New EMBO Members Review
- The EMBO Journal (2003) 22, 4579 - 4583
- doi:10.1093/emboj/cdg441
Subject Category:
Multiple roles for ATP hydrolysis in nucleic acid modifying enzymes
Martin R. Singleton1 and Dale B. Wigley1
- Cancer Research UK Clare Hall Laboratories, The London Research Institute, Blanche Lane, South Mimms, Potters Bar, Hertfordshire EN6 3LD, UK
Correspondence to:
Dale B. Wigley, E-mail: Dale.Wigley@cancer.org.uk
Received 24 April 2003; Accepted 17 July 2003; Revised 17 July 2003
Abstract
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.
Keywords:
- ATP hydrolysis,
- binding energy,
- catalysis,
- nucleic acid modifying enzymes



