EC Number   |
General Information |
Reference |
|---|
    1.17.1.8 | metabolism |
DHDPR catalyzes the NADH/NADPH-dependent second step of the lysine-biosynthesis pathway in bacteria and plants |
-, 710760 |
| 1.17.1.8 | metabolism |
DHDPR is central to the diaminopimelate pathway for lysine biosynthesis |
712704 |
| 1.17.1.8 | 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 |
696300 |
| 1.17.1.8 | metabolism |
the enzyme belongs to the L-lysine biosynthetic pathway |
-, 721156 |
| 1.17.1.8 | metabolism |
the enzyme catalyses the second reaction in the diaminopimelate pathway of lysine biosynthesis in bacteria and plants |
744277 |
| 1.17.1.8 | metabolism |
the enzyme catalyzes the second committed step in the diaminopimelate/lysine anabolic pathways |
-, 743963 |
| 1.17.1.8 | metabolism |
the enzyme catalyzes the second step of the lysine biosynthesis pathway |
-, 723702 |
| 1.17.1.8 | metabolism |
the enzyme is involved in L-lysine biosynthesis |
-, 745538 |
| 1.17.1.8 | more |
NMR studies uncover that dihydrodipicolinate reductase is also a dehydratase, overview |
712704 |
| 1.17.1.8 | physiological function |
Brucellae are intracellular bacterial pathogens that cause Brucellosis. Earlier immune response plays an important role in the Brucella infection. The dihydrodipicolinate reductase protein could induce Th1 and Th2-type immune responses in vivo and in vitro |
-, 746555 |
