View source for Biology:UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase

{{Infobox enzyme
| Name       = UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase
| EC_number  = 2.3.1.191
| CAS_number =
| GO_code    = 
| image      = 
| width      = 
| caption    =  
}}
'''UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase''' ({{EC number|2.3.1.191}}, ''UDP-3-O-acyl-glucosamine N-acyltransferase'', ''UDP-3-O-(R-3-hydroxymyristoyl)-glucosamine N-acyltransferase'', ''acyltransferase LpxD'', ''acyl-ACP:UDP-3-O-(3-hydroxyacyl)-GlcN N-acyltransferase'', ''firA (gene)'', ''lpxD (gene)'') is an [[Biology:Enzyme|enzyme]] with [[Biology:List of enzymes|systematic name]] ''(3R)-3-hydroxymyristoyl-(acyl-carrier protein):UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine N-acetyltransferase''.<ref>{{cite journal | vauthors = Bartling CM, Raetz CR | title = Crystal structure and acyl chain selectivity of Escherichia coli LpxD, the N-acyltransferase of lipid A biosynthesis | journal = Biochemistry | volume = 48 | issue = 36 | pages = 8672–83 | date = September 2009 | pmid = 19655786 | pmc = 2748855 | doi = 10.1021/bi901025v }}</ref><ref>{{cite journal | vauthors = Buetow L, Smith TK, Dawson A, Fyffe S, Hunter WN | title = Structure and reactivity of LpxD, the N-acyltransferase of lipid A biosynthesis | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 104 | issue = 11 | pages = 4321–6 | date = March 2007 | pmid = 17360522 | pmc = 1810333 | doi = 10.1073/pnas.0606356104 | bibcode = 2007PNAS..104.4321B | doi-access = free }}</ref><ref>{{cite journal | vauthors = Bartling CM, Raetz CR | title = Steady-state kinetics and mechanism of LpxD, the N-acyltransferase of lipid A biosynthesis | journal = Biochemistry | volume = 47 | issue = 19 | pages = 5290–302 | date = May 2008 | pmid = 18422345 | pmc = 2435086 | doi = 10.1021/bi800240r }}</ref><ref>{{cite journal | vauthors = Kelly TM, Stachula SA, Raetz CR, Anderson MS | title = The firA gene of Escherichia coli encodes UDP-3-O-(R-3-hydroxymyristoyl)-glucosamine N-acyltransferase. The third step of endotoxin biosynthesis | journal = The Journal of Biological Chemistry | volume = 268 | issue = 26 | pages = 19866–74 | date = September 1993 | doi = 10.1016/S0021-9258(19)36593-7 | pmid = 8366125 | doi-access = free }}</ref><ref>{{cite journal | vauthors = Bainbridge BW, Karimi-Naser L, Reife R, Blethen F, Ernst RK, Darveau RP | title = Acyl chain specificity of the acyltransferases LpxA and LpxD and substrate availability contribute to lipid A fatty acid heterogeneity in Porphyromonas gingivalis | journal = Journal of Bacteriology | volume = 190 | issue = 13 | pages = 4549–58 | date = July 2008 | pmid = 18456814 | pmc = 2446808 | doi = 10.1128/jb.00234-08 }}</ref> This enzyme [[Chemistry:Catalysis|catalyses]] the following [[Chemistry:Chemical reaction|chemical reaction]]

: (3R)-3-hydroxymyristoyl-[acyl-carrier protein] + UDP-3-O-[(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine <math>\rightleftharpoons</math> UDP-2,3-bis[O-(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine + holo-[acyl-carrier protein]

The enzyme catalyses a step of [[Biology:Lipid A|lipid A]] biosynthesis.

== References ==
{{reflist}}

== External links ==
* {{MeshName|UDP-3-O-(3-hydroxymyristoyl)glucosamine+N-acyltransferase}}

{{Acyltransferases}}
{{Enzymes}}

[[Category:EC 2.3.1]]

{{Sourceattribution|UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase}}