Inhibition of liver acetyl-coenzyme-A carboxylase by 2-tetradecanylglutarate.
- 1 January 1986
- journal article
- research article
- Published by Japan Antibiotics Research Association in The Journal of Antibiotics
- Vol. 39 (2) , 275-280
- https://doi.org/10.7164/antibiotics.39.275
Abstract
In a previous study (A. ENDO, et al., J. Antibiotics 38: 599-604, 1985), 2-alkyl glutarate and its derivatives isolated from cultures of Gongronella butleri were shown to inhibit animal acetyl-CoA carboxylase. In the present communication, the inhibition of liver acetyl-CoA carboxylase was investigated with several 2-alkyl glutarate and 2-alkyl succinate analogs. Their inhibitory potency increased with the chain length of the alkyl moiety, and 2-tetradecanylglutarate was most potent among the inhibitors tested. Kinetic analysis indicated that inhibition by 2-tetradecanylglutarate was non-competitive with respect to the substrates, ATP, HCO3-and acetyl-CoA, and competitive with respect to the allosteric regulator citrate, giving a Ki value of 40 μM. Sucrose density gradient centrifugation analysis showed that the citrate-induced polymerization of the enzyme was inhibited by 2-tetradecanylglutarate.This publication has 1 reference indexed in Scilit:
- Inhibition of Rat-Liver Acetyl-Coenzyme-A Carboxylase by Palmitoyl-Coenzyme A. Formation of Equimolar Enzyme-Inhibitor ComplexEuropean Journal of Biochemistry, 1978