From Wikipedia, the free encyclopedia
 |
| Structure of the RNase PH hexamer |
|
Ribonuclease PH
|
| Identifiers |
| Symbol |
RNASEPH |
| Other data |
| EC number |
2.7.7.56 |
RNase PH is an 3'-5' exoribonuclease and nucleotidyltransferase, present in archaebacteria and eubacteria, that is involved in tRNA processing. Contrary to hydrolytic enzymes, it is a phosphorolytic enzyme, meaning that it uses inorganic phosphate as a cofactor to cleave nucleotide-nucleotide bonds, releasing diphosphate nucleotides. The active structure of the proteins is actually a homohexameric complex, consisting of three RNase PH dimers. [1] RNase PH has homologues in many other organisms, which are referred to as RNase PH-like proteins. When a part of another larger protein has a domain that is very similar to RNase PH, this is called an RNase PH domain (RPD).
[edit] See also
Two highly related exoribonuclease complexes:
[edit] References
- ^ Ishii et al. (2003). "Crystal structure of the tRNA processing enzyme RNase PH from Aquifex aeolicus". J Biol Chem. 278: 32397–404. doi:10.1074/jbc.M300639200. PMID 12746447.
[edit] External links
