Structural highlights4mqy is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 2.005Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
FunctionLPXC_ECOLI Catalyzes the hydrolysis of UDP-3-O-myristoyl-N-acetylglucosamine to form UDP-3-O-myristoylglucosamine and acetate, the committed step in lipid A biosynthesis.[HAMAP-Rule:MF_00388][1] [2] [3] [4]
See AlsoReferences
- ↑ Jackman JE, Raetz CR, Fierke CA. UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase of Escherichia coli is a zinc metalloenzyme. Biochemistry. 1999 Feb 9;38(6):1902-11. doi: 10.1021/bi982339s. PMID:10026271 doi:http://dx.doi.org/10.1021/bi982339s
- ↑ Young K, Silver LL, Bramhill D, Cameron P, Eveland SS, Raetz CR, Hyland SA, Anderson MS. The envA permeability/cell division gene of Escherichia coli encodes the second enzyme of lipid A biosynthesis. UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase. J Biol Chem. 1995 Dec 22;270(51):30384-91. doi: 10.1074/jbc.270.51.30384. PMID:8530464 doi:http://dx.doi.org/10.1074/jbc.270.51.30384
- ↑ Sorensen PG, Lutkenhaus J, Young K, Eveland SS, Anderson MS, Raetz CR. Regulation of UDP-3-O-[R-3-hydroxymyristoyl]-N-acetylglucosamine deacetylase in Escherichia coli. The second enzymatic step of lipid a biosynthesis. J Biol Chem. 1996 Oct 18;271(42):25898-905. doi: 10.1074/jbc.271.42.25898. PMID:8824222 doi:http://dx.doi.org/10.1074/jbc.271.42.25898
- ↑ Barb AW, Zhou P. Mechanism and inhibition of LpxC: an essential zinc-dependent deacetylase of bacterial lipid A synthesis. Curr Pharm Biotechnol. 2008 Feb;9(1):9-15. PMID:18289052
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