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Literature summary for 2.7.2.4 extracted from

  • Chen, Z.; Rappert, S.; Sun, J.; Zeng, A.P.
    Integrating molecular dynamics and co-evolutionary analysis for reliable target prediction and deregulation of the allosteric inhibition of aspartokinase for amino acid production (2011), J. Biotechnol., 154, 248-254.
    View publication on PubMed
Search for more literature for 2.7.2.4

Protein Variants

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

Inhibitors Comment Organism Structure
L-lysine
-
 Escherichia coli
L-threonine
-
 Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-aspartate
-
 Escherichia coli ADP + 4-phospho-L-aspartate
-
 ?

Synonyms

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Escherichia coli