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Literature summary 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

Protein Variants

EC Number Protein Variants Comment Organism
2.7.2.4 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
2.7.2.4 E346A mutation reduces feedback-inhibition of AK1 by L-threonine without significant change in enzymatic activity Escherichia coli
2.7.2.4 E346R mutation within L-lysine binding site desensitizes AK3 from L-lysine inhibition. Mutant shows reduced L-lysine inhibition Escherichia coli
2.7.2.4 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
2.7.2.4 G323D mutation within L-lysine binding site desensitizes AK3 from L-lysine inhibition. Mutant shows reduced L-lysine inhibition Escherichia coli
2.7.2.4 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
2.7.2.4 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
2.7.2.4 I344P mutation reduces feedback-inhibition of AK1 by L-threonine without significant change in enzymatic activity Escherichia coli
2.7.2.4 I427P mutation reduces feedback-inhibition of AK1 by L-threonine without significant change in enzymatic activity Escherichia coli
2.7.2.4 L325F mutation within L-lysine binding site desensitizes AK3 from L-lysine inhibition. Mutant shows reduced L-lysine inhibition Escherichia coli
2.7.2.4 M251P mutation destroys van der Waals interaction significantly which releases L-lysine inhibition Escherichia coli
2.7.2.4 M318I mutation within L-lysine binding site desensitizes AK3 from L-lysine inhibition. Mutant shows reduced L-lysine inhibition Escherichia coli
2.7.2.4 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
2.7.2.4 N424A mutation reduces feedback-inhibition of AK1 by L-threonine without significant change in enzymatic activity Escherichia coli
2.7.2.4 N426A mutation reduces feedback-inhibition of AK1 by L-threonine without significant change in enzymatic activity Escherichia coli
2.7.2.4 Q351A mutation reduces feedback-inhibition of AK1 by L-threonine without significant change in enzymatic activity Escherichia coli
2.7.2.4 R305A mutation destroys van der Waals interaction significantly which releases L-lysine inhibition Escherichia coli
2.7.2.4 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
2.7.2.4 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
2.7.2.4 S338L mutation within L-lysine binding site desensitizes AK3 from L-lysine inhibition. Mutant shows reduced L-lysine inhibition Escherichia coli
2.7.2.4 S345L mutation within L-lysine binding site desensitizes AK3 from L-lysine inhibition. Mutant shows reduced L-lysine inhibition Escherichia coli
2.7.2.4 T253R mutation leads to repulse interaction with Arg305 which destroys the allosteric regulation by L-lysine Escherichia coli
2.7.2.4 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
2.7.2.4 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
2.7.2.4 V339A mutation within L-lysine binding site desensitizes AK3 from L-lysine inhibition. Mutant shows reduced L-lysine inhibition Escherichia coli
2.7.2.4 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
2.7.2.4 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

EC Number Inhibitors Comment Organism Structure
2.7.2.4 L-lysine
-
 Escherichia coli
2.7.2.4 L-threonine
-
 Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
2.7.2.4 Escherichia coli
-
-
-

Substrates and Products (Substrate)

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

Synonyms

EC Number Synonyms Comment Organism
2.7.2.4 AK1
-
 Escherichia coli
2.7.2.4 AK3
-
 Escherichia coli
2.7.2.4 aspartokinase I
-
 Escherichia coli
2.7.2.4 aspartokinase III
-
 Escherichia coli
2.7.2.4 lysC
-
 Escherichia coli
2.7.2.4 thrA
-
 Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.2.4 30
-
 assay at Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.2.4 7.5
-
 assay at Escherichia coli