D
IPR022663

Dihydrodipicolinate reductase, C-terminal

InterPro entry
Short nameDapB_C

Description

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

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.

References

1.Interaction of pyridine nucleotide substrates with Escherichia coli dihydrodipicolinate reductase: thermodynamic and structural analysis of binary complexes. Reddy SG, Scapin G, Blanchard JS. Biochemistry 35, 13294-302, (1996). View articlePMID: 8873595

2.Three-dimensional structure of Escherichia coli dihydrodipicolinate reductase in complex with NADH and the inhibitor 2,6-pyridinedicarboxylate. Scapin G, Reddy SG, Zheng R, Blanchard JS. Biochemistry 36, 15081-8, (1997). View articlePMID: 9398235

3.Three-dimensional structure of Escherichia coli dihydrodipicolinate reductase. Scapin G, Blanchard JS, Sacchettini JC. Biochemistry 34, 3502-12, (1995). View articlePMID: 7893645

4.Characterization of dihydrodipicolinate reductase from Thermotoga maritima reveals evolution of substrate binding kinetics. Pearce FG, Sprissler C, Gerrard JA. J. Biochem. 143, 617-23, (2008). View articlePMID: 18250105

GO terms

Cross References

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