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Literature summary for 4.3.3.7 extracted from

  • Phenix, C.P.; Palmer, D.R.
    Isothermal titration microcalorimetry reveals the cooperative and noncompetitive nature of inhibition of Sinorhizobium meliloti L5-30 dihydrodipicolinate synthase by (S)-lysine (2008), Biochemistry, 47, 7779-7781.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
(S)-lysine no significant conformational change between the pyruvate-bound and (S)-lysine-bound enzyme, presence of substrate has substantial effect on the nature of enzyme-inhibitor association, solvent plays a key role in binding of inhibitor Sinorhizobium meliloti

Organism

Organism UniProt Comment Textmining
Sinorhizobium meliloti Q07607 L5-30
-
Sinorhizobium meliloti L5-30 Q07607 L5-30
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
titration of (S)-lysine into buffered solutions of MosA protein in the presence or absence of saturating amounts of pyruvate, thermodynamic data for (S)-Lysine binding to MosA protein, non-competitive mechanism with substrate-dependent differences in the energetics of inhibitor binding Sinorhizobium meliloti

Synonyms

Synonyms Comment Organism
DHDPS
-
Sinorhizobium meliloti
MosA protein
-
Sinorhizobium meliloti