Activating Compound | Comment | Organism | Structure |
---|---|---|---|
NADH | - |
Escherichia coli | |
NADPH | similar affinity as NADH | Escherichia coli |
Application | Comment | Organism |
---|---|---|
drug development | enzyme is a potential target for new antimicrobial and herbicidal compounds | Escherichia coli |
Cloned (Comment) | Organism |
---|---|
expressed in Escherichia coli (BL21) | Escherichia coli |
expression of pET11a expression construct in Escherichia coli (BL21) | Escherichia coli |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
2,6-pyridine dicarboxylate | stable analog of the dihydrodipicolinate substrate, the binding affinity is not affected by the presence of NADH or NAD+ | Escherichia coli | |
catechol rhodanine acetic acid | binds to the NADH cofactor site | Escherichia coli |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
28000 | - |
SDS-PAGE | Escherichia coli |
28820 | - |
by MALDI-TOF mass spectrometry | Escherichia coli |
28820 | - |
MALDI-TOF, 28756 Da expected | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
2,3-dihydrodipicolinate + NAD(P)H | Escherichia coli | enzyme is a part of the biosynthetic pathway leading to meso-diaminopimelic acid and L-lysine in bacteria and higher plants | 2,3,4,5-tetrahydrodipicolinate + NAD(P)+ | - |
? | |
dihydrodipicolinate + NADH + H+ | Escherichia coli | substrate dihydrodipicolinate is instable | tetrahydrodipicolinate + NAD+ | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Purification (Comment) | Organism |
---|---|
cells grown in M9 medium containing 2H, 15N, and 13C-labeled sources, collected, lysed, and protein purified with a QA52 anion exchange column and a Blue Trisacryl affinity column with gravity gradient chromatography, fractions with activity pooled and concentrated using an Amicon ultrafiltration device with YM10 membrane, desalted and loaded onto the Blue Trisacryl affinity column and eluted with a linear gradient of 0-2 M NaCl, 25 mM Tris buffer, pH 7.5, pooled, concentrated and buffer ecxchanged | Escherichia coli |
protein is purified using a QA52 anion exchange column and a Blue Trisacryl affinity column with gravity gradient chromatography | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2,3-dihydrodipicolinate + NAD(P)H | enzyme is a part of the biosynthetic pathway leading to meso-diaminopimelic acid and L-lysine in bacteria and higher plants | Escherichia coli | 2,3,4,5-tetrahydrodipicolinate + NAD(P)+ | - |
? | |
dihydrodipicolinate + NADH + H+ | substrate dihydrodipicolinate is instable | Escherichia coli | tetrahydrodipicolinate + NAD+ | - |
? | |
pyridine dicarboxylate + NADH + H+ | stable substrate analog, 25 mM phosphate D2O (deuterium water) buffer, pH 7.8 for NMR analysis of binding interactions with saturation transfer difference titration studies at 298 K (25°C) | Escherichia coli | reduced pyridine dicarboxylate + NAD+ | - |
? |
Subunits | Comment | Organism |
---|---|---|
homotetramer | native state | Escherichia coli |
Synonyms | Comment | Organism |
---|---|---|
DHPR | - |
Escherichia coli |
dihydrodipicolinate reductase | - |
Escherichia coli |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADH | dihydrodipicolinate reductase activity requires NADH binding at only one of the four monomers | Escherichia coli | |
NADPH | - |
Escherichia coli |
General Information | Comment | Organism |
---|---|---|
metabolism | part of the biosynthetic pathway leading to meso-diaminopimelic acid and L-lysine, only NADH binding at one of the 4 monomers is required to activate the dihydrodipicolinate reductase, a model of sequential conformational change in each monomer upon NADH binding is proposed | Escherichia coli |