Any feedback?
Literature summary extracted from
- Exploring the allosteric mechanism of dihydrodipicolinate synthase by reverse engineering of the allosteric inhibitor binding sites and its application for lysine production (2012), Appl. Microbiol. Biotechnol., 97, 1963-1971.
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.3.3.7 | L-lysine | mutagenesis of the lysine binding sites of the Corynebacterium glutamicum enzyme according to the residues in the Escherichia coli enzyme does not conver the expected feedback inhibition but an activation of the enzyme by L-lysine | Corynebacterium glutamicum |  |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 4.3.3.7 | gene dapA, expression of wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3) | Corynebacterium glutamicum |
| 4.3.3.7 | gene dapA, recombinant expression of lysine-insensitive mutants in Escherichia coli strain MG1655 with a yield improved by 46% compared to the wild-type enzyme | Escherichia coli |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 4.3.3.7 | A49K | site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme | Escherichia coli |
| 4.3.3.7 | A49P | site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme and is still sensitive to L-lysine | Escherichia coli |
| 4.3.3.7 | A49W | site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme | Escherichia coli |
| 4.3.3.7 | E84T | site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme and is insensitive to L-lysine | Escherichia coli |
| 4.3.3.7 | H56K | site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme and is insensitive to L-lysine | Escherichia coli |
| 4.3.3.7 | K68H | site-directed mutagenesis, the mutant is not inhibited by L-lysine | Corynebacterium glutamicum |
| 4.3.3.7 | L51K | site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme | Escherichia coli |
| 4.3.3.7 | L51T | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme and is sill sensitive to L-lysine | Escherichia coli |
| 4.3.3.7 | additional information | feedback inhibition of the Escherichia coli enzyme by lysine is successfully alleviated after substitution of the residues around the inhibitor's binding sites with those of the Corynabacterium glutamicum enzyme | Escherichia coli |
| 4.3.3.7 | additional information | mutagenesis of the lysine binding sites of the Corynebacterium glutamicum enzyme according to the residues in the Escherichia coli enzyme does not conver the expected feedback inhibition but an activation of the nezyme by L-lysine | Corynebacterium glutamicum |
| 4.3.3.7 | P61A/T63L | site-directed mutagenesis, the mutant is not inhibited by L-lysine | Corynebacterium glutamicum |
| 4.3.3.7 | P61A/T63L/A65H | site-directed mutagenesis, the mutant is not inhibited by L-lysine | Corynebacterium glutamicum |
| 4.3.3.7 | T63L | site-directed mutagenesis, the mutant is not inhibited by L-lysine | Corynebacterium glutamicum |
| 4.3.3.7 | T92E | site-directed mutagenesis, the mutant is not inhibited by L-lysine | Corynebacterium glutamicum |
| 4.3.3.7 | T96E | site-directed mutagenesis, the mutant is not inhibited by L-lysine and shows reduced activity compared to the wild-type enzyme | Corynebacterium glutamicum |
| 4.3.3.7 | T96E/K68H | site-directed mutagenesis, the mutant is not inhibited by L-lysine and shows reduced activity compared to the wild-type enzyme | Corynebacterium glutamicum |
| 4.3.3.7 | T96E/K68H/P61A/T63L | site-directed mutagenesis, the mutant is activated by L-lysine 3fold shows reduced activity compared to the wild-type enzyme | Corynebacterium glutamicum |
| 4.3.3.7 | T96E/K68H/P61A/T63L/A65H | site-directed mutagenesis the mutant is activated by L-lysine 5fold shows reduced activity compared to the wild-type enzyme | Corynebacterium glutamicum |
| 4.3.3.7 | T96E/K68H/T63L | site-directed mutagenesis, the mutant is activated by L-lysine and shows reduced activity compared to the wild-type enzyme | Corynebacterium glutamicum |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.3.3.7 | (S)-lysine | feedback inhibition, feedback inhibition of the Escherichia coli enzyme by lysine is successfully alleviated after substitution of the residues around the inhibitor's binding sites with those of the Corynabacterium glutamicum enzyme | Escherichia coli | |
| 4.3.3.7 | additional information | no feedback inhibition by L-lysine | Corynebacterium glutamicum |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 4.3.3.7 | 0.137 | - |
(S)-aspartate-4-semialdehyde | recombinant mutant H56K, pH 8.0, temperature not specified in the publication | Escherichia coli | |
| 4.3.3.7 | 0.248 | - |
(S)-aspartate-4-semialdehyde | recombinant mutant E84T, pH 8.0, temperature not specified in the publication | Escherichia coli | |
| 4.3.3.7 | 0.3 | - |
(S)-aspartate-4-semialdehyde | recombinant wild-type enzyme, pH 8.0, temperature not specified in the publication | Escherichia coli | |
| 4.3.3.7 | 0.556 | - |
pyruvate | recombinant mutant E84T, pH 8.0, temperature not specified in the publication | Escherichia coli | |
| 4.3.3.7 | 0.64 | - |
pyruvate | recombinant mutant H56K, pH 8.0, temperature not specified in the publication | Escherichia coli | |
| 4.3.3.7 | 0.827 | - |
pyruvate | recombinant wild-type enzyme, pH 8.0, temperature not specified in the publication | Escherichia coli | |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.3.3.7 | (S)-aspartate-4-semialdehyde + pyruvate | Escherichia coli | - |
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid + H2O | - |
? | |
| 4.3.3.7 | (S)-aspartate-4-semialdehyde + pyruvate | Corynebacterium glutamicum | - |
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid + H2O | - |
? | |
| 4.3.3.7 | (S)-aspartate-4-semialdehyde + pyruvate | Corynebacterium glutamicum ATCC 13032 | - |
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid + H2O | - |
? | |
| 4.3.3.7 | (S)-aspartate-4-semialdehyde + pyruvate | Escherichia coli MG1655 | - |
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid + H2O | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.3.3.7 | Corynebacterium glutamicum | - |
gene dapA | - |
| 4.3.3.7 | Corynebacterium glutamicum ATCC 13032 | - |
gene dapA | - |
| 4.3.3.7 | Escherichia coli | - |
gene dapA | - |
| 4.3.3.7 | Escherichia coli MG1655 | - |
gene dapA | - |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 4.3.3.7 | 14.5 | - |
purified recombinant mutant L51K, pH 8.0, temperature not specified in the publication | Escherichia coli |
| 4.3.3.7 | 19.2 | - |
purified recombinant mutant A49K, pH 8.0, temperature not specified in the publication | Escherichia coli |
| 4.3.3.7 | 60.5 | - |
purified recombinant mutant L51T, pH 8.0, temperature not specified in the publication | Escherichia coli |
| 4.3.3.7 | 81.6 | - |
purified recombinant mutant A49W, pH 8.0, temperature not specified in the publication | Escherichia coli |
| 4.3.3.7 | 454.2 | - |
purified recombinant mutant H56K, pH 8.0, temperature not specified in the publication | Escherichia coli |
| 4.3.3.7 | 478.1 | - |
purified recombinant mutant E84T, pH 8.0, temperature not specified in the publication | Escherichia coli |
| 4.3.3.7 | 500.8 | - |
purified recombinant wild-type enzyme, pH 8.0, temperature not specified in the publication | Escherichia coli |
| 4.3.3.7 | 559.4 | - |
purified recombinant mutant A49P, pH 8.0, temperature not specified in the publication | Escherichia coli |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.3.3.7 | (S)-aspartate-4-semialdehyde + pyruvate | - |
Escherichia coli | (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid + H2O | - |
? | |
| 4.3.3.7 | (S)-aspartate-4-semialdehyde + pyruvate | - |
Corynebacterium glutamicum | (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid + H2O | - |
? | |
| 4.3.3.7 | (S)-aspartate-4-semialdehyde + pyruvate | - |
Corynebacterium glutamicum ATCC 13032 | (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid + H2O | - |
? | |
| 4.3.3.7 | (S)-aspartate-4-semialdehyde + pyruvate | - |
Escherichia coli MG1655 | (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid + H2O | - |
? | |
| 4.3.3.7 | additional information | coupled assay with dihydrodipicolinate reductase | Escherichia coli | ? | - |
? | |
| 4.3.3.7 | additional information | coupled assay with dihydrodipicolinate reductase | Escherichia coli MG1655 | ? | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 4.3.3.7 | DHDPS | - |
Escherichia coli |
| 4.3.3.7 | DHDPS | - |
Corynebacterium glutamicum |
| 4.3.3.7 | dihydrodipicolinate synthase | - |
Escherichia coli |
| 4.3.3.7 | dihydrodipicolinate synthase | - |
Corynebacterium glutamicum |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 4.3.3.7 | 8 | - |
assay at | Escherichia coli |
| 4.3.3.7 | 8 | - |
assay at | Corynebacterium glutamicum |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 4.3.3.7 | metabolism | feedback regulation of the enzyme is directly correlated to L-lysine production | Escherichia coli |
| 4.3.3.7 | additional information | structure comparison with the enzyme from Corynebacterium glutamicum | Escherichia coli |
| 4.3.3.7 | additional information | structure comparison with the enzyme from Escherichia coli | Corynebacterium glutamicum |
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