2.3.1.129: acyl-[acyl-carrier-protein]-UDP-N-acetylglucosamine O-acyltransferase
This is an abbreviated version!
For detailed information about acyl-[acyl-carrier-protein]-UDP-N-acetylglucosamine O-acyltransferase, go to the full flat file.
Word Map on EC 2.3.1.129
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2.3.1.129
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udp-glcnac
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lipopolysaccharide
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left-handed
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acyl-acp
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endotoxin
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drug development
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beta-helix
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beta-helical
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homotrimer
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udp-3-o-r-3-hydroxymyristoyl-glcnac
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raetz
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medicine
- 2.3.1.129
- udp-glcnac
- lipopolysaccharide
-
left-handed
- acyl-acp
- endotoxin
- drug development
-
beta-helix
-
beta-helical
-
homotrimer
-
udp-3-o-r-3-hydroxymyristoyl-glcnac
-
raetz
- medicine
Reaction
Synonyms
acyltransferase, uridine diphosphoacetylglucosamine, LiLpxA, LpxA, type II ACP-dependent UDP-N-acetylglucosamine acyltransferase, type II acyl carrier protein-dependent UDP-N-acetylglucosamine acyltransferase, UDP-N-acetylglucosamine 3-O-acyltransferase, UDP-N-acetylglucosamine acyltransferase, uridine diphosphoacetylglucosamine acyltransferase
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General Information
General Information on EC 2.3.1.129 - acyl-[acyl-carrier-protein]-UDP-N-acetylglucosamine O-acyltransferase
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evolution
metabolism
physiological function
additional information
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the enzymes in early lipid A biosynthesis are highly conserved in gram-negative pathogens. LpxA and LpxD are structurally homologous possessing the unique left-handed beta-helix fold, which stems from an extensive hexapeptide repeat motif in their respective primary amino acid sequences
evolution
the overall structure of AtLpxA is very similar to that of Escherichia coli LpxA, EcLpxA, with an alpha-helical-rich C-terminus and characteristic N-terminal left-handed parallel beta-helix. All key catalytic and chain length determining residues of EcLpxA are conserved in AtLpxA,but AtLpxA has an additional coil and loop added to the N-terminal left-handed parallel beta-helix not seen in EcLpxA
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acyltransferases LpxA and LpxD catalyze functionally similar acylations of their respective UDP-glucosamine-based substrates using R-3-hydroxymyristoyl-ACP as the acyl donor in the Kdo2-lipid A biosynthesis in Escherichia coli
metabolism
LpxA catalyzes the first step in lipid A biosynthesis, pathway overview
metabolism
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LpxA is the first enzyme in the biosynthetic pathway for the Lipid A component of the outer membrane lipopolysaccharide
metabolism
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UDP-N-acetylglucosamine acyltransferase, LpxA, catalyzes the first step of lipid A biosynthesis
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acyl-carrier protein (ACP), a small 8-10 kDa component of the type II dissociated fatty acid synthase system, of Vibrio harveyi interacts with LpxA and induces ACP-folding
physiological function
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LpxA catalyzes the condensation of UDP N-acetylglucosamine with R-3-hydroxymyristic acid from R-3-hydroxymyristoyl-acyl carrier protein in the biosynthesis of lipopolysaccharide
physiological function
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UDP-GlcNAc is acylated at the 3-hydroxyl through a thermodynamically unfavorable reaction catalyzed by the type II acyl carrier protein-dependent UDP-N-acetylglucosamine acyltransferase, LpxA, first step in biosynthesis of lipid A and essential for survival among Gram-negative bacteria that synthesize lipopolysaccharide. Lipopolysaccharide contains the glycolipid lipid A, which anchors it to the membrane through fatty acyl chains, a core polysaccharide region, and an O-antigen repeat. Lipid A is an essential moiety necessary for survival of the bacterium and further plays a crucial role in natural antibacterial resistance and bacterial sepsis
physiological function
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enzyme interacts with virulence factor CSK29544_02616, i.e. Labp. Labp increases the enzymatic activity of LpxA without influencing its expression
physiological function
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Francisella novicida LpxA functionally complements an Escherichia coli LpxA knockout mutant and efficiently transfers 3-OH-myristoylate as well as 3-OH-palmitate in Echerichia coli. The acyl chain length of lipid A is determined by several factors including acyl chain selectivity of LpxA and downstream enzymes, as well as the composition of the acyl-ACP pool in vivo
additional information
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UDP-N-acetylglucosamine 3-O-acyltransferase is a protein with a left-handed parallel beta-helix, which is a natural nanotube associated with unusual high stability, molecular dynamics simulations using LpxA crystal structure, PDB ID 1LXA, and formation of a dynamical cross-correlation map, overview. Construction of the unfolding conformational energy landscape identifies the probable intermediates that can appear in the unfolding pathway of the protein, unfolding kinetics of the three-stranded beta-sheet protein, overview