The activity of the enzyme acyl-CoA oxidase (EC 184.108.40.206) is influenced by detergents. At concentrations above the critical micellar concentration, Triton X-100, Triton X-114 and Thesit stimulate oxidase activity. Lower concentrations of Triton X-100 and Triton X-114 render the acyl-CoA oxidase less sensitive towards substrate inhibition by palmitoyl-CoA or dec-4-cis-enoyl-CoA. Other detergents inhibited the enzyme activity. CoA was found to be a relatively powerful competitive inhibitor of the enzyme, with a Ki, slope value of 63 +/- 3 microM. This inhibition is dependent on an intact CoA molecule, as dephospho-CoA, dethio-CoA and acetyl-CoA are less potent inhibitors of the enzyme. Dec-2-trans-enoyl-CoA is a product-inhibitor of acyl-CoA oxidase, with a Ki, slope value of 7 +/- 1 microM.
Skip Nav Destination
Research Article| February 15 1993
Factors which affect the activity of purified rat liver acyl-CoA oxidase
R Hovik ;
Biochem J (1993) 290 (1): 97–102.
- Views Icon Views
- Share Icon Share
R Hovik, H Osmundsen; Factors which affect the activity of purified rat liver acyl-CoA oxidase. Biochem J 15 February 1993; 290 (1): 97–102. doi: https://doi.org/10.1042/bj2900097
Download citation file:
Don't already have an account? Register
Get Access To This Article
Buy This Article