Information on EC 2.3.1.129 - acyl-[acyl-carrier-protein]-UDP-N-acetylglucosamine O-acyltransferase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY
2.3.1.129
-
RECOMMENDED NAME
GeneOntology No.
acyl-[acyl-carrier-protein]-UDP-N-acetylglucosamine O-acyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
(R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetyl-alpha-D-glucosamine = an [acyl-carrier protein] + UDP-3-O-[(3R)-3-hydroxytetradecanoyl]-N-acetyl-alpha-D-glucosamine
show the reaction diagram
-
-
-
-
(R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetyl-alpha-D-glucosamine = an [acyl-carrier protein] + UDP-3-O-[(3R)-3-hydroxytetradecanoyl]-N-acetyl-alpha-D-glucosamine
show the reaction diagram
mechanism involving essential His125
-
(R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetyl-alpha-D-glucosamine = an [acyl-carrier protein] + UDP-3-O-[(3R)-3-hydroxytetradecanoyl]-N-acetyl-alpha-D-glucosamine
show the reaction diagram
reaction mechanism, acylation occurs via nucleophilic attack of deprotonated UDP-GlcNAc on the acyl donor in a general base-catalyzed mechanism involving a catalytic dyad of His125 and Asp126, His125, the general base, interacts with the 3'-hydroxyl group of UDP-GlcNAc to generate the nucleophile, the Asp126 side-chain accepts a hydrogen bond from His125 and helps orientate the general base to participate in catalysis; reaction mechanism, acylation occurs via nucleophilic attack of deprotonated UDP-GlcNAc on the acyl donor in a general base-catalyzed mechanism involving a catalytic dyad of His125 and Asp126, His125, the general base, interacts with the 3'-hydroxyl group of UDP-GlcNAc to generate the nucleophile, the Asp126 side-chain accepts a hydrogen bond from His125 and helps orient the general base to participate in catalysis
P0A722
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Acyl group transfer
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
lipid IVA biosynthesis
-
Lipopolysaccharide biosynthesis
-
Metabolic pathways
-
SYSTEMATIC NAME
IUBMB Comments
(R)-3-hydroxytetradecanoyl-[acyl-carrier protein]:UDP-N-acetylglucosamine 3-O-(3-hydroxytetradecanoyl)transferase
Involved with EC 2.4.1.182 (lipid-A-disaccharide synthase) and EC 2.7.1.130 (tetraacyldisaccharide 4'-kinase) in the biosynthesis of the phosphorylated glycolipid, Lipid A, in the outer membrane of Escherichia coli.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
acyltransferase, uridine diphosphoacetylglucosamine
-
-
-
-
LiLpxA
Q8EZA6
-
LpxA
Q3BDJ0
-
-
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
-
-
-
-
UDP-N-acetylglucosamine acyltransferase
Q9SU91
-
UDP-N-acetylglucosamine acyltransferase
-
-
UDP-N-acetylglucosamine acyltransferase
-
-
UDP-N-acetylglucosamine acyltransferase
Q3BDJ0
-
UDP-N-acetylglucosamine acyltransferase
Q3BDJ0
-
-
UDP-N-acetylglucosamine acyltransferase
-
-
uridine diphosphoacetylglucosamine acyltransferase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
105843-69-4
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
gene lpxA, isozymes LpxA1 and LpxA2
UniProt
Manually annotated by BRENDA team
; gene lpxA
Uniprot
Manually annotated by BRENDA team
gene lpxA
Uniprot
Manually annotated by BRENDA team
K12 wild-type; MC1061/pSR1 (overproducing strain harbouring plasmid pSR1); strains JB1104; W3106
-
-
Manually annotated by BRENDA team
K12 wild-type; R477, R477/pTIH1, MI6383; strains JB1104
-
-
Manually annotated by BRENDA team
MC1061/pSR1 (overproducing strain harbouring plasmid pSR1)
-
-
Manually annotated by BRENDA team
SM 101, SM 108; SM105
-
-
Manually annotated by BRENDA team
SM105; strains JB1104
-
-
Manually annotated by BRENDA team
strain MG1655, gene lpxA
-
-
Manually annotated by BRENDA team
Escherichia coli SM105
SM105
-
-
Manually annotated by BRENDA team
Escherichia coli strains JB1104
strains JB1104
-
-
Manually annotated by BRENDA team
Escherichia coli W3106
W3106
-
-
Manually annotated by BRENDA team
strain O35E, gene lpxA
SwissProt
Manually annotated by BRENDA team
strain O35E, gene lpxA
SwissProt
Manually annotated by BRENDA team
gene lpxA
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
evolution
-
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
-, Q9SU91
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
metabolism
-
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
-
UDP-N-acetylglucosamine acyltransferase, LpxA, catalyzes the first step of lipid A biosynthesis
metabolism
-
LpxA is the first enzyme in the biosynthetic pathway for the Lipid A component of the outer membrane lipopolysaccharide
physiological function
-
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
-
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
-
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
metabolism
Q9SU91
LpxA catalyzes the first step in lipid A biosynthesis, pathway overview
additional information
-, Q9SU91
active site structure of AtLpxA, overview
additional information
-
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
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(3R)-3-hydroxylauroyl-methylphosphopantetheine + UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucopyranose
methylphosphopantetheine + UDP-3-N-((3R)-3-hydroxylauroyl)-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucopyranose
show the reaction diagram
-, Q8EZA6
synthetic (3R)-3-hydroxylauroyl-methylphosphopantetheine is an excellent alternative donor substrate for LiLpxA
-
-
?
(R)-3-hydroxydecanoyl-[acyl-carrier protein] + UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucopyranose
[acyl-carrier protein] + UDP-3-N-(3-hydroxydecanoyl)-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucopyranose
show the reaction diagram
-
-
-
-
?
(R)-3-hydroxydodecanoyl-[acyl-carrier protein] + UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucopyranose
[acyl-carrier protein] + UDP-3-N-(3-hydroxydodecanoyl)-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucopyranose
show the reaction diagram
-
-
-
-
?
(R)-3-hydroxydodecanoyl-[acyl-carrier protein] + UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucopyranose
[acyl-carrier protein] + UDP-3-N-(3-hydroxydodecanoyl)-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucopyranose
show the reaction diagram
-
first step in lipid A biosynthesis pathway, lipid A is an unusual variant in this species containing 2,3-diamino-2,3-dideoxy-D-glucopyranose units, the enzyme is absolute specific for 3-hydroxylauroyl-ACP as donor substrate
-
-
?
(R)-3-hydroxydodecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxydodecanoyl)-N-acetylglucosamine
show the reaction diagram
-
-
-
-
?
(R)-3-hydroxyhexadecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxyhexadecanoyl)-N-acetylglucosamine
show the reaction diagram
-
-
-
-
?
(R)-3-hydroxylauroyl-[acyl-carrier protein] + UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucopyranose
[acyl-carrier protein] + UDP-3-N-((3R)-3-hydroxylauroyl)-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucopyranose
show the reaction diagram
-, Q8EZA6
LiLpxA is highly selective for (R)-3-hydroxylauroyl-[acyl-carrier protein] and UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucopyranose
-
-
?
(R)-3-hydroxymyristoyl-[acyl carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine
show the reaction diagram
P0A722
first step in lipid A biosynthesis
-
-
?
(R)-3-hydroxymyristoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxymyristoyl)-N-acetylglucosamine
show the reaction diagram
P0A722
first step in lipid A biosynthesis
-
-
?
(R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucopyranose
[acyl-carrier protein] + UDP-3-N-(3-hydroxytetradecanoyl)-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucopyranose
show the reaction diagram
-
-, first step in lipid A biosynthesis pathway, lipid A is an unusual variant in this species containing 2,3-diamino-2,3-dideoxy-D-glucopyranose units
-
-
?
(R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucopyranose
[acyl-carrier protein] + UDP-3-N-(3-hydroxytetradecanoyl)-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucopyranose
show the reaction diagram
Q6QHI7
first step in lipid A biosynthesis pathway, lipid A is an unusual variant in this species containing 2,3-diamino-2,3-dideoxy-D-glucopyranose units
-
-
?
(R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucopyranose
[acyl-carrier protein] + UDP-3-N-(3-hydroxytetradecanoyl)-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucopyranose
show the reaction diagram
-
only in vitro
-
-
?
(R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucopyranose
[acyl-carrier protein] + UDP-3-N-(3-hydroxytetradecanoyl)-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucopyranose
show the reaction diagram
Q6QHI7
specific for UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucopyranose
-
-
?
(R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine
show the reaction diagram
-
-
-
-
-
(R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine
show the reaction diagram
-
-
-
-
?
(R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine
show the reaction diagram
-
-
-
-
?
(R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine
show the reaction diagram
-
-
-
-
?
(R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine
show the reaction diagram
-
-
-
-
?
(R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine
show the reaction diagram
-
-
-
-
?
(R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine
show the reaction diagram
-
-
-
-
?
(R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine
show the reaction diagram
-
-
-
-
?
(R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine
show the reaction diagram
-
-
-
-
?
(R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine
show the reaction diagram
-
-
-
-
?
(R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine
show the reaction diagram
-
-
-
-
?
(R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine
show the reaction diagram
-
-
-
-
?
(R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine
show the reaction diagram
-
-
-
-
?
(R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine
show the reaction diagram
Q6QHI7
low activity
-
-
?
(R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine
show the reaction diagram
-
essential for cell growth of gram-negative bacteria, involved with EC 2.4.1.182 and 2.7.1.130 in the biosynthesis of the phosphorylated glycolipid and outer membrane component, Lipid A
-
-
-
(R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine
show the reaction diagram
-
involved with EC 2.4.1.182 and 2.7.1.130 in the biosynthesis of the phosphorylated glycolipid and outer membrane component, Lipid A
-
-
-
(R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine
show the reaction diagram
-
initial reaction in lipid A biosynthesis
-
-
-
(R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine
show the reaction diagram
-
first step in lipid A biosynthesis pathway
-
-
?
(R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine
show the reaction diagram
P0A722
LpxA is essential for the growth of Escherichia coli, and is important in lipid A biosynthesis, overview
-
-
?
(R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine
show the reaction diagram
P0A722
the enzyme is responsible for the first step of lipid A biosynthesis, lipid A is an integral component of the lipopolysaccharide that forms the selective and protective outer monolayer of Gram-negative bacteria, and is essential for bacterial growth and viability
-
-
?
(R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine
show the reaction diagram
P0A722
i.e. (R)-3-hydroxymyristoyl-[acyl-carrier protein], the enzyme catalyzes the first step of lipid A biosynthesis, the transfer of the (R)-3-hydroxyacyl chain from (R)-3-hydroxytetradecanoyl-[acyl-carrier protein] to the glucosamine 3-OH group of UDP-GlcNAc
-
-
?
(R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine
show the reaction diagram
-
i.e. (R)-3-hydroxymyristoyl-[acyl-carrier protein], the forward reaction direction is thermodynamically unfavorable, recombinant His-tagged enzyme, the activity with mutant acyl-carrier proteins is impaired, especially with mutations of the B-site of the acyl-carrier protein, recombinant wild-type and mutant ACP substrates, overview
-
-
?
(R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine
show the reaction diagram
P0A722
substrate binding site structure with prominent hydrophilic interactions between highly conserved clusters of residues Asn198, Glu200, Arg204 and Arg205 with UDP, and Asp74, His125, His144 and Gln161 with the GlcNAc moiety, these interactions serve to bind and orient the substrate for catalysis, overview, substrate binding site structure with prominent hydrophilic interactions between highly conserved clusters of residues Asn198, Glu200, Arg204 and Arg205 with UDP, and Asp74, His125, His144 and Gln161 with the GlcNAc moiety, these interactions serve to bind and orientate the substrate for catalysis, overview
-
-
?
(R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine
show the reaction diagram
Escherichia coli strains JB1104
-
initial reaction in lipid A biosynthesis
-
-
-
(R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine
show the reaction diagram
Escherichia coli strains JB1104
-
-
-
-
-
(R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine
show the reaction diagram
Escherichia coli W3106
-
initial reaction in lipid A biosynthesis
-
-
-
(R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine
show the reaction diagram
Escherichia coli SM105
-
-
-
-
-
(R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-butyrylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-butyrylglucosamine
show the reaction diagram
-
transacylation at 8% the rate of the reaction with UDP-N-acetylglucosamine
-
-
?
(R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-propionylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-propionylglucosamine
show the reaction diagram
-
transacylation at 22% the rate of the reaction with UDP-N-acetylglucosamine
-
-
?
(R,S)-3-hydroxydodecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxydodecanoyl)-N-acetylglucosamine
show the reaction diagram
-
-
-
-
?
(R,S)-3-hydroxydodecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxydodecanoyl)-N-acetylglucosamine
show the reaction diagram
-
-
-
-
?
(R,S)-3-hydroxydodecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxydodecanoyl)-N-acetylglucosamine
show the reaction diagram
-
-
-
-
?
(R,S)-3-hydroxydodecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxydodecanoyl)-N-acetylglucosamine
show the reaction diagram
-
-
-
-
?
(R,S)-3-hydroxydodecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxydodecanoyl)-N-acetylglucosamine
show the reaction diagram
-
-
-
-
?
(R,S)-3-hydroxydodecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxydodecanoyl)-N-acetylglucosamine
show the reaction diagram
-
-
-
-
?
(R,S)-3-hydroxydodecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxydodecanoyl)-N-acetylglucosamine
show the reaction diagram
-
main activity in crude extracts
-
-
?
(R,S)-3-hydroxydodecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxydodecanoyl)-N-acetylglucosamine
show the reaction diagram
-
main activity in crude extracts
-
-
-
(R,S)-3-hydroxydodecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxydodecanoyl)-N-acetylglucosamine
show the reaction diagram
-
i.e. 3-hydroxylauroyl-[acyl-carrier-protein], poor substrate
-
-
-
(R,S)-3-hydroxydodecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxydodecanoyl)-N-acetylglucosamine
show the reaction diagram
Escherichia coli strains JB1104, Escherichia coli SM105
-
-
-
-
?
(R,S)-3-hydroxyhexadecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxyhexadecanoyl)-N-acetylglucosamine
show the reaction diagram
-
-
-
-
?
(R,S)-3-hydroxylauroyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxylauroyl)-N-acetylglucosamine
show the reaction diagram
-
-
-
-
?
(R,S)-3-hydroxylauroyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxylauroyl)-N-acetylglucosamine
show the reaction diagram
-
-
-
-
?
(R,S)-3-hydroxylauroyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxylauroyl)-N-acetylglucosamine
show the reaction diagram
-
-
-
-
?
(R,S)-3-hydroxymyristoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxymyristoyl)-N-acetylglucosamine
show the reaction diagram
-
-
-
-
?
(R,S)-3-hydroxymyristoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxymyristoyl)-N-acetylglucosamine
show the reaction diagram
-
-
-
-
?
(R,S)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine
show the reaction diagram
-
-
-
-
-
(R,S)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine
show the reaction diagram
-
-
-
-
r
(R,S)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine
show the reaction diagram
-
-
-
-
?
(R,S)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine
show the reaction diagram
-
-
-
-
-
(R,S)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine
show the reaction diagram
-
-
-
-
?
(R,S)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine
show the reaction diagram
-
-
-
-
?
(R,S)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine
show the reaction diagram
-
-
-
-
?
(R,S)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine
show the reaction diagram
-
-
-
-
?
(R,S)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine
show the reaction diagram
-
-
-
-
?
(R,S)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine
show the reaction diagram
-
-
-
-
?
(R,S)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine
show the reaction diagram
-
-
-
-
?
(R,S)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine
show the reaction diagram
-
no substrates are UDPglucosamine, UDP-N-(R)-3-hydroxymyristoylglucosamine, ADP-N-acetylglucosamine, GDP-N-acetylglucosamine, CDP-N-acetylglucosamine, (R)-3-hydroxytetradecanoyl-CoA, or palmitoyl-CoA, myristoyl-[acyl-carrier-protein], and palmitoyl-[acyl-carrier-protein]
-
-
-
(R,S)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine
show the reaction diagram
-
no substrates are UDPglucosamine, UDP-N-(R)-3-hydroxymyristoylglucosamine, ADP-N-acetylglucosamine, GDP-N-acetylglucosamine, CDP-N-acetylglucosamine, (R)-3-hydroxytetradecanoyl-CoA, or palmitoyl-CoA, myristoyl-[acyl-carrier-protein], and palmitoyl-[acyl-carrier-protein], high specificity with respect to acyl-donor, equilibrium constant favors thioester acyl carrier substrate
-
-
r
(R,S)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine
show the reaction diagram
Escherichia coli strains JB1104
-
no substrates are UDPglucosamine, UDP-N-(R)-3-hydroxymyristoylglucosamine, ADP-N-acetylglucosamine, GDP-N-acetylglucosamine, CDP-N-acetylglucosamine, (R)-3-hydroxytetradecanoyl-CoA, or palmitoyl-CoA, myristoyl-[acyl-carrier-protein], and palmitoyl-[acyl-carrier-protein]
-
-
-
(R,S)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine
show the reaction diagram
Escherichia coli strains JB1104
-
-
-
-
-
(R,S)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine
show the reaction diagram
Escherichia coli W3106
-
-
-
-
-
(R,S)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine
show the reaction diagram
Escherichia coli SM105
-
-
-
-
-
(S)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine
show the reaction diagram
-
transacylation at 7% the rate of (R)-enantiomer
-
-
?
an (R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetyl-alpha-D-glucosamine
an [acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetyl-alpha-D-glucosamine
show the reaction diagram
-
-
-
-
?
an (R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetyl-alpha-D-glucosamine
an [acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetyl-alpha-D-glucosamine
show the reaction diagram
-
-
-
-
r
an (R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetyl-alpha-D-glucosamine
an [acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetyl-alpha-D-glucosamine
show the reaction diagram
-, Q9SU91
-
-
-
r
an (R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetyl-alpha-D-glucosamine
an [acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetyl-alpha-D-glucosamine
show the reaction diagram
Q9SU91
-
-
-
r
an (R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetyl-alpha-D-glucosamine
an [acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetyl-alpha-D-glucosamine
show the reaction diagram
-
assay is optimal at 10 nM LpxA
-
-
?
an (R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetyl-alpha-D-glucosamine
an [acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetyl-alpha-D-glucosamine
show the reaction diagram
-, Q9SU91
specificity for (R)-3-hydroxymyristoyl-ACP over other chain lengths in vitro
-
-
r
myristoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-myristoyl-N-acetylglucosamine
show the reaction diagram
-
higher specific activity than to (R,S)-3-hydroxymyristoyl-[acyl-carrier-protein]
-
-
?
R-3-hydroxydecanoyl-[acyl carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-o-hydroxydecanoyl-N-acetylglucosamine
show the reaction diagram
P0A722
first step in lipid A biosynthesis
-
-
?
decanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-decanoyl-N-acetylglucosamine
show the reaction diagram
-
-
-
-
?
additional information
?
-
Q6QHI7
substrate specificity, lipid A structure overview
-
-
-
additional information
?
-
-
substrate specificity, no activity with UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucopyranose due to lack of genes gnnA and gnnB, lipid A structure overview
-
-
-
additional information
?
-
-
substrate specificity, no activity with UDP-N-acetylglucosamine, equally effective with 3-hydroxyacyl-ACP of different chain lengths, lipid A structure overview
-
-
-
additional information
?
-
-
substrate specificity, no activity with UDP-N-acetylglucosamine, lipid A structure overview
-
-
-
additional information
?
-
-, Q3BDJ0
the enzyme is responsible for the first step of lipid A biosynthesis
-
-
-
additional information
?
-
P0A722
nucleotide substrate recognition by LpxA, overview
-
-
-
additional information
?
-
-
development of a fluorescence polarization assay, detecting displacement of a fluorescently labeled peptide inhibitor based on the previously reported inhibitor peptide 920 by active site ligands, for high-throughput screening of LpxA competitve inhibitors, overview
-
-
-
additional information
?
-
Q3BDJ0
the enzyme is responsible for the first step of lipid A biosynthesis
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(R)-3-hydroxydodecanoyl-[acyl-carrier protein] + UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucopyranose
[acyl-carrier protein] + UDP-3-N-(3-hydroxydodecanoyl)-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucopyranose
show the reaction diagram
-
first step in lipid A biosynthesis pathway, lipid A is an unusual variant in this species containing 2,3-diamino-2,3-dideoxy-D-glucopyranose units
-
-
?
(R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucopyranose
[acyl-carrier protein] + UDP-3-N-(3-hydroxytetradecanoyl)-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucopyranose
show the reaction diagram
-
first step in lipid A biosynthesis pathway, lipid A is an unusual variant in this species containing 2,3-diamino-2,3-dideoxy-D-glucopyranose units
-
-
?
(R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucopyranose
[acyl-carrier protein] + UDP-3-N-(3-hydroxytetradecanoyl)-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucopyranose
show the reaction diagram
Q6QHI7
first step in lipid A biosynthesis pathway, lipid A is an unusual variant in this species containing 2,3-diamino-2,3-dideoxy-D-glucopyranose units
-
-
?
(R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine
show the reaction diagram
-
-
-
-
-
(R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine
show the reaction diagram
-
-
-
-
?
(R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine
show the reaction diagram
-
-
-
-
?
(R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine
show the reaction diagram
-
-
-
-
?
(R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine
show the reaction diagram
-
-
-
-
?
(R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine
show the reaction diagram
-
-
-
-
?
(R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine
show the reaction diagram
-
-
-
-
?
(R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine
show the reaction diagram
-
-
-
-
?
(R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine
show the reaction diagram
-
-
-
-
?
(R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine
show the reaction diagram
-
-
-
-
?
(R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine
show the reaction diagram
-
-
-
-
?
(R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine
show the reaction diagram
-
essential for cell growth of gram-negative bacteria, involved with EC 2.4.1.182 and 2.7.1.130 in the biosynthesis of the phosphorylated glycolipid and outer membrane component, Lipid A
-
-
-
(R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine
show the reaction diagram
-
involved with EC 2.4.1.182 and 2.7.1.130 in the biosynthesis of the phosphorylated glycolipid and outer membrane component, Lipid A
-
-
-
(R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine
show the reaction diagram
-
initial reaction in lipid A biosynthesis
-
-
-
(R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine
show the reaction diagram
-
first step in lipid A biosynthesis pathway
-
-
?
(R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine
show the reaction diagram
P0A722
LpxA is essential for the growth of Escherichia coli, and is important in lipid A biosynthesis, overview
-
-
?
(R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine
show the reaction diagram
P0A722
the enzyme is responsible for the first step of lipid A biosynthesis, lipid A is an integral component of the lipopolysaccharide that forms the selective and protective outer monolayer of Gram-negative bacteria, and is essential for bacterial growth and viability
-
-
?
(R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine
show the reaction diagram
Escherichia coli strains JB1104
-
initial reaction in lipid A biosynthesis
-
-
-
(R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine
show the reaction diagram
Escherichia coli strains JB1104
-
-
-
-
-
(R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine
show the reaction diagram
Escherichia coli W3106
-
initial reaction in lipid A biosynthesis
-
-
-
(R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetylglucosamine
[acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine
show the reaction diagram
Escherichia coli SM105
-
-
-
-
-
an (R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetyl-alpha-D-glucosamine
an [acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetyl-alpha-D-glucosamine
show the reaction diagram
-
-
-
-
?
an (R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetyl-alpha-D-glucosamine
an [acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetyl-alpha-D-glucosamine
show the reaction diagram
-
-
-
-
r
an (R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetyl-alpha-D-glucosamine
an [acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetyl-alpha-D-glucosamine
show the reaction diagram
-, Q9SU91
-
-
-
r
an (R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetyl-alpha-D-glucosamine
an [acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetyl-alpha-D-glucosamine
show the reaction diagram
Q9SU91
-
-
-
r
additional information
?
-
-, Q3BDJ0
the enzyme is responsible for the first step of lipid A biosynthesis
-
-
-
additional information
?
-
Q3BDJ0
the enzyme is responsible for the first step of lipid A biosynthesis
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
not as effective as Mg2+
KCl
-
slight activation at 0.25 M
LiCl
-
slight activation at 0.25 M
Mg2+
-
is required for stabilization of substrate acyl-carrier protein in a helical conformation
Mn2+
-
not as effective as Mg2+
NaCl
-
slight activation at 0.25 M
sulfate
-
2 ions per asymmetrical unit
Tartrate
-
1 ions per asymmetrical unit
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
diethyldicarbonate
-
-
DL-3-hydroxymyristic acid
-
competitive versus TAMRA peptide
-
FITC-P920
-
i.e. FITC-(betaa)SSGWMLDPIAGKWSRNH2, fluoresecent-labeled peptide
-
HM-UNAG peptide
-
-
-
HMA peptide
-
-
-
myristoyl-[acyl-carrier protein]
-
-
myristoyl-[acyl-carrier protein]
-
-
P920
-
i.e. SSGWMLDPIAGKWSR
-
peptide 920
P0A722
a pentadecapeptide
-
peptide 920
P0A722
pentadecapeptide NH2-SSGWMLDPIAGKWSR-COOH, the enzyme binds peptide 920 with three peptides, each of which adopts a beta-hairpin conformation, bound per LpxA trimer, the peptides are located at the interfaces of adjacent subunits in the vicinity of the three active sites, each peptide interacts with residues from both adjacent subunits, noncovalent interaction and binding structure, overview
-
peptide 920
-
i.e. pentadecapeptide 920, with C-terminus WMLDPIAGKWSR, competitive versus peptide inhibitors derived from its own C-terminal sequence
-
Phenylglyoxal
-
-
pyridoxal 5'-phosphate/sodium borohydride
-
-
RJPXD31
-
i.e. QHFMVPDINDMQ-NH2
-
RJPXD33
-
i.e. TNLYMLPKWDIP-NH2, a peptide identified from a phage-bound random peptide library screen uing Escherichia oli strain XL-1 Blue, binds to UDP-3-O-(R-3-hydroxyacyl)GlcN N-acyltransferase, LpxD, and UDP-N-acetylglucosamine acyltransferase, LpxA. RJPXD33 binds to LpxA in a competitive fashion with P920
-
TAMRA peptide
-
ability of the TAMRA-peptide to inhibit the catalytic activity
-
Triton X-100
-
-
UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine
-
competitive versus TAMRA peptide
UDP-N-acetylglucosamine
-
competitive versus TAMRA peptide
UNAG peptide
-
-
-
additional information
-
no inhibition by N-ethylmaleimide, UDP-2,3-diacyl-N-glucosamine, lipid X, lipid IVA, 3-deoxy-D-mannooctulosonate, octyl-beta-D-glucoside
-
additional information
-
measurement of binding of fluorescein-labeled peptide to acyltransferase by measuring the changes in fluorescence polarization, KD values, overview. No inhibition of LpxA by SENNFMLPLLPL-NH2, i.e. peptide RJPXD34
-
additional information
-
development of a fluorescence polarization assay, detecting displacement of a fluorescently labeled peptide inhibitor, based on inhibitor peptide 920 C-terminal 12 residues WMLDPIAGKWSR, by active site ligands, for high-throughput screening of LpxA competitve inhibitors, overview. Abilities of several ligands to compete with TAMRA peptide for binding to Escherichia coli LpxA. Acyl carrier protein does not significantly affect the inhibitory potencies
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0016
-
(R)-3-hydroxytetradecanoyl-[acyl-carrier protein]
-
-
0.005
-
(R)-3-hydroxytetradecanoyl-[acyl-carrier protein]
P0A722
pH 8.0, 30C
0.099
-
UDP-N-acetylglucosamine
-
-
0.82
-
UDP-N-acetylglucosamine
-
wild-type
7
-
UDP-N-acetylglucosamine
-
K76R
15
-
UDP-N-acetylglucosamine
-
K76A
0.004
-
3R-3-hydroxylauroyl-methylphosphopantetheine
-, Q8EZA6
-
additional information
-
additional information
-
the kinetic analysis of LpxA is complicated by the thermodynamically unfavorable reaction in the forward direction, overview
-
additional information
-
additional information
-
Michaelis-Menten steady-state kinetics of LpxA, overview
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
7.17
-
UDP-N-acetylglucosamine
-
wild-type
9.83
-
UDP-N-acetylglucosamine
-
K76R
10.5
-
UDP-N-acetylglucosamine
-
K76A
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
5e-05
-
peptide 920
P0A722
peptide 920 disrupts LpxA interactions with the R-3-hydroxymyristoyl-ACP substrate
-
5e-05
-
peptide 920
P0A722
pH 8.0, 30C
-
additional information
-
additional information
P0A722
inhibition kinetics
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.05
-
DL-3-hydroxymyristic acid
-
pH 7.0, 22C
-
0.00014
-
HM-UNAG peptide
-
forward reaction, pH 7.0, 22C, versus TAMRA peptide, in absence of holo-ACP
-
0.000238
-
HM-UNAG peptide
-
forward reaction, pH 7.0, 22C, versus TAMRA peptide, in presence of holo-ACP
-
0.047
-
HMA peptide
-
forward reaction, pH 7.0, 22C, versus TAMRA peptide, in absence of holo-ACP
-
0.063
-
HMA peptide
-
forward reaction, pH 7.0, 22C, versus TAMRA peptide, in presence of holo-ACP
-
6e-05
-
peptide 920
-
forward reaction, pH 7.0, 22C, versus TAMRA peptide
-
0.00051
-
peptide 920
-
forward reaction, pH 7.0, 22C, versus TAMRA peptide, in presence of holo-ACP
-
0.0006
-
peptide 920
-
forward reaction, pH 7.0, 22C, versus 0.001 mM UNAG peptide
-
0.00073
-
peptide 920
-
forward reaction, pH 7.0, 22C, versus TAMRA peptide, in absence of holo-ACP
-
0.000923
-
peptide 920
-
forward reaction, pH 7.0, 22C, versus 5 mM UNAG peptide
-
0.019
-
RJPXD33
-
pH 7.5, 30C
-
0.00015
-
TAMRA peptide
-
forward reaction, pH 7.0, 22C
-
0.0002
-
UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine
-
pH 7.0, 22C
6
-
UDP-N-acetylglucosamine
-
pH 7.0, 22C
5.8
-
UNAG peptide
-
forward reaction, pH 7.0, 22C, versus TAMRA peptide, in absence of holo-ACP
-
6.6
-
UNAG peptide
-
forward reaction, pH 7.0, 22C, versus TAMRA peptide, in presence of holo-ACP
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2e-08
-
-
S)-3-hydroxytetradecanoyl-[acyl-carrier-protein] as substrate, pTO15
1.4e-07
-
-
S)-3-hydroxydecanoyl-[acyl-carrier-protein] as substrate, pTO14
2.8e-07
-
-
S)-3-hydroxydodecanoyl-[acyl-carrier-protein] as substrate, pTO15
3.4e-07
-
-
S)-3-hydroxydodecanoyl-[acyl-carrier-protein] as substrate, pTO14
7.2e-07
-
-
S)-3-hydroxyhexadecanoyl-[acyl-carrier-protein]
1e-06
-
-
S)-3-hydroxydodecanoyl-[acyl-carrier-protein] as substrate, pTO202; S)-3-hydroxytetradecanoyl-[acyl-carrier-protein] as substrate, pTO9
1.1e-06
-
-
S)-3-hydroxymyristoyl-[acyl-carrier-protein] as substrate
1.5e-06
-
-
decanoyl-[acyl-carrier-protein] as substrate
3e-06
-
-
S)-3-hydroxydecanoyl-[acyl-carrier-protein] as substrate, pTO201
3.2e-06
-
-
S)-3-hydroxylauroyl-[acyl-carrier-protein] as substrate
6e-06
-
-
S)-3-hydroxydecanoyl-[acyl-carrier-protein] as substrate, pTO10 and pTO105
7e-06
-
-
S)-3-hydroxydodecanoyl-[acyl-carrier-protein] as substrate, pTO10
1e-05
-
-
S)-3-hydroxytetradecanoyl-[acyl-carrier-protein] as substrate, pTO202
1.1e-05
-
-
S)-3-hydroxydecanoyl-[acyl-carrier-protein] as substrate, pTO15
1.4e-05
-
-
S)-3-hydroxytetradecanoyl-[acyl-carrier-protein] as substrate, pTO14
1.5e-05
-
-
S)-3-hydroxydodecanoyl-[acyl-carrier-protein]
1.9e-05
-
-
S)-3-myristoyl-[acyl-carrier-protein] as substrate
2.2e-05
-
-
S)-3-hydroxydecanoyl-[acyl-carrier-protein] as substrate, pTO105
2.3e-05
-
-
S)-3-hydroxydecanoyl-[acyl-carrier-protein] as substrate, pTO103
2.4e-05
-
-
S)-3-hydroxydodecanoyl-[acyl-carrier-protein] as substrate, pTO201
3e-05
-
-
SM 101
3.8e-05
-
-
S)-3-hydroxydecanoyl-[acyl-carrier-protein] as substrate, pTO202
4e-05
-
-
S)-3-hydroxydodecanoyl-[acyl-carrier-protein] as substrate, pTO9
5.4e-05
-
-
S)-3-hydroxydecanoyl-[acyl-carrier-protein] as substrate, pTO1
5.5e-05
-
-
S)-3-hydroxymyristoyl-[acyl-carrier-protein] as substrate
6e-05
-
-
S)-3-hydroxytetradecanoyl-[acyl-carrier-protein] as substrate, pTO101
6.7e-05
-
-
S)-3-hydroxymyristoyl-[acyl-carrier-protein] as substrate
6.8e-05
-
-
S)-3-hydroxytetradecanoyl-[acyl-carrier-protein] as substrate, pTO104
7e-05
-
-
SM 108
7e-05
-
-
S)-3-hydroxydecanoyl-[acyl-carrier-protein] as substrate
7.9e-05
-
-
S)-3-hydroxydecanoyl-[acyl-carrier-protein] as substrate, pTO101
8.7e-05
-
-
S)-3-hydroxytetradecanoyl-[acyl-carrier-protein] as substrate, pTO103
0.0002
-
-
S)-3-hydroxytetradecanoyl-[acyl-carrier-protein] as substrate, pTO102
0.000247
-
-
S)-3-hydroxydecanoyl-[acyl-carrier-protein] as substrate
0.000347
-
-
S)-3-hydroxytetradecanoyl-[acyl-carrier-protein] as substrate, pTO10
0.00035
-
-
S)-3-hydroxydecanoyl-[acyl-carrier-protein] as substrate, pTO104
0.00035
-
-
S)-3-hydroxydodecanoyl-[acyl-carrier-protein]
0.00047
-
-
S)-3-hydroxydodecanoyl-[acyl-carrier-protein]
0.00053
-
-
S)-3-hydroxytetradecanoyl-[acyl-carrier-protein] as substrate, pTO102
0.00059
-
-
S)-3-hydroxydecanoyl-[acyl-carrier-protein]
0.00079
-
-
S)-3-hydroxytetradecanoyl-[acyl-carrier-protein]
0.00087
-
-
S)-3-hydroxydecanoyl-[acyl-carrier-protein]
0.001
-
-
S)-3-hydroxydecanoyl-[acyl-carrier-protein] as substrate, pTO102
0.001
-
-
S)-3-hydroxydecanoyl-[acyl-carrier-protein] as substrate, pTO9
0.001
-
-
S)-3-hydroxytetradecanoyl-[acyl-carrier-protein]
0.0011
-
-
S)-3-hydroxydecanoyl-[acyl-carrier-protein]
0.0012
-
-
S)-3-hydroxydodecanoyl-[acyl-carrier-protein] as substrate, pTO1
0.0012
-
-
S)-3-hydroxytetradecanoyl-[acyl-carrier-protein] as substrate, pTO201
0.00139
-
-
S)-3-hydroxylauroyl-[acyl-carrier-protein] as substrate
0.0015
-
-
SM 105
0.00325
-
-
S)-3-hydroxylauroyl-[acyl-carrier-protein] as substrate
0.011
-
-
S)-3-hydroxydecanoyl-[acyl-carrier-protein] as substrate
0.074
-
-
S)-3-hydroxytetradecanoyl-[acyl-carrier-protein] as substrate, pTO1
3
-
-, Q8EZA6
using synthetic (3R)-3-hydroxylauroyl-methylphosphopantetheine + UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucopyranose as a substrate the specific activity is comparable to substrates (3R)-3-hydroxylauroyl-[acyl-carrier protein] + UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucopyranose
additional information
-
Q6QHI7
activity of the recombinant enzyme
additional information
-
-
substrate specificity with different acyl acceptors, activity of the recombinant enzyme
additional information
-
-
substrate specificity with different acyl acceptors
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.8
8.2
-
broad
7
-
-
assay at, binding measurements are performed at pH 8.0
7.4
-
-, Q9SU91
assay at
7.5
-
-
activity assay at
8
-
-
assay at
8
-
P0A722
assay at
8
-
-, Q8EZA6
assay at
8
-
-
binding assay at
8
-
-
assay at
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
22
-
-
assay at room temperature
25
-
-
assay at
25
-
-
assay at
30
-
-
assay at
30
-
Q6QHI7
assay at
30
-
P0A722
assay at
30
-
-, Q8EZA6
assay at
30
-
-
folding assay is performed at 30C
30
-
-
assay at
30
-
-, Q9SU91
assay at
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
Acinetobacter baumannii (strain TCDC-AB0715)
Acinetobacter baumannii (strain TCDC-AB0715)
Burkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 / CIP 106301)
Campylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 11168)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Helicobacter pylori (strain ATCC 700392 / 26695)
Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601)
Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601)
Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
28000
-
-
SDS-PAGE
90000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 27000, calculated from nucleotide sequence
dimer or trimer
-
alpha2, 2 * 30000, SDS-PAGE
homotrimer
-, Q8EZA6
in aqueous solution, shown by gel filtration
trimer
-
alpha3, 3 * 30000, SDS-PAGE
trimer
-
3 * 29855, amino acid sequence and crystal structure determination
trimer
P0A722
; homotrimer, the active site lies within a positively charged cleft formed at the subunit-subunit interface
trimer
P0A722
homotrimer, LpxA contains an unusual, left-handed parallel beta-helix fold, crystal structure analysis
trimer
-
SDS-PAGE, 3 * 30000 Da
homotrimer
-
-
additional information
-
enzyme structure contains a left-handed parallel beta-helix motif
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
purified recombinant LpxA, sitting drop vapor diffusion method, mixing of AtLpxA at 18 mg/mL in 10 mM potassium phosphate buffer, pH 7.0, 200 mM KCl, and 20% glycerol, in a 1:1 ratio with precipitant solution containing 0.5 M ammonium sulfate, 0.1 M sodium citrate, pH 5.6, and 1.0 M lithium sulfate monohydrate, equilibration at 20C, 1-2 days, X-ray diffraction structure determination and analysis at 2.1 A resolution
-, Q9SU91
by the sitting-drop, vapour-diffusion method using 0.00l ml of protein solution; LpxA in complex with UDP-GlcNAc, modelling
P0A722
by using the hanging drop vapor diffusion method, in the presence of a 25-fold molar excess of either UDP-3-O-(R-3-hydroxymyristoyl)-GlcNAc or UDP-3-O-(R-3-hydroxydecanoyl)-GlcNAc, structures show how LpxA selects for 14-carbon R-3-hydroxyacyl chains and reveal two modes of UDP binding
-
purified enzyme LpxA in a complex with inhibitor peptide 920, 20 mg/ml protein in solution with a 25fold molar excess of peptide 920 of 12.5 mM, crystal growth at 18C, hanging drop vapor diffusion method, mixing of 0.002 ml protein solution with 0.002 ml of 0.81.8 M phosphate buffer, pH 6.36.9, and 30-35% DMSO, about 2 weeks, X-ray diffraction structure determination and analysis at 1.8 A resolution, molecular replacement using crystal structure PDB ID code 1LXA, determined at 2.6 A resolution
P0A722
crystallized at 297 K using (NH4)2SO4 and Na/K tartrate as precipitants in the presence of a detergent, space group: P6322 with unit cell-parameters: a = b = 90.69, and c = 148.20 ANG
-
purified recombinant, C-terminally eight-residue-tagged enzyme, X-ray diffraction structure analysis at 2.1 A resolution, modeling of the enzyme complexed with [acyl-carrier protein]
-
crystal structures of free LiLpxA and its complexes with its product UDP-3-N-((R)-3-hydroxylauroyl)-GlcNAc3N and with its substrate (R)-3-hydroxylauroyl-methylphosphopantetheine are presented. The selectivity of LiLpxA for UDPGlcNAc3N may be explained by the orientation of the backbone carbonyl group of Q68, which differs by 82 from the corresponding Q73 carbonyl group in Escherichia coli LpxA. This arrangement provides an extra hydrogen-bond acceptor for the 3-NH2 group of UDP-GlcNAc3N in LiLpxA. The R-3-hydroxylauroyl selectivity of LiLpxA is explained by the position of the K171 side chain, which limits the length of the acyl-chain-binding groove. H120 functions as a catalytic base
-, Q8EZA6
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
60
-
-
20 min stable
100
-
-
inactivation after 10 min
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
bovine serum albumin prevents denaturation
-
freeze-thawing inactivates
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-80C, flash-frozen in liquid nitrogen, at least 3 months
-
4C, several days
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant LpxA, excluding the region encoding the predicted signal peptide (residues 2-32), from Escherichia coli strain C41(DE3) by Reactive Green 19 affinity chromatography and gel filtration to homogeneity
-, Q9SU91
partial, overproducing strain MC1061/pSR1
-
recombinant LpxA from Echerichia coli strain BL21-AI/pET24a by Reactive Green 19 affinity chromatography, dialysis, and ion exchange chromatography
-
using Ni-NTA chromatography and gel filtration. Around 15 mg of purified protein is obtained from 1 l of bacterial culture
-
ion-exchange-chromatography and gel filtration
-, Q8EZA6
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
gene lpxA, DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain BL21(DE3)
Q6QHI7
gene lpxA, excluding the region encoding the predicted signal peptide (residues 2-32), expression of the plant enzyme in Escherichia coli strain C41(DE3). Functional expression of AtlpxA in and complementation of the constructed lpxA Escherichia coli knockout mutant strains
-, Q9SU91
gene lpxA, five AtLpxC orthologues located in a 68-kb region on chromosome one, DNA and amino acid sequence determination and analysis, sequence comparison
Q9SU91
overexpression in Escherichia coli
-
expressed in Escherchia coli as a His-tagged fusion protein
-
expression in Corynebacterium glutamicum
-
gene lpxA, cloning from strain strain MG1655, subcloning in strain XL-1 Blue, expression in Escherichia coli strain BL21-AI/pET24a
-
gene lpxA, expression in strain BL21(DE3)
-
recombinant expresssion
-
expressed in Escherichia coli
-, Q8EZA6
gene lpxA, expression in Escherichia coli strain BL21(DE3)
-
gene lpxA, DNA and amino acid sequence determination, subcloning in Escherichia coli, wild-type and mutant strains expression analysis
-, Q3BDJ0
expression in Escherichia coli
-
expression in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
G189S
-
Escherichia coli strain SM101 is deficient in LpxA activity due to a G189S inactivating mutation. Enzymatic activity is restored when the mutant strain is transformed with a wild-type bearing plasmid is inactive
G52L/R58L
-
residue tolerance in the beta-helical domain: mutation is tolerated
G52V/R58V
-
residue tolerance in the beta-helical domain: mutation is tolerated
G52W/R58W
-
residue tolerance in the beta-helical domain: mutation is tolerated
G57P/N51P
-
residue tolerance in the beta-helical domain: mutation is not tolerated
H122A
-
lower specific activity than wild-type
H122N
-
lower specific activity than wild-type
H125A
-
lower specific activity than wild-type
H125A
-
H125 is an important residue at the active site its mutation eliminates activity. Mutant shows significant growth reduction after introduction into Escherichia coli strain SM101 bearing a defective LpxA gene (G189S), and under novobiocin supplementation
H125N
-
lower specific activity than wild-type
H144A
-
lower specific activity than wild-type
H144N
-
lower specific activity than wild-type
H160A
-
lower specific activity than wild-type
H160F
-
lower specific activity than wild-type
H53I/D59I
-
residue tolerance in the beta-helical domain: mutation is tolerated
H53V/D59V
-
residue tolerance in the beta-helical domain: mutation is tolerated
I20R
-
mutation in the hydrophobic residue in the beta-helical core located in rung 2: LpxA is active
I2R
-
mutation in the hydrophobic residue in the beta-helical core located in rung 1: LpxA is active
I38R
-
mutation in the hydrophobic residue in the beta-helical core located in rung 3: LpxA is partially active
I56A
-
mutation in the hydrophobic core of the beta-helical domain: LpxA activity is not significantly affected compared to wild-type
I56D/I62D
-
residue tolerance in the beta-helical domain: mutation is not tolerated
I56E/I62E
-
residue tolerance in the beta-helical domain: mutation is not tolerated
I56G
-
mutation in the hydrophobic core of the beta-helical domain: LpxA activity is decreased compared to wild-type
I56G/I62G
-
residue tolerance in the beta-helical domain: mutation is tolerated
I56H/I62H
-
residue tolerance in the beta-helical domain: mutation is not tolerated
I56K/I62K
-
residue tolerance in the beta-helical domain: mutation is not tolerated
I56N
-
mutation in the hydrophobic core of the beta-helical domain: LpxA activity is decreased compared to wild-type
I56N/I62N
-
residue tolerance in the beta-helical domain: mutation is tolerated
I56P/I62P
-
residue tolerance in the beta-helical domain: mutation is not tolerated
I56Q
-
mutation in the hydrophobic core of the beta-helical domain: LpxA activity is decreased compared to wild-type
I56Q/I62Q
-
residue tolerance in the beta-helical domain: mutation is tolerated
I56R
-
mutation in the hydrophobic core of the beta-helical domain: LpxA activity is completely abolished compared to wild-type; mutation in the hydrophobic residue in the beta-helical core located in rung 4: LpxA is inactive
I56R/I62R
-
residue tolerance in the beta-helical domain: mutation is not tolerated
I56S/I62S
-
residue tolerance in the beta-helical domain: mutation is tolerated
I56W/I62W
-
residue tolerance in the beta-helical domain: mutation is not tolerated
I56Y/I62Y
-
residue tolerance in the beta-helical domain: mutation is not tolerated
I86R
-
mutation in the hydrophobic residue in the beta-helical core located in rung 5: LpxA is inactive; residue is located in the fifth rung of the beta-helical domain in the hydrophobic core of a beta helix, mutant is improperly folded, destabilized and its enzymatic activity is decreased. Mutant shows significant growth reduction after introduction into Escherichia coli strain SM101 bearing a defective LpxA gene (G189S), and under novobiocin supplementation
K55D/E61D
-
residue tolerance in the beta-helical domain: mutation is tolerated
K55P/E61P
-
residue tolerance in the beta-helical domain: mutation is not tolerated
K76A
-
lower specific activity than wild-type
P10A/P28A/P34A/P183A
-
proline mutation at the turn region of the beta-helical domain: mutant shows lower activity compared to wild-type
P28A/P34A
-
proline mutation at the turn region of the beta-helical domain: mutant shows greater activity than the P10A/P28A/P34A/P183A mutant
T54D/N60D
-
residue tolerance in the beta-helical domain: mutation is not tolerated
T54E/N60E
-
residue tolerance in the beta-helical domain: mutation is not tolerated
T54G/N60G
-
residue tolerance in the beta-helical domain: mutation is tolerated
T54H/N60H
-
residue tolerance in the beta-helical domain: mutation is not tolerated
T54K/N60K
-
residue tolerance in the beta-helical domain: mutation is not tolerated
T54M/N60M
-
residue tolerance in the beta-helical domain: mutation is tolerated
T54P/N60P
-
residue tolerance in the beta-helical domain: mutation is not tolerated
T54Q/N60Q
-
residue tolerance in the beta-helical domain: mutation is tolerated
T54R/N60R
-
residue tolerance in the beta-helical domain: mutation is not tolerated
T54W/N60W
-
residue tolerance in the beta-helical domain: mutation is not tolerated
T54Y/N60Y
-
residue tolerance in the beta-helical domain: mutation is not tolerated
V111R
-
mutation in the hydrophobic residue in the beta-helical core located in rung 6: LpxA is inactive
V129R
-
mutation in the hydrophobic residue in the beta-helical core located in rung 7: LpxA is inactive
additional information
-, Q9SU91
Arabidopsis thaliana lpxA complements an Escherichia coli mutant lacking the chromosomal lpxA and promotes the synthesis of lipid A in vivo similar to the lipid A produced in the presence of Escherichia coli lpxA
K76R
-
lower specific activity than wild-type
additional information
-
heterologous expression of Acidithiobacillus ferrooxidans' genes lpxA, gnnA, and gnnB results in occurence of UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucopyranose utilizing activity in Escherichia coli cells with defective lpxA gene in vivo
additional information
-
a recombinant prion protein-LpxA protein is generated, in which a PrP fragment that is thought to be essential for the conformational conversion is incorporated into the beta-helical domain of LpxA. Partial Lpxa enzymatic activity is observed, suggesting that the beta-helical structure may be able to accommodate a portion of the prion protein sequence and, as a corollary, that a prion protein fragment may adopt left-handed parallel beta helix (LbetaH) architecture
Y66F/Y77F/Y219F/Y223F/Y243H
-
all but one tyrosine residues are mutated. Mutant shows growth similar to wild-type after introduction into Escherichia coli strain SM101 bearing a defective LpxA gene (G189S), and under novobiocin supplementation
additional information
-, Q3BDJ0
construction and characterization of an isogenic Moraxella catarrhalis lpxA mutant in strain O35E, which is viable despite the complete loss of cell surface lipooligosaccharides, the mutant strain shows significantly decreased toxicity in the Limulus amebocyte lysate assay, reduced resistance to normal human serum, reduced adherence to human epithelial cells, and enhanced clearance in lungs and nasopharynx in a mouse aerosol challenge model, phenotype, overview, the mutant elicits high levels of antibodies with bactericidal activity and provides protection against a challenge with the wild-type strain, thus the null LOS mutant is attenuated and may be a potential vaccine candidate against Moraxella catarrhalis
additional information
-
construction and characterization of an isogenic Moraxella catarrhalis lpxA mutant in strain O35E, which is viable despite the complete loss of cell surface lipooligosaccharides, the mutant strain shows significantly decreased toxicity in the Limulus amebocyte lysate assay, reduced resistance to normal human serum, reduced adherence to human epithelial cells, and enhanced clearance in lungs and nasopharynx in a mouse aerosol challenge model, phenotype, overview, the mutant elicits high levels of antibodies with bactericidal activity and provides protection against a challenge with the wild-type strain, thus the null LOS mutant is attenuated and may be a potential vaccine candidate against Moraxella catarrhalis
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
drug development
P0A722
the enzyme is a target for design of inhibitors with antibiotic potency
drug development
-
development of small molecule, dual-binding LpxA/LpxD inhibitors as novel antimicrobials
drug development
-
Lpxa is a viable target for antimicrobial drug development
drug development
-
LpxA is a potential target for antibacterial drug discovery
medicine
-
structures helps to design new inhibitors that target LpxA, antibiotics