Singleton Martin R, Wigley Dale B
Cancer Research UK Clare Hall Laboratories, The London Research Institute, Blanche Lane, South Mimms, Potters Bar, Hertfordshire EN6 3LD, UK.
EMBO J. 2003 Sep 15;22(18):4579-83. doi: 10.1093/emboj/cdg441.
Enzymes that operate on nucleic acid substrates are faced with the unusual situation where the substrate is much larger than themselves. Despite the potential to promote catalysis by utilizing the significant binding energy available through their interaction with substrate, ATP hydrolysis is frequently a part of the mechanism of these enzymes. The reasons for this have become clearer in recent years, and a surprising range of ways that these enzymes utilize the free energy of hydrolysis of ATP has been revealed. This review describes these different mechanisms in the context of the biochemical reactions that they support.
作用于核酸底物的酶面临着一种特殊情况,即底物比它们自身大得多。尽管通过与底物相互作用利用大量结合能有促进催化作用的潜力,但ATP水解常常是这些酶作用机制的一部分。近年来,这样做的原因已变得更加清晰,并且已经揭示出这些酶利用ATP水解自由能的一系列惊人方式。本综述在它们所支持的生化反应背景下描述了这些不同机制。