InterPro domain: IPR022663

Dihydrodipicolinate reductase catalyzes the second step in the biosynthesis of diaminopimelic acid and lysine, the NAD or NADP-dependent reduction of 2,3-dihydrodipicolinate into 2,3,4,5-tetrahydrodipicolinate [ 1 , 2 , 3 ].

In Escherichia coli and Mycobacterium tuberculosis, dihydrodipicolinate reductase has equal specificity for NADH and NADPH, however in Thermotoga maritima there it has a greater affinity for NADPH [ 4 ]. In addition, the enzyme is inhibited by high concentrations of its substrate, which consequently acts as a feedback control on the lysine biosynthesis pathway. In T. maritima, the enzyme also lacks N-terminal and C-terminal loops which are present in enzyme of the former two organisms.

This entry represents the C-terminal region of Dihydrodipicolinate reductase.

1. Interaction of pyridine nucleotide substrates with Escherichia coli dihydrodipicolinate reductase: thermodynamic and structural analysis of binary complexes. Biochemistry 35, 13294-302
2. Three-dimensional structure of Escherichia coli dihydrodipicolinate reductase in complex with NADH and the inhibitor 2,6-pyridinedicarboxylate. Biochemistry 36, 15081-8
3. Three-dimensional structure of Escherichia coli dihydrodipicolinate reductase. Biochemistry 34, 3502-12
4. Characterization of dihydrodipicolinate reductase from Thermotoga maritima reveals evolution of substrate binding kinetics. J. Biochem. 143, 617-23