RNase PH
Ribonuclease PH | |
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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).
See also
Two highly related exoribonuclease complexes:
- Polynucleotide phosphorylase
- Exosome complex
References
- ^ Ishii R, Nureki O, Yokoyama S (August 2003). "Crystal structure of the tRNA processing enzyme RNase PH from Aquifex aeolicus". The Journal of Biological Chemistry. 278 (34): 32397–404. doi:10.1074/jbc.M300639200. PMID 12746447.
External links
- Crystal structure of Aquifex aeolicus RNase PH at the RCSB Protein Data Bank
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phosphotransferase/kinase
(PO4)
2.7.1: OH acceptor | |
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2.7.2: COOH acceptor | |
2.7.3: N acceptor | |
2.7.4: PO4 acceptor |
(P2O7)
(PO4-nucleoside)
Polymerase |
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Phosphorolytic 3' to 5' exoribonuclease |
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Nucleotidyltransferase | |||||
Guanylyltransferase | |||||
Other |
Phosphatidyltransferases | |
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Glycosyl-1-phosphotransferase |
(PO4; protein acceptor)
2.7.10: protein-tyrosine |
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2.7.11: protein-serine/threonine |
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2.7.12: protein-dual-specificity |
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2.7.13: protein-histidine |
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