Cloned (Comment) | Organism |
---|---|
expressed in Escherichia coli XL-1 Blue harbouring the plasmid pJG001 | Escherichia coli |
Crystallization (Comment) | Organism |
---|---|
examination of the specificity of the active site of DHDPS, co-crystallization with the substrate analogue oxaloacetate, data-collection and refinement statistics | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
(S)-aspartate 4-semialdehyde + pyruvate | Escherichia coli | - |
dihydrodipicolinate + H2O | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P0A6L2 | - |
- |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
attempt to examine the specificity of the active site of DHDPS, co-crystallization with the substrate analogue oxaloacetate, solution of the protein structure indicates that pyruvate rather than oxaloacetic acid bounds in the active site, decarboxylation of oxaloacetate not catalysed by DHDPS, rate of pyruvate production independent of DHDPS concentration, indicating that the decarboxylation of oxaloacetate is occurring by a spontaneous and enzyme-independent mechanism, confirmed by kinetic analysis | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
(S)-aspartate 4-semialdehyde + pyruvate | - |
Escherichia coli | dihydrodipicolinate + H2O | - |
? | |
(S)-aspartate 4-semialdehyde + pyruvate | biosynthesis of (S)-lysine and meso-diaminopimelate | Escherichia coli | dihydrodipicolinate + H2O | - |
? |
Synonyms | Comment | Organism |
---|---|---|
DHDPS | - |
Escherichia coli |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.6 | - |
assay at, measured using a coupled assay with lactate dehydrogenase to detect pyruvate production | Escherichia coli |