| Entry |
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| Name |
UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase;
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 name);
lpxD (gene name);
(3R)-3-hydroxymyristoyl-[acyl-carrier protein]:UDP-3-O-[(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine N-acetyltransferase
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| Class |
Transferases;
Acyltransferases;
Transferring groups other than aminoacyl groups
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| Sysname |
(3R)-3-hydroxytetradecanoyl-[acyl-carrier protein]:UDP-3-O-[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosamine N-acetyltransferase
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| Reaction(IUBMB) |
(3R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-3-O-[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosamine = UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosamine + a holo-[acyl-carrier protein] [RN: R04550]
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| Reaction(KEGG) |
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| Substrate |
(3R)-3-hydroxytetradecanoyl-[acyl-carrier protein] [CPD: C04688];
UDP-3-O-[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosamine
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| Product |
UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosamine;
holo-[acyl-carrier protein] [CPD: C00229]
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| Comment |
The enzyme catalyses a step of lipid A biosynthesis. LpxD from Escherichia prefers (R,S)-3-hydroxytetradecanoyl-[acyl-carrier protein] over (R,S)-3-hydroxyhexadecanoyl-[acyl-carrier protein] [1]. Escherichia coli lipid A acyltransferases do not have an absolute specificity for 14-carbon hydroxy fatty acids but can transfer fatty acids differing by one carbon unit if the fatty acid substrates are available. When grown on 1% propionic acid, lipid A also contains the odd-chain fatty acids tridecanoic acid, pentadecanoic acid, hydroxytridecanoic acid, and hydroxypentadecanoic acid [5].
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| History |
EC 2.3.1.191 created 2010
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| Pathway |
| ec00540 | Lipopolysaccharide biosynthesis |
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| Orthology |
| K02536 | UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase |
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| Genes |
» show all
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| Reference |
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| Authors |
Bartling CM, Raetz CR |
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| Title |
Crystal structure and acyl chain selectivity of Escherichia coli LpxD, the N-acyltransferase of lipid A biosynthesis. |
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| Journal |
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| Sequence |
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| Reference |
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| Authors |
Buetow L, Smith TK, Dawson A, Fyffe S, Hunter WN |
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| Title |
Structure and reactivity of LpxD, the N-acyltransferase of lipid A biosynthesis. |
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| Journal |
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| Sequence |
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| Reference |
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| Authors |
Bartling CM, Raetz CR |
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| Title |
Steady-state kinetics and mechanism of LpxD, the N-acyltransferase of lipid A biosynthesis. |
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| Journal |
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| Sequence |
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| Reference |
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| Authors |
Kelly TM, Stachula SA, Raetz CR, Anderson MS |
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| Title |
The firA gene of Escherichia coli encodes UDP-3-O-(R-3-hydroxymyristoyl)-glucosamine N-acyltransferase. The third step of endotoxin biosynthesis. |
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| Journal |
J Biol Chem 268:19866-74 (1993) |
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| Sequence |
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| Reference |
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| Authors |
Bainbridge BW, Karimi-Naser L, Reife R, Blethen F, Ernst RK, Darveau RP |
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| Title |
Acyl chain specificity of the acyltransferases LpxA and LpxD and substrate availability contribute to lipid A fatty acid heterogeneity in Porphyromonas gingivalis. |
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| Journal |
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| Other DBs |
| ExPASy - ENZYME nomenclature database: | 2.3.1.191 |
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| LinkDB |
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