Protein Variants | Comment | Organism |
---|---|---|
C428R | mutation is not directly involved in L-lysine binding. Mutation located within regulatory domain, participates in the allosteric regulation within regulatory domain. Mutation greatly reduces L-lysine inhibition | Escherichia coli |
E346A | mutation reduces feedback-inhibition of AK1 by L-threonine without significant change in enzymatic activity | Escherichia coli |
E346R | mutation within L-lysine binding site desensitizes AK3 from L-lysine inhibition. Mutant shows reduced L-lysine inhibition | Escherichia coli |
F329R | mutation is not directly involved in L-lysine binding. Mutation located within regulatory domain, participates in the allosteric regulation within regulatory domain. Mutation greatly reduces L-lysine inhibition | Escherichia coli |
G323D | mutation within L-lysine binding site desensitizes AK3 from L-lysine inhibition. Mutant shows reduced L-lysine inhibition | Escherichia coli |
H320A | mutation is not directly involved in L-lysine binding. Mutation located within regulatory domain, participates in the allosteric regulation within regulatory domain. Mutation greatly reduces L-lysine inhibition | Escherichia coli |
I337P | mutation is not directly involved in L-lysine binding. Mutation located within regulatory domain, participates in the allosteric regulation within regulatory domain. Mutation greatly reduces L-lysine inhibition | Escherichia coli |
I344P | mutation reduces feedback-inhibition of AK1 by L-threonine without significant change in enzymatic activity | Escherichia coli |
I427P | mutation reduces feedback-inhibition of AK1 by L-threonine without significant change in enzymatic activity | Escherichia coli |
L325F | mutation within L-lysine binding site desensitizes AK3 from L-lysine inhibition. Mutant shows reduced L-lysine inhibition | Escherichia coli |
M251P | mutation destroys van der Waals interaction significantly which releases L-lysine inhibition | Escherichia coli |
M318I | mutation within L-lysine binding site desensitizes AK3 from L-lysine inhibition. Mutant shows reduced L-lysine inhibition | Escherichia coli |
M417I | mutation is not directly involved in L-lysine binding. Mutation located within regulatory domain, participates in the allosteric regulation within regulatory domain. Mutation greatly reduces L-lysine inhibition | Escherichia coli |
N424A | mutation reduces feedback-inhibition of AK1 by L-threonine without significant change in enzymatic activity | Escherichia coli |
N426A | mutation reduces feedback-inhibition of AK1 by L-threonine without significant change in enzymatic activity | Escherichia coli |
Q351A | mutation reduces feedback-inhibition of AK1 by L-threonine without significant change in enzymatic activity | Escherichia coli |
R305A | mutation destroys van der Waals interaction significantly which releases L-lysine inhibition | Escherichia coli |
R416A | mutation is not directly involved in L-lysine binding. Mutation located within regulatory domain, participates in the allosteric regulation within regulatory domain. Mutation greatly reduces L-lysine inhibition | Escherichia coli |
S315A | mutation is not directly involved in L-lysine binding. Mutation located within regulatory domain, participates in the allosteric regulation within regulatory domain. Mutation greatly reduces L-lysine inhibition | Escherichia coli |
S338L | mutation within L-lysine binding site desensitizes AK3 from L-lysine inhibition. Mutant shows reduced L-lysine inhibition | Escherichia coli |
S345L | mutation within L-lysine binding site desensitizes AK3 from L-lysine inhibition. Mutant shows reduced L-lysine inhibition | Escherichia coli |
T253R | mutation leads to repulse interaction with Arg305 which destroys the allosteric regulation by L-lysine | Escherichia coli |
T344M | mutation is not directly involved in L-lysine binding. Mutation located within regulatory domain, participates in the allosteric regulation within regulatory domain. Mutation greatly reduces L-lysine inhibition | Escherichia coli |
T352I | mutation is not directly involved in L-lysine binding. Mutation located within regulatory domain, participates in the allosteric regulation within regulatory domain. Mutation greatly reduces L-lysine inhibition | Escherichia coli |
V339A | mutation within L-lysine binding site desensitizes AK3 from L-lysine inhibition. Mutant shows reduced L-lysine inhibition | Escherichia coli |
V347M | mutation is not directly involved in L-lysine binding. Mutation located within regulatory domain, participates in the allosteric regulation within regulatory domain. Mutation greatly reduces L-lysine inhibition | Escherichia coli |
V349M | mutation is not directly involved in L-lysine binding. Mutation located within regulatory domain, participates in the allosteric regulation within regulatory domain. Mutation greatly reduces L-lysine inhibition | Escherichia coli |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
L-lysine | - |
Escherichia coli | |
L-threonine | - |
Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-aspartate | - |
Escherichia coli | ADP + 4-phospho-L-aspartate | - |
? |
Synonyms | Comment | Organism |
---|---|---|
AK1 | - |
Escherichia coli |
AK3 | - |
Escherichia coli |
aspartokinase I | - |
Escherichia coli |
aspartokinase III | - |
Escherichia coli |
lysC | - |
Escherichia coli |
thrA | - |
Escherichia coli |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Escherichia coli |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Escherichia coli |