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dihydrodipicolinate reductase C-terminal domain-containing protein
Dihydrodipicolinate reductase (DapB) reduces the alpha,beta-unsaturated cyclic imine, dihydro-dipicolinate. This reaction is the second committed step in the biosynthesis of L-lysine and its precursor meso-diaminopimelate, which are critical for both protein and cell wall biosynthesis. The C-terminal domain of DapB has been proposed to be the substrate- binding domain. [1]. 8873595. Interaction of pyridine nucleotide substrates with Escherichia coli dihydrodipicolinate reductase: thermodynamic and structural analysis of binary complexes. Reddy SG, Scapin G, Blanchard JS;. Biochemistry 1996;35:13294-13302. [2]. 9398235. 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 1997;36:15081-15088. [3]. 7893645. Three-dimensional structure of Escherichia coli dihydrodipicolinate reductase. Scapin G, Blanchard JS, Sacchettini JC;. Biochemistry 1995;34:3502-3512. (from Pfam)
Dihydrodipicolinate reductase, N-terminus
Dihydrodipicolinate reductase (DapB) reduces the alpha,beta-unsaturated cyclic imine, dihydro-dipicolinate. This reaction is the second committed step in the biosynthesis of L-lysine and its precursor meso-diaminopimelate, which are critical for both protein and cell wall biosynthesis. The N-terminal domain of DapB binds the dinucleotide NADPH. [1]. 8873595. Interaction of pyridine nucleotide substrates with Escherichia coli dihydrodipicolinate reductase: thermodynamic and structural analysis of binary complexes. Reddy SG, Scapin G, Blanchard JS;. Biochemistry 1996;35:13294-13302. [2]. 9398235. 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 1997;36:15081-15088. [3]. 7893645. Three-dimensional structure of Escherichia coli dihydrodipicolinate reductase. Scapin G, Blanchard JS, Sacchettini JC;. Biochemistry 1995;34:3502-3512. (from Pfam)
4-hydroxy-tetrahydrodipicolinate reductase
4-hydroxy-tetrahydrodipicolinate reductase catalyzes the NAD(P)-dependent conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate in amino acid biosynthesis pathways
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