Welcome to Journal of University of Chinese Academy of Sciences,Today is

Inhibition of Two Type of β-Ketoacyl Reductase by Black Tea and Theaflavins

  • DU Ya-Tao ,
  • ZHAO Jiong ,
  • WU Xiao-Dong ,
  • TIAN Wei-Xi
Expand
  • Department of biology, Graduate school of the Chinese Academy of Sciences, Beijing 100049, China

Received date: 2005-01-17

  Revised date: 2005-01-27

  Online published: 2005-11-15

Abstract

Inhibitory activity and character of black tea extract and theaflavins are measured through inhibition kinetics.Based on the kinetics data,both of them are proved to be effective inhibitors of β-ketoacyl reductase of type I fatty acid synthase (KR),which exists in animals and β-ketoacyl reductase of type II fatty acid synthase (FabG),which exists in bacteria.The two inhibitors exhibit potent reversible and irreversible inhibitory activity on KR and FabG and are competitive inhibitors against NADPH,which is one of substrates of KR and FabG.The presence of NADPH clearly prevents the inactivation of KR and FabG by those two inhibitors.This shows that the inhibitors might act on NADPH binding site of KR and FabG.The consistent inhibitory character of two inhibitors suggests that these two β-ketoacyl reductases with different evaluation degrees possess similar active sites.The homology analysis of amino acid sequence shows that there exists one highly homologous region which may be responsible for the formation of active site located in KR and FabG.Therefore,the conformation of the active site in KR can be understood through the study of FabG.These two inhibitors are promising for practical application because of their potent inhibitory activity and rich sources.

Cite this article

DU Ya-Tao , ZHAO Jiong , WU Xiao-Dong , TIAN Wei-Xi . Inhibition of Two Type of β-Ketoacyl Reductase by Black Tea and Theaflavins[J]. Journal of University of Chinese Academy of Sciences, 2005 , 22(6) : 701 -706 . DOI: 10.7523/j.issn.2095-6134.2005.6.007

References

[1] Smith S.The animal fatty acid synthase:one gene,one polypeptide,seven enzymes.Faseb.J.,1994,8 (15):1248~1259.

[2] Rock CO,Jackowski S.Forty years of bacterial fatty acid synthesis.Biochem.Biophys.Res.Commun.,2002,292 (5):1155~1166.

[3] Kuhajda FP.Fattyl-Acid synthase and human cancer:new perspectives on its role in tumor biology.Nutrition,2000,16:202~208.

[4] Loftus TM,Jaworsky DE,Frehywot GL,et al.Reduced food intake and body weight in mice treated with fatty acid synthase inhibitors.Science,2000,288 (5475):2379~2381.

[5] Smith S,Witkowski A,Joshi AK.Structural and functional organization of the animal fatty acid synthase.Prog.Lipid.Res.,2003,42 (4):289~317.

[6] Yang CS,Wang ZY.Tea and cancer.J.Natl.Cancer.Inst.,1993,85 (13):1038~1049.

[7] Tian WX,Hsu RY,Wang YS.Studies on the reactivity of the essential sulfhydryl groups as a conformational probe for the fatty acid synthetase of chicken liver.Inactivation by 5,5'-dithiobis-(2-nitrobenzoic acid) and intersubunit cross-linking of the inactivated enzyme.J.Biol.Chem.,1985,260 (20):11375~11387.

[8] Zhang YM,Rock CO.Evaluation of epigallocatechin gallate and related plant polyphenols as inhibitors of the FabGand FabI reductases of bacterial type II fatty2acid synthase.J.Biol.Chem.,2004,279 (30):30994~31001.

[9] Tian WX,Liang Q,Qu BH,et al.The inhibition of carboxylates to fatty acid synthase of duck.Acta Biophysics Sinica ( China),1992,8 (1):22~28 (in Chinese with English abstract).

[10] Wang X,Tian WX.Green tea epigallocatechin gallate:a natural inhibitor of fatty-acid synthase.Biochem.Biophys.Res.Commun.,2001,288(5):1200~1206.

[11] Stoner GD,Mukhtar H.Polyphenols as cancer chemopreventive agents.J.Cell.Biochem.Suppl.,1995,22:169~180.

[12] Price AC,Zhang YM,Rock CO,et al.Structure of beta-ketoacyl-[acyl carrier protein]reductase from Escherichia coli:negative cooperativity and its structural basis.Biochemistry,2001,40 (43):12772~12781.

Outlines

/