InterPro : IPR000846

Name  Dihydrodipicolinate reductase, N-terminal Short Name  DapB_N
Type  Domain Description  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 [, , ].In Escherichia coliand Mycobacterium tuberculosis, dihydrodipicolinate reductase has equal specificity for NADH and NADPH, however in Thermotoga maritimathere it has a greater affinity for NADPH []. 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.
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Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

Other

0 Child Features

0 Contains

1 Found In

Id Name Short Name Type
IPR011770 Dihydrodipicolinate reductase, bacterial/plant Dihydrodipicolinate_Rdtase Family

1 Parent Features

Id Name Short Name Type
IPR016040 NAD(P)-binding domain NAD(P)-bd_dom Domain

4 Publications

First Author Title Year Journal Volume Pages
Scapin G Three-dimensional structure of Escherichia coli dihydrodipicolinate reductase. 1995 Biochemistry 34 3502-12
Reddy SG Interaction of pyridine nucleotide substrates with Escherichia coli dihydrodipicolinate reductase: thermodynamic and structural analysis of binary complexes. 1996 Biochemistry 35 13294-302
Scapin G Three-dimensional structure of Escherichia coli dihydrodipicolinate reductase in complex with NADH and the inhibitor 2,6-pyridinedicarboxylate. 1997 Biochemistry 36 15081-8
Pearce FG Characterization of dihydrodipicolinate reductase from Thermotoga maritima reveals evolution of substrate binding kinetics. 2008 J Biochem 143 617-23



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)