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Literature summary extracted from

  • Nguyen, L.; Kozlov, G.; Gehring, K.
    Structure of Escherichia coli tetrahydrodipicolinate N-succinyltransferase reveals the role of a conserved C-terminal helix in cooperative substrate binding (2008), FEBS Lett., 582, 623-626.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.117 expressed in Escherichia coli as a His-tagged fusion protein Escherichia coli

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.3.1.117 crystal structure of DapD from Escherichia coli at 2.0 A resolution is shown. Comparison of the structure with the homologous enzyme from Mycobacterium bovis reveals the C-terminal helix undergoes a large rearrangement upon substrate binding, which contributes to cooperativity in substrate binding Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.117 Escherichia coli Q8X8Y7
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.1.117 using Ni-NTA chromatography Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.117 succinyl-CoA + L-2-aminopimelate
-
 Escherichia coli CoA + N-succinyl-L-aminopimelate
-
 ?
2.3.1.117 succinyl-CoA + tetrahydrodipicolinate
-
 Escherichia coli ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.3.1.117 tetrahydrodipicolinate-N-succinyltransferase
-
 Escherichia coli
2.3.1.117 THDP
-
 Escherichia coli