Dihydrodipicolinate reductase (IPR023940)

Short name: DHDPR_bac

Overlapping homologous superfamilies

Family relationships



Dihydrodipicolinate reductase (DHDPR), a product of an essential gene referred to as dapB, catalyzes the second step of lysine biosynthesis [PMID: 21803042, PMID: 23722845]. It catalyses the reduction of 2,3-dihydrodipicolinate (DHDP) to 2,3,4,5-tetrahydrodipicolinate (THDP) in a nucleotide dependent reaction [PMID: 8993314]:

2,3-dihydrodipicolinate + NAD(P)H = 2,3,4,5-tetrahydrodipicolinate + NAD(P)(+)

Interestingly, DHDPR could also function as a dehydratase in addition to the role of a nucleotide dependent reductase [PMID: 20503968].

The structures of the Escherichia coli (P04036) and Mycobacterium tuberculosis (P72024) enzymes have been determined [PMID: 7893645, PMID: 12962488]. The enzyme is a homotetramer where each monomer is composed of two domains, an N-terminal NAD(P)H-binding domain which forms a Rossman fold, and a C-terminal substrate-binding domain that forms an open, mixed alpha-beta sandwich.Tetramerisation occurs exclusively through interactions between C-terminal domain residues. Both enzymes show relatively little preference for either NADH or NADPH as cofactor. Conformational changes upon substrate binding bring the cofactor and substrate into close proximity and allow catalysis to occur.

As this enzyme is not found in mammals it is a potential target for the development of novel antibacterial and herbicidal compounds.

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.