Burning fat: the structural basis of fatty acid beta-oxidation.
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.
Kim
Jung-Ja P
JJ
Department of Biochemistry, Medical College of Wisconsin, 8701 Watertown Plank Road, Milwaukee 53226, USA. jjkim@mcw.edu
Battaile
Kevin P
KP
D000102:Acetyl-CoA C-Acyltransferase / Q000737:chemistry / Q000378:metabolism; D000818:Animals; D004746:Enoyl-CoA Hydratase / Q000737:chemistry / Q000378:metabolism; D044943:Fatty Acid Desaturases / Q000737:chemistry / Q000378:metabolism; D005227:Fatty Acids / Q000378:metabolism*; D006801:Humans; D008928:Mitochondria / Q000378:metabolism; D008958:Models, Molecular; D010084:Oxidation-Reduction; D010088:Oxidoreductases / Q000737:chemistry / Q000378:metabolism; D017434:Protein Structure, Tertiary
D005227:Fatty Acids; D010088:Oxidoreductases; D044943:Fatty Acid Desaturases; D000102:Acetyl-CoA C-Acyltransferase; D004746:Enoyl-CoA Hydratase