Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Boughton, B.A.; Dobson, R.C.; Gerrard, J.A.; Hutton, C.A.
    Conformationally constrained diketopimelic acid analogues as inhibitors of dihydrodipicolinate synthase (2008), Bioorg. Med. Chem. Lett., 18, 460-463.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.3.3.7 2,2'-benzene-1,3-diylbis(oxoacetic acid)
-
 Escherichia coli
4.3.3.7 dimethyl 2,2'-benzene-1,3-diylbis[(hydroxyimino)ethanoate]
-
 Escherichia coli
4.3.3.7 additional information new constrained inhibitors of DHDPS identified and tested, time-dependent inhibition and substrate protection, dimethyl 2,2'-benzene-1,3-diylbis[(hydroxyimino)ethanoate] discovered as a relatively potent inhibitor of DHDPS enzyme, validates constrained acyclic-intermediate model as a potential inhibitor lead, modifications of the aromatic ring are possible and may result in improvements in activity Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
4.3.3.7 Escherichia coli P0A6L2
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.3.3.7 (S)-aspartate 4-semialdehyde + pyruvate diketopimelic acid derivatives designed as mimics of the acyclic enzyme-bound condensation product of (S)-aspartate 4-semialdehyde and pyruvate, inhibition analysis Escherichia coli dihydrodipicolinate + H2O
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.3.3.7 DHDPS
-
 Escherichia coli

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
4.3.3.7 0.33
-
 dimethyl 2,2'-benzene-1,3-diylbis[(hydroxyimino)ethanoate] 15% inhibition at 1 mM, binding with the active site lysine residue, kinetic analysis corresponds to slow-binding model of inhibition Escherichia coli
4.3.3.7 2.96
-
 2,2'-benzene-1,3-diylbis(oxoacetic acid) 49% inhibition at 5 mM, mimics the substrate pyruvate, binding with the active site lysine residue, slow inhibition Escherichia coli