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Literature summary extracted from

  • Kramer, P.R.; Miziorko, H.M.
    3-Hydroxy-3-methylglutaryl-CoA lyase: catalysis of acetyl coenzyme A enolization (1983), Biochemistry, 22, 2353-2357.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.1.3.4 3-hydroxyglutaryl-CoA Ki: 0.05 mM, Ki of acetyl-CoA enolization: 0.095 mM Anas sp.
4.1.3.4 S-(4-carboxy-3hydroxyisoamyl)-CoA Ki: 0.08 mM Anas sp.

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.1.3.4 Mg2+ possibly involved in coordination of the thioesther carbonyl during catalysis, also stimulates acetyl-CoA enolization Anas sp.

Organism

EC Number Organism UniProt Comment Textmining
4.1.3.4 Anas sp.
-
 duck
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
4.1.3.4 liver
-
 Anas sp.
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.3.4 (S)-3-Hydroxy-3-methylglutaryl-CoA mechanism Anas sp. Acetyl-CoA + acetoacetate
-
 ?
4.1.3.4 Acetyl-CoA enolization Anas sp. ?
-
 ?

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
4.1.3.4 0.05
-
 3-hydroxyglutaryl-CoA
-
 Anas sp.
4.1.3.4 0.08
-
 S-(4-carboxy-3hydroxyisoamyl)-CoA
-
 Anas sp.