Evaluation of inhibition of fatty acid synthase by ursolic acid: positive cooperation mechanism

Biochem Biophys Res Commun. 2010 Feb 12;392(3):386-90. doi: 10.1016/j.bbrc.2010.01.031. Epub 2010 Jan 13.

Abstract

The inhibitory effect of ursolic acid (UA) on fatty acid synthase (FAS, EC 2.3.1.85) was investigated. We found that UA potently inhibited the activity of FAS with a half-inhibitory concentration value (IC(50)) of 6.0 microg/ml. The inhibition kinetic results showed that the inhibition of FAS by UA was competitive against acetyl-CoA and malonyl-CoA, but uncompetitive to NADPH. UA at low concentration slowly inactivated FAS, but FAS was fast inactivated by high concentration of UA in a positive cooperative manner. Moreover, NADPH significantly enhanced the inactivation of FAS by low concentration of UA, but NADPH slightly decreased the inactivation of FAS by high concentration of UA. Taken together, the results suggest that ursolic acid decreases the FAS activity through inactivation of acetyl/malonyl transferase. The combination of NADPH and KR domain promotes the inhibitory effect of UA on FAS.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antineoplastic Agents, Phytogenic / pharmacology*
  • Fatty Acid Synthases / antagonists & inhibitors*
  • Fatty Acid Synthases / metabolism
  • Hypolipidemic Agents / pharmacology*
  • Inhibitory Concentration 50
  • NADP / metabolism
  • Triterpenes / pharmacology*
  • Ursolic Acid

Substances

  • Antineoplastic Agents, Phytogenic
  • Hypolipidemic Agents
  • Triterpenes
  • NADP
  • Fatty Acid Synthases