Dihydrodipicolinate reductase, N-terminal (IPR000846)

Short name: DapB_N

Overlapping homologous superfamilies

Domain relationships


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 [PMID: 8873595, PMID: 9398235, PMID: 7893645].

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 [PMID: 18250105]. 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 N-terminal domain of dihydrodipicolinate reductase which binds the dinucleotide NAD(P)H.

GO terms

Biological Process

GO:0009089 lysine biosynthetic process via diaminopimelate
GO:0055114 oxidation-reduction process

Molecular Function

GO:0008839 4-hydroxy-tetrahydrodipicolinate reductase

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.