Kim Jung-Ja P, Battaile Kevin P
Department of Biochemistry, Medical College of Wisconsin, 8701 Watertown Plank Road, Milwaukee 53226, USA.
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.
参与脂肪酸氧化的酶的结构生物学的最新进展揭示了它们的催化机制和底物结合模式。尽管这些酶都使用辅酶A(CoA)硫酯作为底物,但它们没有共同的多肽折叠拓扑结构或CoA结合基序。每个家族都采用完全独特的蛋白质折叠方式。它们结合CoA硫酯的模式相似,即脂肪酰基部分埋在蛋白质内部,核苷酸部分主要暴露于溶剂中;然而,与酶结合的CoA配体的构象差异很大。此外,这些结构的比较为这些酶独特的广泛底物链长特异性提供了结构基础。