Cloned (Comment) | Organism |
---|---|
gene dapA, expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) | Vitis vinifera |
Crystallization (Comment) | Organism |
---|---|
purified recombinant His-tagged enzyme, hanging drop vapor diffusion method, mixing of 0.002 ml of protein in 20 mM pyruvate and 20 mM lysine, with 0.002 ml of reservoir solution containing 0.1 M MES, pH 6.5, 6% v/v PEG 20000, X-ray diffraction structure determination and analysis at 2.40 A resolution | Vitis vinifera |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
L-lysine | feedback inhibition, binding of lysine to the allosteric cleft of the enzyme, cooperative binding, structural mechanism for allosteric inhibition, overview. With respect to L-aspartate-4-semialdehyde, lysine is a noncompetitive inhibitor | Vitis vinifera |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | Michaelis-Menten kinetics | Vitis vinifera |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
pyruvate + L-aspartate-4-semialdehyde | Vitis vinifera | - |
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H2O | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Vitis vinifera | D7U7T8 | gene dapA | - |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by metal affinity chromatography | Vitis vinifera |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
pyruvate + L-aspartate-4-semialdehyde = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H2O | the reaction proceeds via a ping-pong kinetic mechanism in which pyruvate binds and forms a Schiff base to an active-site lysine residue (Lys184 in Vitis vinifera enzyme). L-aspartate-4-semialdehyde then reacts with the resultant enamine and following cyclization forms the product (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate | Vitis vinifera |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | coupled assay with dihydrodipicolinate reductase | Vitis vinifera | ? | - |
? | |
pyruvate + L-aspartate-4-semialdehyde | - |
Vitis vinifera | (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H2O | - |
? |
Subunits | Comment | Organism |
---|---|---|
homotetramer | homotetramer of four identical (beta/alpha)8-barrel monomers, a dimer of tight dimers, with two tight-dimers binding in a head-to-head manner, with the active site situated near the center of the barrel, molecular dynamics simulations | Vitis vinifera |
Synonyms | Comment | Organism |
---|---|---|
DHDPS | - |
Vitis vinifera |
dihydrodipicolinate synthase | - |
Vitis vinifera |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Vitis vinifera |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Vitis vinifera |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | kinetic and thermodynamics of allosteric inhibitin by lysine, overview | Vitis vinifera | |
0.049 | - |
L-lysine | versus L-aspartate-4-semialdehyde, pH 8.0, 30°C, recombinant enzyme | Vitis vinifera |
General Information | Comment | Organism |
---|---|---|
metabolism | lysine biosynthesis in plants is tightly regulated by feedback inhibition of the end product on dihydrodipicolinate synthase, the first enzyme of the lysine-specific branch | Vitis vinifera |