Cloned (Comment) | Organism |
---|---|
expressed in Escherchia coli as a His-tagged fusion protein | Escherichia coli |
Protein Variants | Comment | Organism |
---|---|---|
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 | Escherichia coli |
G52L/R58L | residue tolerance in the beta-helical domain: mutation is tolerated | Escherichia coli |
G52V/R58V | residue tolerance in the beta-helical domain: mutation is tolerated | Escherichia coli |
G52W/R58W | residue tolerance in the beta-helical domain: mutation is tolerated | Escherichia coli |
G57P/N51P | residue tolerance in the beta-helical domain: mutation is not tolerated | Escherichia coli |
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 | Escherichia coli |
H53I/D59I | residue tolerance in the beta-helical domain: mutation is tolerated | Escherichia coli |
H53V/D59V | residue tolerance in the beta-helical domain: mutation is tolerated | Escherichia coli |
I20R | mutation in the hydrophobic residue in the beta-helical core located in rung 2: LpxA is active | Escherichia coli |
I2R | mutation in the hydrophobic residue in the beta-helical core located in rung 1: LpxA is active | Escherichia coli |
I38R | mutation in the hydrophobic residue in the beta-helical core located in rung 3: LpxA is partially active | Escherichia coli |
I56A | mutation in the hydrophobic core of the beta-helical domain: LpxA activity is not significantly affected compared to wild-type | Escherichia coli |
I56D/I62D | residue tolerance in the beta-helical domain: mutation is not tolerated | Escherichia coli |
I56E/I62E | residue tolerance in the beta-helical domain: mutation is not tolerated | Escherichia coli |
I56G | mutation in the hydrophobic core of the beta-helical domain: LpxA activity is decreased compared to wild-type | Escherichia coli |
I56G/I62G | residue tolerance in the beta-helical domain: mutation is tolerated | Escherichia coli |
I56H/I62H | residue tolerance in the beta-helical domain: mutation is not tolerated | Escherichia coli |
I56K/I62K | residue tolerance in the beta-helical domain: mutation is not tolerated | Escherichia coli |
I56N | mutation in the hydrophobic core of the beta-helical domain: LpxA activity is decreased compared to wild-type | Escherichia coli |
I56N/I62N | residue tolerance in the beta-helical domain: mutation is tolerated | Escherichia coli |
I56P/I62P | residue tolerance in the beta-helical domain: mutation is not tolerated | Escherichia coli |
I56Q | mutation in the hydrophobic core of the beta-helical domain: LpxA activity is decreased compared to wild-type | Escherichia coli |
I56Q/I62Q | residue tolerance in the beta-helical domain: mutation is tolerated | Escherichia coli |
I56R | mutation in the hydrophobic core of the beta-helical domain: LpxA activity is completely abolished compared to wild-type | Escherichia coli |
I56R | mutation in the hydrophobic residue in the beta-helical core located in rung 4: LpxA is inactive | Escherichia coli |
I56R/I62R | residue tolerance in the beta-helical domain: mutation is not tolerated | Escherichia coli |
I56S/I62S | residue tolerance in the beta-helical domain: mutation is tolerated | Escherichia coli |
I56W/I62W | residue tolerance in the beta-helical domain: mutation is not tolerated | Escherichia coli |
I56Y/I62Y | residue tolerance in the beta-helical domain: mutation is not tolerated | Escherichia coli |
I86R | mutation in the hydrophobic residue in the beta-helical core located in rung 5: LpxA is inactive | Escherichia coli |
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 | Escherichia coli |
K55D/E61D | residue tolerance in the beta-helical domain: mutation is tolerated | Escherichia coli |
K55P/E61P | residue tolerance in the beta-helical domain: mutation is not tolerated | Escherichia coli |
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 | Escherichia coli |
P10A/P28A/P34A/P183A | proline mutation at the turn region of the beta-helical domain: mutant shows lower activity compared to wild-type | Escherichia coli |
P28A/P34A | proline mutation at the turn region of the beta-helical domain: mutant shows greater activity than the P10A/P28A/P34A/P183A mutant | Escherichia coli |
T54D/N60D | residue tolerance in the beta-helical domain: mutation is not tolerated | Escherichia coli |
T54E/N60E | residue tolerance in the beta-helical domain: mutation is not tolerated | Escherichia coli |
T54G/N60G | residue tolerance in the beta-helical domain: mutation is tolerated | Escherichia coli |
T54H/N60H | residue tolerance in the beta-helical domain: mutation is not tolerated | Escherichia coli |
T54K/N60K | residue tolerance in the beta-helical domain: mutation is not tolerated | Escherichia coli |
T54M/N60M | residue tolerance in the beta-helical domain: mutation is tolerated | Escherichia coli |
T54P/N60P | residue tolerance in the beta-helical domain: mutation is not tolerated | Escherichia coli |
T54Q/N60Q | residue tolerance in the beta-helical domain: mutation is tolerated | Escherichia coli |
T54R/N60R | residue tolerance in the beta-helical domain: mutation is not tolerated | Escherichia coli |
T54W/N60W | residue tolerance in the beta-helical domain: mutation is not tolerated | Escherichia coli |
T54Y/N60Y | residue tolerance in the beta-helical domain: mutation is not tolerated | Escherichia coli |
V111R | mutation in the hydrophobic residue in the beta-helical core located in rung 6: LpxA is inactive | Escherichia coli |
V129R | mutation in the hydrophobic residue in the beta-helical core located in rung 7: LpxA is inactive | Escherichia coli |
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 | Escherichia coli |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
28000 | - |
SDS-PAGE | Escherichia coli |
30000 | - |
SDS-PAGE, 3 * 30000 Da | Escherichia coli |
90000 | - |
gel filtration | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P0A722 | - |
- |
Purification (Comment) | Organism |
---|---|
using Ni-NTA chromatography and gel filtration. Around 15 mg of purified protein is obtained from 1 l of bacterial culture | Escherichia coli |
Subunits | Comment | Organism |
---|---|---|
trimer | SDS-PAGE, 3 * 30000 Da | Escherichia coli |
Synonyms | Comment | Organism |
---|---|---|
LpxA | - |
Escherichia coli |
UDP-N-acetylglucosamine acyltransferase | - |
Escherichia coli |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
folding assay is performed at 30°C | Escherichia coli |