EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
4.3.3.7 | 2-oxobutyrate | competitive inhibitor of DHDPS | Escherichia coli | |
4.3.3.7 | 2-oxoglutarate | competitive inhibitor of DHDPS | Escherichia coli | |
4.3.3.7 | 3-Fluoropyruvate | competitive inhibitor of DHDPS, and a competitive substrates | Escherichia coli | |
4.3.3.7 | 3-hydroxypyruvate | competitive inhibitor of DHDPS and a competitive substrate | Escherichia coli | |
4.3.3.7 | Bromopyruvate | is an irreversible inhibitor of DHDPS | Escherichia coli | |
4.3.3.7 | additional information | the substrate specificity of the enzyme, two pyruvate analogues, previously classified as weak competitive inhibitors, are turned over productively by DHDPS, NMR spectroscopy, overview | Escherichia coli |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.17.1.8 | additional information | Escherichia coli | DHDPR accepts (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid as true substrate rather than dihydrodipicolinate, suggesting that DHDPR catalyzes an overall deoxygenation reaction, likely by a dehydratase-reductase route, substrate specificity, overview. A critical role is played by residue His 159 in the catalytic mechanism of DHDPR. Replacement of this residue with an alanine or a glutamine is reported to result in a 150-200fold reduction in catalytic rate as well as a 6fold increase in KM. His 159 has been proposed to act as a general acid during catalysis, providing the proton required after hydride addition. No activity with beta-hydroxypyruvate and 3-fluoropyruvate | ? | - |
? | |
4.3.3.7 | L-aspartate 4-semialdehyde + pyruvate | Escherichia coli | - |
(S)-2,3-dihydropyridine-2,6-dicarboxylate + 2 H2O | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.17.1.8 | Escherichia coli | - |
- |
- |
4.3.3.7 | Escherichia coli | - |
- |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.17.1.8 | additional information | DHDPR accepts (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid as true substrate rather than dihydrodipicolinate, suggesting that DHDPR catalyzes an overall deoxygenation reaction, likely by a dehydratase-reductase route, substrate specificity, overview. A critical role is played by residue His 159 in the catalytic mechanism of DHDPR. Replacement of this residue with an alanine or a glutamine is reported to result in a 150-200fold reduction in catalytic rate as well as a 6fold increase in KM. His 159 has been proposed to act as a general acid during catalysis, providing the proton required after hydride addition. No activity with beta-hydroxypyruvate and 3-fluoropyruvate | Escherichia coli | ? | - |
? | |
4.3.3.7 | L-aspartate 4-semialdehyde + pyruvate | - |
Escherichia coli | (S)-2,3-dihydropyridine-2,6-dicarboxylate + 2 H2O | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.17.1.8 | More | crystal structure modelling and analysis, PDB ID 1ARZ, overview | Escherichia coli |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.17.1.8 | DHDPR | - |
Escherichia coli |
4.3.3.7 | DHDPS | - |
Escherichia coli |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
4.3.3.7 | 23 | - |
assay at | Escherichia coli |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.17.1.8 | 8 | - |
dehydration assay at | Escherichia coli |
4.3.3.7 | 8 | - |
assay at | Escherichia coli |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.17.1.8 | metabolism | DHDPR is central to the diaminopimelate pathway for lysine biosynthesis | Escherichia coli |
1.17.1.8 | additional information | NMR studies uncover that dihydrodipicolinate reductase is also a dehydratase, overview | Escherichia coli |