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Literature summary for 5.3.3.14 extracted from

  • Helmkamp, G.; Rando, R.R.; Brock, D.J.H.; Bloch, K.
    beta-Hydroxydecanoyl thioester dehydrase (1968), J. Biol. Chem., 243, 3229-3231.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
3-decynoyl-N-acetylcysteamine strong inhibition of both dehydrase activity of EC 4.2.1.60 and isomerase activity of enzyme Escherichia coli
3-dodecynoyl-N-acetylcysteamine
-
Escherichia coli
3-nonynoyl-N-acetylcysteamine noncompetitive Escherichia coli
3-octynoyl-N-acetylcysteamine 24% inhibition at 0.005 mM Escherichia coli
3-undecynoyl-N-acetylcysteamine
-
Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
multifunctional enzyme, catalyzing in addition reaction of EC 4.2.1.60
-

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.00013
-
3-decynoyl-N-acetylcysteamine pH 7.0, 30°C, isomerase acitivity Escherichia coli
0.00019
-
3-undecynoyl-N-acetylcysteamine pH 7.0, 30°C, isomerase acitivity Escherichia coli
0.00023
-
3-nonynoyl-N-acetylcysteamine pH 7.0, 30°C, isomerase acitivity Escherichia coli
0.00075
-
3-dodecynoyl-N-acetylcysteamine pH 7.0, 30°C, isomerase acitivity Escherichia coli