Literature summary extracted from
Li, C.C.; Yang, M.J.; Liu, L.; Li, T.; Peng, C.T.; He, L.H.; Song, Y.J.; Zhu, Y.B.; Shen, Y.L.; Yang, J.; Zhao, N.L.; Zhao, C.; Zhou, Q.X.; Li, H.; Kang, M.; Tong, A.P.; Tang, H.; Bao, R.
Mechanistic insights into the allosteric regulation of Pseudomonas aeruginosa aspartate kinase (2018), Biochem. J., 475, 1107-1119 .
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
2.7.2.4 |
expressed in Escherichia coli BL21(DE3) cells |
Pseudomonas aeruginosa |
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
2.7.2.4 |
hanging drop vapor diffusion method, using 0.4 M ammonium sulfate, 0.1 M sodium citrate tribasic dihydrate (pH 5.6) and 0.9 M lithium sulfate monohydrate |
Pseudomonas aeruginosa |
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
2.7.2.4 |
D182/R184A |
the mutations decrease the enzyme activities to about 65% |
Pseudomonas aeruginosa |
2.7.2.4 |
G152L |
the mutant shows about 35% activity compared to the wild type enzyme |
Pseudomonas aeruginosa |
2.7.2.4 |
H399A |
the mutant shows wild type activity |
Pseudomonas aeruginosa |
2.7.2.4 |
N371A/I372A |
the mutations do not affect the ATP binding with threonine |
Pseudomonas aeruginosa |
2.7.2.4 |
R150A |
the mutant shows about 30% activity compared to the wild type enzyme |
Pseudomonas aeruginosa |
2.7.2.4 |
S12C/S231C |
the mutant shows wild type activity |
Pseudomonas aeruginosa |
2.7.2.4 |
S378A/E202A |
the mutant shows slightly increased activity (about 108%) compared to the wild type enzyme |
Pseudomonas aeruginosa |
2.7.2.4 |
S378A/E202A |
the mutations do not affect the ATP binding with threonine |
Pseudomonas aeruginosa |
2.7.2.4 |
V357/M351A |
the mutant shows reduced activity compared to the wild type enzyme |
Pseudomonas aeruginosa |
Inhibitors
EC Number |
Inhibitors |
Comment |
Organism |
Structure |
---|
2.7.2.4 |
lysine |
- |
Pseudomonas aeruginosa |
|
2.7.2.4 |
threonine |
- |
Pseudomonas aeruginosa |
|
Metals/Ions
EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
---|
2.7.2.4 |
Mg2+ |
10 mM used in assay conditions |
Pseudomonas aeruginosa |
|
Natural Substrates/ Products (Substrates)
EC Number |
Natural Substrates |
Organism |
Comment (Nat. Sub.) |
Natural Products |
Comment (Nat. Pro.) |
Rev. |
Reac. |
---|
2.7.2.4 |
ATP + L-aspartate |
Pseudomonas aeruginosa |
- |
ADP + 4-phospho-L-aspartate |
- |
? |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
2.7.2.4 |
Pseudomonas aeruginosa |
O69077 |
- |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
2.7.2.4 |
Ni-NTA resin column chromatography and Superdex 200 gel filtration |
Pseudomonas aeruginosa |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
2.7.2.4 |
ATP + L-aspartate |
- |
Pseudomonas aeruginosa |
ADP + 4-phospho-L-aspartate |
- |
? |
|
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
2.7.2.4 |
heterotetramer |
x-ray crystallography |
Pseudomonas aeruginosa |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
2.7.2.4 |
aspartokinase |
- |
Pseudomonas aeruginosa |
2.7.2.4 |
lysC |
- |
Pseudomonas aeruginosa |