| DNA Topoisomerase II (ATP-hydrolyzing) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Structure of the 42 KDa fragment of the N-terminal ATPase and transducer domains of DNA gyrase homologous to all other type IIA topoisomerases. | |||||||||
| Identifiers | |||||||||
| EC no. | 5.6.2.2 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Type II topoisomerases are topoisomerases that cut both strands of the DNA helix simultaneously in order to manage DNA tangles and supercoils. They use the hydrolysis of ATP, unlike Type I topoisomerase. In this process, these enzymes change the linking number of circular DNA by ±2. Topoisomerases are ubiquitous enzymes, found in all living organisms.[1]
In animals, topoisomerase II is a chemotherapy target. In prokaryotes, gyrase is an antibacterial target.[2] Indeed, these enzymes are of interest for a wide range of effects.
- ^ Deweese JE, Osheroff N (February 2009). "The DNA cleavage reaction of topoisomerase II: wolf in sheep's clothing". Nucleic Acids Research. 37 (3): 738–748. doi:10.1093/nar/gkn937. PMC 2647315. PMID 19042970.
- ^ Reece RJ, Maxwell A (1991). "DNA gyrase: structure and function". Critical Reviews in Biochemistry and Molecular Biology. 26 (3–4): 335–375. doi:10.3109/10409239109114072. PMID 1657531.