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Literature summary for 1.17.1.8 extracted from

  • Reddy, S.G.; Scapin, G.; Blanchard, J.S.
    Interaction of pyridine nucleotide substrates with Escherichia coli dihydrodipicolinate reductase: Thermodynamic and structural analysis of binary complexes (1996), Biochemistry, 35, 13294-13302.
    View publication on PubMed
Search for more literature for 1.17.1.8

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop vapour diffusion method, crystal structure x-ray analysis and binding study with NADPH, NADH, 3-acetyl-NADH, and reduced nicotinamide hypoxanthine dinucleotide phosphate and other pyridine nucleotide derivatives in complex with the enzyme Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2,3-dihydrodipicolinate + NAD(P)H Escherichia coli
-
 2,3,4,5-tetrahydrodipicolinate + NAD(P)+
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli P04036
-
-

Reaction

Reaction Comment Organism Reaction ID
(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NAD(P)+ + H2O = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NAD(P)H + H+ structure of substrate-cofactor-complex Escherichia coli
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2,3-dihydrodipicolinate + NAD(P)H
-
 Escherichia coli 2,3,4,5-tetrahydrodipicolinate + NAD(P)+
-
 ?

Synonyms

Synonyms Comment Organism
DHPR
-
 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
additional information broad pyridine nucleotide specificity, binding study with NADPH, NADH, 3-acetyl-NADH, and nicotinamide hypoxanthine dinucleotide phosphate reduced and other pyridine nucleotide derivatives Escherichia coli
NADH thermodynamic binding parameters Escherichia coli
NADH twice as effective as NADPH Escherichia coli
NADPH thermodynamic binding parameters Escherichia coli