Literature summary for 2.3.1.129 extracted from

Choi, J.H.; May, B.C.; Govaerts, C.; Cohen, F.E.
Site-directed mutagenesis demonstrates the plasticity of the beta helix: implications for the structure of the misfolded prion protein (2009), Structure, 17, 1014-1023.

Search for more literature for 2.3.1.129

Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherchia coli as a His-tagged fusion protein	Escherichia coli

Protein Variants

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 [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

Organism	UniProt	Comment	Textmining
Escherichia coli	P0A722	-	-

Purification (Commentary)

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

Subunits	Comment	Organism
trimer	SDS-PAGE, 3 * 30000 Da	Escherichia coli

Synonyms

Synonyms	Comment	Organism
LpxA	-	Escherichia coli
UDP-N-acetylglucosamine acyltransferase	-	Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
30	-	folding assay is performed at 30°C	Escherichia coli