[{"@context":"http:\/\/schema.org\/","@type":"BlogPosting","@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/udp-3-o-3-hydroxymyristoylglucosamine-n-acyltransferase-wikipedia\/#BlogPosting","mainEntityOfPage":"https:\/\/wiki.edu.vn\/en\/wiki24\/udp-3-o-3-hydroxymyristoylglucosamine-n-acyltransferase-wikipedia\/","headline":"UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase – Wikipedia","name":"UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase – Wikipedia","description":"before-content-x4 From Wikipedia, the free encyclopedia after-content-x4 UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase (EC 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","datePublished":"2022-04-21","dateModified":"2022-04-21","author":{"@type":"Person","@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/author\/lordneo\/#Person","name":"lordneo","url":"https:\/\/wiki.edu.vn\/en\/wiki24\/author\/lordneo\/","image":{"@type":"ImageObject","@id":"https:\/\/secure.gravatar.com\/avatar\/c9645c498c9701c88b89b8537773dd7c?s=96&d=mm&r=g","url":"https:\/\/secure.gravatar.com\/avatar\/c9645c498c9701c88b89b8537773dd7c?s=96&d=mm&r=g","height":96,"width":96}},"publisher":{"@type":"Organization","name":"Enzyklop\u00e4die","logo":{"@type":"ImageObject","@id":"https:\/\/wiki.edu.vn\/wiki4\/wp-content\/uploads\/2023\/08\/download.jpg","url":"https:\/\/wiki.edu.vn\/wiki4\/wp-content\/uploads\/2023\/08\/download.jpg","width":600,"height":60}},"image":{"@type":"ImageObject","@id":"https:\/\/wikimedia.org\/api\/rest_v1\/media\/math\/render\/svg\/1c37b981df851b9e54e489e017b1481e37d418f3","url":"https:\/\/wikimedia.org\/api\/rest_v1\/media\/math\/render\/svg\/1c37b981df851b9e54e489e017b1481e37d418f3","height":"","width":""},"url":"https:\/\/wiki.edu.vn\/en\/wiki24\/udp-3-o-3-hydroxymyristoylglucosamine-n-acyltransferase-wikipedia\/","about":["Wiki"],"wordCount":2933,"articleBody":"     (adsbygoogle = window.adsbygoogle || []).push({});before-content-x4From Wikipedia, the free encyclopedia       (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase (EC 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 enzyme with systematic name (3R)-3-hydroxymyristoyl-(acyl-carrier protein):UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine N-acetyltransferase.[1][2][3][4][5] This enzyme catalyses the following chemical reaction(3R)-3-hydroxymyristoyl-[acyl-carrier protein] + UDP-3-O-[(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine        (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4\u21cc{displaystyle rightleftharpoons } UDP-2,3-bis[O-(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine + holo-[acyl-carrier protein]The enzyme catalyses a step of lipid A biosynthesis.References[edit]^ Bartling CM, Raetz CR (September 2009). “Crystal structure and acyl chain selectivity of Escherichia coli LpxD, the N-acyltransferase of lipid A biosynthesis”. Biochemistry. 48 (36): 8672\u201383. doi:10.1021\/bi901025v. PMC\u00a02748855. PMID\u00a019655786.^ Buetow L, Smith TK, Dawson A, Fyffe S, Hunter WN (March 2007). “Structure and reactivity of LpxD, the N-acyltransferase of lipid A biosynthesis”. Proceedings of the National Academy of Sciences of the United States of America. 104 (11): 4321\u20136. Bibcode:2007PNAS..104.4321B. doi:10.1073\/pnas.0606356104. PMC\u00a01810333. PMID\u00a017360522.^ Bartling CM, Raetz CR (May 2008). “Steady-state kinetics and mechanism of LpxD, the N-acyltransferase of lipid A biosynthesis”. Biochemistry. 47 (19): 5290\u2013302. doi:10.1021\/bi800240r. PMC\u00a02435086. PMID\u00a018422345.^ Kelly TM, Stachula SA, Raetz CR, Anderson MS (September 1993). “The firA gene of Escherichia coli encodes UDP-3-O-(R-3-hydroxymyristoyl)-glucosamine N-acyltransferase. The third step of endotoxin biosynthesis”. The Journal of Biological Chemistry. 268 (26): 19866\u201374. doi:10.1016\/S0021-9258(19)36593-7. PMID\u00a08366125.^ Bainbridge BW, Karimi-Naser L, Reife R, Blethen F, Ernst RK, Darveau RP (July 2008). “Acyl chain specificity of the acyltransferases LpxA and LpxD and substrate availability contribute to lipid A fatty acid heterogeneity in Porphyromonas gingivalis”. Journal of Bacteriology. 190 (13): 4549\u201358. doi:10.1128\/jb.00234-08. PMC\u00a02446808. 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