Ribonuclease PH | |
---|---|
![]()
Structure of the RNase PH hexamer
| |
Identifiers | |
Symbol | RNASEPH |
Other data | |
EC number | 2.7.7.56 |
RNase PH is a tRNA nucleotidyltransferase, present in archaea and bacteria, that is involved in tRNA processing. Contrary to hydrolytic enzymes, it is a phosphorolytic enzyme, meaning that it uses inorganic phosphate as a reactant to cleave nucleotide-nucleotide bonds, releasing diphosphate nucleotides. The active structure of the proteins is a homohexameric complex, consisting of three ribonuclease (RNase) PH dimers.[1] RNase PH has homologues in many other organisms, which are referred to as RNase PH-like proteins. The part of another larger protein with a domain that is very similar to RNase PH is called an RNase PH domain (RPD).
Two highly related exoribonuclease complexes:
| |||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
2.7.1-2.7.4: phosphotransferase/kinase (PO4) |
| ||||||||||||||
2.7.6: diphosphotransferase (P2O7) |
| ||||||||||||||
2.7.7: nucleotidyltransferase (PO4-nucleoside) |
| ||||||||||||||
2.7.8: miscellaneous |
| ||||||||||||||
2.7.10-2.7.13: protein kinase (PO4; protein acceptor) |
|
| |
---|---|
Activity |
|
Regulation |
|
Classification |
|
Kinetics |
|
Types |
|
![]() | This genetics article is a stub. You can help Wikipedia by expanding it. |