Literature summary extracted from
Yoshida, A.; Tomita, T.; Kuzuyama, T.; Nishiyama, M.
Mechanism of concerted inhibition of alpha2beta2-type hetero-oligomeric aspartate kinase from Corynebacterium glutamicum (2010), J. Biol. Chem., 285, 27477-27486.
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
2.7.2.4 |
expressed in Escherichia coli as a His-tagged fusion protein |
Corynebacterium glutamicum |
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
2.7.2.4 |
D45A |
the inhibition of CgAK by lysine is substantially reduced in D45A mutant |
Corynebacterium glutamicum |
2.7.2.4 |
S301F |
the S301F mutant exhibits resistance to feedback inhibition by lysine and threonine, showing activity in the presence of both lysine and threonine |
Corynebacterium glutamicum |
Inhibitors
EC Number |
Inhibitors |
Comment |
Organism |
Structure |
---|
2.7.2.4 |
L-lysine |
enzyme is inhibited by lysine and threonine in a concerted manner: comparison of the crystal structures between inhibitory and active forms reveal that binding inhibitors causes a conformational change to a closed inhibitory form, and the interaction between the catalytic domain in the alpha subunit and beta subunit |
Corynebacterium glutamicum |
|
2.7.2.4 |
L-threonine |
enzyme is inhibited by lysine and threonine in a concerted manner: comparison of the crystal structures between inhibitory and active forms reveal that binding inhibitors causes a conformational change to a closed inhibitory form, and the interaction between the catalytic domain in the alpha subunit and beta subunit |
Corynebacterium glutamicum |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
2.7.2.4 |
Corynebacterium glutamicum |
- |
- |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
2.7.2.4 |
using Ni-NTA chromatography |
Corynebacterium glutamicum |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
2.7.2.4 |
ATP + L-aspartate |
- |
Corynebacterium glutamicum |
ADP + 4-phospho-L-aspartate |
- |
? |
|
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
2.7.2.4 |
heterotetramer |
crystal structure, heterotetramer composed of two alpha subunits and two beta subunits |
Corynebacterium glutamicum |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
2.7.2.4 |
CgAK |
- |
Corynebacterium glutamicum |
Temperature Optimum [°C]
EC Number |
Temperature Optimum [°C] |
Temperature Optimum Maximum [°C] |
Comment |
Organism |
---|
2.7.2.4 |
30 |
- |
assay at |
Corynebacterium glutamicum |
pH Optimum
EC Number |
pH Optimum Minimum |
pH Optimum Maximum |
Comment |
Organism |
---|
2.7.2.4 |
7.5 |
- |
assay at |
Corynebacterium glutamicum |