Cloned (Comment) | Organism |
---|---|
expressed in Escherichia coli STBL2, pET23b vector | Corynebacterium glutamicum |
Crystallization (Comment) | Organism |
---|---|
hanging drop method, data collection and refinement statistics, refinement resolution originally extended to 3.0 A, gradually increased to 2.5 A, and finally to 2.2 A, structural similarities to other dihydrodipicolinate synthase | Corynebacterium glutamicum |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
3-Bromopyruvate | competitive inhibition, pyruvate as varied substrate | Corynebacterium glutamicum | |
L-aspartate | competitive inhibition, L-aspartate 4-semialdehyde as varied substrate | Corynebacterium glutamicum | |
L-aspartate 4-semialdehyde | uncompetitive inhibition by high concentrations of, no overcome by increasing pyruvate concentrations from 5 to 15 mM | Corynebacterium glutamicum | |
L-lysine | lack of feedback inhibition, not regulated under normal physiological conditions | Corynebacterium glutamicum | |
oxaloacetate | non-competitive inhibition, pyruvate as varied substrate | Corynebacterium glutamicum | |
Succinic semialdehyde | uncompetitive inhibition, L-aspartate 4-semialdehyde as varied substrate | Corynebacterium glutamicum |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.32 | - |
pyruvate | 2.5 mM pyruvate replaced by 0.1-2 mM, no substrate inhibition observed at high concentrations of pyruvate | Corynebacterium glutamicum | |
0.63 | - |
L-aspartate 4-semialdehyde | reaction mixture includes 100 mM Tris-HCl, 2.5 mM pyruvate, 0.05-0.1 microg dihydrodipicolinate synthase and 0.2 mM NADPH, from 5.6 to 22.4 mM plots deviate from typical Michaelis-Menten kinetics, increased concentration fits an uncompetitive substrate inhibition model | Corynebacterium glutamicum |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
73000 | - |
approximating the size of two DHDPS proteins interacting to form a dimer | Corynebacterium glutamicum |
158000 | - |
native protein, gel filtration, homotetramer predicted | Corynebacterium glutamicum |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Corynebacterium glutamicum | P19808 | - |
- |
Purification (Comment) | Organism |
---|---|
gel filtration, SDS-PAGE | Corynebacterium glutamicum |
Source Tissue | Comment | Organism | Textmining |
---|
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
structure in vicinity of the putative binding site for S-lysine indicates that the allosteric binding site in the Escherichia coli dihydrodipicolinate synthase does not exist in the enzyme of Corynebacterium glutamicum, difference of three non-conservative amino acids substitutions, explains lack of feedback inhibition by lysine in Corynebacterium glutamicum | Corynebacterium glutamicum |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-aspartate 4-semialdehyde + pyruvate | lysine insensitivity of dihydrodipicolinate synthase analyzed, catalytic lysine residue forms a Schiff base adduct with pyruvate, active site lysine residues (K176a, K176b) | Corynebacterium glutamicum | dihydrodipicolinate + H2O | - |
? |
Subunits | Comment | Organism |
---|---|---|
homotetramer | ribbons rendition of homotetramer in the crystal lattice shown | Corynebacterium glutamicum |
Synonyms | Comment | Organism |
---|---|---|
cDHDPS | - |
Corynebacterium glutamicum |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
213 | - |
L-aspartate 4-semialdehyde | - |
Corynebacterium glutamicum |
IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
---|---|---|---|---|---|
660 | - |
5 mM pyruvate, addition of 0-716 mM lysine, lack of feedback inhibition | Corynebacterium glutamicum | L-lysine |