EC Number | Cloned (Comment) | Organism |
---|---|---|
4.3.3.7 | wild-type and mutant cloned into plasmid pET-151/D-TOPO and expressed in Escherichia coli BL21 Star (DE3) competent cells | Escherichia coli |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
4.3.3.7 | K161A | substantially diminished binding affinity of pyruvate, the surrounding active site scaffold is unable to compensate the entropic penalty associated with ligand localisation in the absence of Schiff-base formation | Escherichia coli |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
4.3.3.7 | L-aspartate 4-semialdehyde | competitive inhibition at high substrate concentrations | Escherichia coli | |
4.3.3.7 | L-lysine | binding interaction of L-lysine is characterised as a cooperative event in which an entropic pre-organisation step precedes a secondary enthalpic association. This allosteric association is of a mixed competitive nature in which heterotropic ligand cooperativity is observed to subtly influence the binding events | Escherichia coli | |
4.3.3.7 | additional information | is insensitive to L-lysine inhibition, produces no binding isotherm upon L-lysine addition in either the absence or presence of pyruvate | Thermotoga maritima | |
4.3.3.7 | NaBH4 | NaBH4 reduction of the pyruvyl-Schiff-base intermediate results in enzyme inactivation | Escherichia coli |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
4.3.3.7 | Escherichia coli | P0A6L2 | - |
- |
4.3.3.7 | Thermotoga maritima | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
4.3.3.7 | - |
Escherichia coli |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.3.3.7 | L-aspartate 4-semialdehyde + pyruvate | pyruvate is a weak binder (0.023 mM) and L-aspartate 4-semialdehyde does not interact with the enzyme in the absence of a Schiff-base with pyruvate. Lys161 plays a crucial role in providing the thermodynamic force for the association of pyruvate with the DHDPS active site | Escherichia coli | dihydrodipicolinate + 2 H2O | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
4.3.3.7 | DHDPS | - |
Thermotoga maritima |
4.3.3.7 | DHDPS | - |
Escherichia coli |
4.3.3.7 | dihydrodipicolinate synthase | - |
Thermotoga maritima |
4.3.3.7 | dihydrodipicolinate synthase | - |
Escherichia coli |