InterPro domain: IPR011859

This narrow family includes genes from Arabidopsis and Fibrobacter succinogenes (Bacteroides succinogenes) (which probably recieved the gene from a plant via lateral gene transfer). The sequences are distantly related to the dihydrodipicolinate reductases from archaea. In Fibrobacter this gene is the only candidate DHPR in the genome.

Dihydrodipicolinate reductase is an enzyme found in bacteria and higher plants which is involved in the biosynthesis of diaminopimelic acid, a component of bacterial cell walls, and the essential amino acid L-lysine. It catalyses the the reduced pyridine nucleotide-dependent reduction of the alpha,beta-unsaturated cyclic imine, dihydrodipicolinate, to generate tetrahydrodipicolinate as shown below [ 1 ]: 2,3-dihydrodipicolinate + NAD(P)H = 2,3,4,5-tetrahydrodipicolinate + NAD(P)(+) As this enzyme is not found in mammals it is a potential target for the development of novel antibacterial and herbicidal compounds.

1. Reaction mechanism of Escherichia coli dihydrodipicolinate synthase investigated by X-ray crystallography and NMR spectroscopy. Biochemistry 36, 24-33