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
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left-handed
- acyl-acp
- endotoxin
- 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
- 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
ECTree
2.3.1.129 acyl-[acyl-carrier-protein]-UDP-N-acetylglucosamine O-acyltransferaseAdvanced search results
results (
results (Engineering
Engineering on EC 2.3.1.129 - acyl-[acyl-carrier-protein]-UDP-N-acetylglucosamine O-acyltransferase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
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
H125A
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
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
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
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
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
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
I56R
mutation in the hydrophobic core of the beta-helical domain: LpxA activity is completely abolished compared to wild-type
I56R
mutation in the hydrophobic residue in the beta-helical core located in rung 4: LpxA is inactive
I86R
mutation in the hydrophobic residue in the beta-helical core located in rung 5: LpxA is inactive
I86R
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
additional information
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
additional information
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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
additional information
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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
additional information
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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
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
additional information
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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
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