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 (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
⇌ ⇌ -->
{\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
^ 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): 8672–83. doi :10.1021/bi901025v . PMC 2748855 . PMID 19655786 .
^ 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): 4321–6. Bibcode :2007PNAS..104.4321B . doi :10.1073/pnas.0606356104 . PMC 1810333 . PMID 17360522 .
^ Bartling CM, Raetz CR (May 2008). "Steady-state kinetics and mechanism of LpxD, the N-acyltransferase of lipid A biosynthesis" . Biochemistry . 47 (19): 5290–302. doi :10.1021/bi800240r . PMC 2435086 . PMID 18422345 .
^ 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): 19866–74. doi :10.1016/S0021-9258(19)36593-7 . PMID 8366125 .
^ 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): 4549–58. doi :10.1128/jb.00234-08 . PMC 2446808 . PMID 18456814 .
External links
Activity Regulation Classification Kinetics Types