Cloned (Comment) | Organism |
---|---|
gene dapA, expression of His-tagged enzyme in Escherichia coli strain XL1-Blue | Campylobacter jejuni |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
(S)-lysine | feedback inhibition, the tetrameric enzyme has two allosteric sites, each of which binds two molecules of lysine. Lysine binds highly cooperatively, and primarily to the F form of the enzyme during the ping-pong mechanism. (S)-Lysine is an uncompetitive partial inhibitor with respect to its first substrate, pyruvate, and a mixed partial inhibitor with respect to its second substrate, (S)-aspartate-4-semialdehyde | Campylobacter jejuni |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | kinetic modeling | Campylobacter jejuni | |
2.83 | - |
pyruvate | pH and temperature not specified in the publication | Campylobacter jejuni |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
(S)-aspartate-4-semialdehyde + pyruvate | Campylobacter jejuni | - |
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid + H2O | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Campylobacter jejuni | - |
gene dapA | - |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged enzyme from Escherichia coli strain XL1-Blue by nickel affinity chromatography | Campylobacter jejuni |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
pyruvate + L-aspartate-4-semialdehyde = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H2O | ping-pong kinetic reaction mechanism | Campylobacter jejuni |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
(S)-aspartate-4-semialdehyde + pyruvate | - |
Campylobacter jejuni | (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid + H2O | - |
? | |
(S)-aspartate-4-semialdehyde + pyruvate | (S)-aspartate-4-semialdehyde binds cooperatively in the presence of (S)-lysine with an average cooperativity coefficient n = 1.3, and the cooperativity of binding increases at near-KM concentrations of pyruvate with an average cooperativity coefficient n = 1.0 | Campylobacter jejuni | (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid + H2O | - |
? |
Subunits | Comment | Organism |
---|---|---|
homotetramer | - |
Campylobacter jejuni |
Synonyms | Comment | Organism |
---|---|---|
DHDPS | - |
Campylobacter jejuni |
dihydrodipicolinate synthase | - |
Campylobacter jejuni |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | (S)-lysine allosteric inhibition kinetics and mechanism, overview | Campylobacter jejuni |
IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
---|---|---|---|---|---|
0.065 | - |
pH and temperature not specified in the publication | Campylobacter jejuni | (S)-lysine |