je enzim sa sistematskim imenom (3R)-3-hidroksimiristoil-(acil-nosilac protein):UDP-3-O-((3R)-3-hidroksimiristoil)-alfa-D-glukozamin N-acetiltransferaza.[1][2][3][4][5] Ovaj enzim katalizuje sledeću hemijsku reakciju
- (3R)-3-hidroksimiristoil-[acil-nosilac protein] + UDP-3-O-[(3R)-3-hidroksimiristoil]-alfa-D-glukozamin UDP-2,3-bis[O-(3R)-3-hidroksimiristoil]-alfa-D-glukozamin + holo-[acil-nosilac protein]
Ovaj enzim katalizuje jedan od koraka biosinteze lipida A.
Reference[uredi | uredi kod]
- ↑ Bartling, C.M. and Raetz, C.R. (2009). „Crystal structure and acyl chain selectivity of Escherichia coli LpxD, the N-acyltransferase of lipid A biosynthesis”. Biochemistry 48: 8672-8683. PMID 19655786.
- ↑ Buetow, L., Smith, T.K., Dawson, A., Fyffe, S. and Hunter, W.N. (2007). „Structure and reactivity of LpxD, the N-acyltransferase of lipid A biosynthesis”. Proc. Natl. Acad. Sci. USA 104: 4321-4326. PMID 17360522.
- ↑ Bartling, C.M. and Raetz, C.R. (2008). „Steady-state kinetics and mechanism of LpxD, the N-acyltransferase of lipid A biosynthesis”. Biochemistry 47: 5290-5302. PMID 18422345.
- ↑ Kelly, T.M., Stachula, S.A., Raetz, C.R. and Anderson, M.S. (1993). „The firA gene of Escherichia coli encodes UDP-3-O-(R-3-hydroxymyristoyl)-glucosamine N-acyltransferase. The third step of endotoxin biosynthesis”. J. Biol. Chem. 268: 19866-19874. PMID 8366125.
- ↑ Bainbridge, B.W., Karimi-Naser, L., Reife, R., Blethen, F., Ernst, R.K. and Darveau, R.P. (2008). „Acyl chain specificity of the acyltransferases LpxA and LpxD and substrate availability contribute to lipid A fatty acid heterogeneity in Porphyromonas gingivalis”. J. Bacteriol. 190: 4549-4558. PMID 18456814.
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.