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Literature summary for 6.4.1.2 extracted from

  • Evans, A.; Ribble, W.; Schexnaydre, E.; Waldrop, G.L.
    Acetyl-CoA carboxylase from Escherichia coli exhibits a pronounced hysteresis when inhibited by palmitoyl-acyl carrier protein (2017), Arch. Biochem. Biophys., 636, 100-109 .
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
palmitoyl-acyl carrier protein 5 min, 55% inhibition, decrease of inhibition thereafter. Enzyme exhibits a significant hysteresis in presence of palmitoyl-acyl carrier protein. Allosteric inhibitor, the pantothenic acid moiety of palmitoyl-acyl carrier protein is responsible for the inhibition. Competitive with respect to acetyl-CoA Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P0ABD5 and P0A9Q5 P0ABD5 i.e. subunit alpha, P0A9Q5 i.e. subunit beta
-

Synonyms

Synonyms Comment Organism
AccA subunit alpha Escherichia coli
ACCB subunit beta Escherichia coli

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.088
-
palmitoyl-acyl carrier protein pH 7.8, temperature not specified in the publication Escherichia coli