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Literature summary for 4.3.3.7 extracted from

  • Blickling, S.; Renner, C.; Laber, B.; Pohlenz, H.; Holak, T.; Huber, R.
    Reaction mechanism of Escherichia coli dihydrodipicolinate synthase investigated by X-ray crystallography and NMR spectroscopy (1997), Biochemistry, 36, 24-33.
    View publication on PubMed
Search for more literature for 4.3.3.7

Crystallization (Commentary)

Crystallization (Comment) Organism
complexed with pyruvate, the substrate analogs succinate alpha-semialdehyde and alpa-ketopimelic acid, the inhibitor dipicolinic acid, and the natural feedback inhibitor L-lysine, hanging drop vapor diffusion method, in the presence of beta-octyl glucoside using either potassium phosphate buffer (pH 10) or potassium citrate buffer (pH 7.0) as the precipitant Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
2-oxopimelic acid
-
 Escherichia coli
dipicolinic acid
-
 Escherichia coli
L-lysine natural feedback inhibitor Escherichia coli
Succinate-semialdehyde reversible inhibitor which is competitive with respect to L-aspartate-4-semialdehyde and uncompetitive with respect to pyruvate Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A6L2
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
pyruvate + L-aspartate-4-semialdehyde
-
 Escherichia coli (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H2O
-
 ?

Synonyms

Synonyms Comment Organism
DHDPS
-
 Escherichia coli
dihydrodipicolinate synthase
-
 Escherichia coli
EC 4.2.1.52 formerly Escherichia coli

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.17
-
 2-oxopimelic acid in 50 mM Tris-HCl (pH 8.2), at 22°C Escherichia coli
0.3
-
 Succinate-semialdehyde in 50 mM Tris-HCl (pH 8.2), at 22°C Escherichia coli

General Information

General Information Comment Organism
metabolism first enzyme unique to the diaminopimelate pathway of lysine biosynthesis Escherichia coli