View source for Biology:UDP-3-O-acyl-N-acetylglucosamine deacetylase

{{Infobox enzyme
| Name       = UDP-3-O-acyl-N-acetylglucosamine deacetylase
| EC_number  = 3.5.1.108
| CAS_number =
| GO_code    = 
| image      = 
| width      = 
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}}
'''UDP-3-O-acyl-N-acetylglucosamine deacetylase''' ({{EC number|3.5.1.108}}, ''LpxC protein'', ''LpxC enzyme'', ''LpxC deacetylase'', ''deacetylase LpxC'', ''UDP-3-O-acyl-GlcNAc deacetylase'', ''UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase'', ''UDP-(3-O-acyl)-N-acetylglucosamine deacetylase'', ''UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase'', ''UDP-(3-O-(R-3-hydroxymyristoyl))-N-acetylglucosamine deacetylase'') is an [[Biology:Enzyme|enzyme]] with [[Biology:List of enzymes|systematic name]] ''UDP-3-O-((3R)-3-hydroxymyristoyl)-N-acetylglucosamine amidohydrolase''.<ref>{{cite journal | vauthors = Hernick M, Gennadios HA, Whittington DA, Rusche KM, Christianson DW, Fierke CA |author5-link=David W. Christianson| title = UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase functions through a general acid-base catalyst pair mechanism | journal = The Journal of Biological Chemistry | volume = 280 | issue = 17 | pages = 16969–78 | date = April 2005 | pmid = 15705580 | doi = 10.1074/jbc.M413560200 | doi-access = free }}</ref><ref>{{cite journal | vauthors = Jackman JE, Raetz CR, Fierke CA | title = UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase of Escherichia coli is a zinc metalloenzyme | journal = Biochemistry | volume = 38 | issue = 6 | pages = 1902–11 | date = February 1999 | pmid = 10026271 | doi = 10.1021/bi982339s }}</ref><ref>{{cite journal | vauthors = Hyland SA, Eveland SS, Anderson MS | title = Cloning, expression, and purification of UDP-3-O-acyl-GlcNAc deacetylase from Pseudomonas aeruginosa: a metalloamidase of the lipid A biosynthesis pathway | journal = Journal of Bacteriology | volume = 179 | issue = 6 | pages = 2029–37 | date = March 1997 | pmid = 9068651 | pmc = 178929 | doi = 10.1128/jb.179.6.2029-2037.1997 }}</ref><ref>{{cite journal | vauthors = Wang W, Maniar M, Jain R, Jacobs J, Trias J, Yuan Z | title = A fluorescence-based homogeneous assay for measuring activity of UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase | journal = Analytical Biochemistry | volume = 290 | issue = 2 | pages = 338–46 | date = March 2001 | pmid = 11237337 | doi = 10.1006/abio.2000.4973 }}</ref><ref>{{cite journal | vauthors = Whittington DA, Rusche KM, Shin H, Fierke CA, Christianson DW | title = Crystal structure of LpxC, a zinc-dependent deacetylase essential for endotoxin biosynthesis | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 100 | issue = 14 | pages = 8146–50 | date = July 2003 | pmid = 12819349 | pmc = 166197 | doi = 10.1073/pnas.1432990100 | bibcode = 2003PNAS..100.8146W | doi-access = free }}</ref><ref>{{cite journal | vauthors = Mochalkin I, Knafels JD, Lightle S | title = Crystal structure of LpxC from Pseudomonas aeruginosa complexed with the potent BB-78485 inhibitor | journal = Protein Science | volume = 17 | issue = 3 | pages = 450–7 | date = March 2008 | pmid = 18287278 | pmc = 2248309 | doi = 10.1110/ps.073324108 }}</ref> This enzyme [[Chemistry:Catalysis|catalyses]] the following [[Chemistry:Chemical reaction|chemical reaction]]

: UDP-3-O-[(3R)-3-hydroxymyristoyl]-N-acetylglucosamine + H<sub>2</sub>O <math>\rightleftharpoons</math> UDP-3-O-[(3R)-3-hydroxymyristoyl]-D-glucosamine + [[Chemistry:Acetate|acetate]]

This zinc protein participates in biosynthesis of [[Biology:Lipid A|lipid A]].

== References ==
{{reflist}}

== External links ==
* {{MeshName|UDP-3-O-acyl-N-acetylglucosamine+deacetylase}}

{{Carbon-nitrogen non-peptide hydrolases}}
{{Enzymes}}

[[Category:EC 3.5.1]]

{{Sourceattribution|UDP-3-O-acyl-N-acetylglucosamine deacetylase}}