Burning fat: the structural basis of fatty acid beta-oxidation

Curr Opin Struct Biol. 2002 Dec;12(6):721-8. doi: 10.1016/s0959-440x(02)00390-1.


Recent advances in the structural biology of the enzymes involved in fatty acid oxidation have revealed their catalytic mechanisms and modes of substrate binding. Although these enzymes all use coenzyme A (CoA) thioesters as substrates, they share no common polypeptide folding topology or CoA-binding motif. Each family adopts an entirely unique protein fold. Their mode of binding the CoA thioester is similar in that the fatty-acyl moiety is buried inside the protein and the nucleotide portion is mainly exposed to solvent; however, the conformations of the enzyme-bound CoA ligands vary considerably. Furthermore, a comparison of these structures suggests a structural basis for the broad substrate chain length specificity that is a unique feature of these enzymes.

Publication types

  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Acetyl-CoA C-Acyltransferase / chemistry
  • Acetyl-CoA C-Acyltransferase / metabolism
  • Animals
  • Enoyl-CoA Hydratase / chemistry
  • Enoyl-CoA Hydratase / metabolism
  • Fatty Acid Desaturases / chemistry
  • Fatty Acid Desaturases / metabolism
  • Fatty Acids / metabolism*
  • Humans
  • Mitochondria / metabolism
  • Models, Molecular
  • Oxidation-Reduction
  • Oxidoreductases / chemistry
  • Oxidoreductases / metabolism
  • Protein Structure, Tertiary


  • Fatty Acids
  • Oxidoreductases
  • Fatty Acid Desaturases
  • Acetyl-CoA C-Acyltransferase
  • Enoyl-CoA Hydratase