Inhibitive effect of zinc ion on fatty acid synthase from chicken liver

Fan Wang, Xuan Wang, Yu Liu, Wei Xi Tian, Hai Meng Zhou

Research output: Contribution to journalArticlepeer-review

2 Scopus citations


Fatty acid synthase (FAS; acyl-CoA:malonyl-CoA C-acyltransferase [decarboxylating, oxoacyl- and enoyl-reducing and thioester-hydrolyzing], EC is an important enzyme participating in energy metabolism in vivo which is related to adiposis and cancer [Cancer Lett. 167 (1) (2001) 99; Nat. Med. 8 (4) (2002) 335]. Tests of fast- and slow-binding inhibitions showed that fatty acid synthase of chicken liver is rapidly and irreversibly inactivated by low Zn2+ concentrations. Electrophoresis and FPLC results showed that FAS cross-links occurred in the presence of high Zn2+ concentrations (>4 μM) which may be another reason that FAS lost its activity. The modification velocity of FAS by DTNB decreased with increasing Zn2+ concentration, which confirmed that Zn2+ interacted with SH groups. Substrate protective experiments and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) showed that all three substrates tested had some protective effects on FAS in the presence of Zn2+, and malonyl-CoA was the most effective of the three substrates. In the presence of malonyl-CoA, the activity loss of FAS decreased sharply and almost no cross-link was observed in SDS-PAGE. This suggests that the phosphopantetheine SH group is the critical group in the cross-link and inhibition of FAS in the presence of Zn2+.

Original languageEnglish (US)
Pages (from-to)391-400
Number of pages10
JournalInternational Journal of Biochemistry and Cell Biology
Issue number3
StatePublished - Mar 1 2003
Externally publishedYes


  • Cross-linking
  • Fatty acid synthase
  • Inhibition
  • Irreversible
  • Zn

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology


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