tRNA nucleotidyltransferase

From Wikipedia, the free encyclopedia

In enzymology, a tRNA nucleotidyltransferase (EC 2.7.7.56) is an enzyme that catalyzes the chemical reaction

tRNAn⁺1 + phosphate $\rightleftharpoons$ tRNAn + a nucleoside diphosphate

Thus, the two substrates of this enzyme are tRNA(n+1) and phosphate, whereas its two products are tRNA(n) and nucleoside diphosphate.

This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is tRNA:phosphate nucleotidyltransferase. Other names in common use include phosphate-dependent exonuclease, RNase PH, and ribonuclease PH.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, 9 structures have been solved for this class of enzymes, with PDB accession codes 1OYP, 1OYR, 1OYS, 1R6L, 1R6M, 1UDN, 1UDO, 1UDQ, and 1UDS.

[edit] References

IUBMB entry for 2.7.7.56
BRENDA references for 2.7.7.56 (Recommended.)
PubMed references for 2.7.7.56
PubMed Central references for 2.7.7.56
Google Scholar references for 2.7.7.56
Cudny H, Deutscher MP (1988). "3' processing of tRNA precursors in ribonuclease-deficient Escherichia coli. Development and characterization of an in vitro processing system and evidence for a phosphate requirement". J. Biol. Chem. 263: 1518–23. PMID 3275667.
Deutscher MP, Marshall GT, Cudny H (1988). "RNase PH: an Escherichia coli phosphate-dependent nuclease distinct from polynucleotide phosphorylase". Proc. Natl. Acad. Sci. U. S. A. 85: 4710–4. doi:10.1073/pnas.85.13.4710. PMID 2455297.