RNA-3'-phosphate cyclase

RNA-3'-phosphate cyclase
Identifiers
EC number 6.5.1.4
CAS number 85638-41-1
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO

In enzymology, a RNA-3'-phosphate cyclase (EC 6.5.1.4) is an enzyme that catalyzes the chemical reaction

ATP + RNA 3'-terminal-phosphate AMP + diphosphate + RNA terminal-2',3'-cyclic-phosphate

Thus, the two substrates of this enzyme are ATP and RNA 3'-terminal-phosphate, whereas its 3 products are AMP, diphosphate, and RNA terminal-2',3'-cyclic-phosphate.

This enzyme belongs to the family of ligases, specifically those forming phosphoric-ester bonds. The systematic name of this enzyme class is RNA-3'-phosphate:RNA ligase (cyclizing, AMP-forming). This enzyme is also called RNA cyclase.

Structural studies

As of 2010, three structures have been solved for this class of enzymes, with PDB accession codes 1QMH​ and 1QMI​, (un-adenylated)[1] and 3KGD​ (adenylated).[2]

References

  1. ↑ Palm GJ, Billy E, Filipowicz W, Wlodawer A (January 2000). "Crystal structure of RNA 3'-terminal phosphate cyclase, a ubiquitous enzyme with unusual topology". Structure. 8 (1): 13–23. doi:10.1016/S0969-2126(00)00076-9. PMID 10673421.
  2. ↑ Tanaka N, Smith P, Shuman S (March 2010). "Structure of the RNA 3'-phosphate cyclase–adenylate intermediate illuminates nucleotide specificity and covalent nucleotidyl transfer". Structure. 18 (4): 449–57. doi:10.1016/j.str.2010.01.016. PMC 2858066. PMID 20399182.

Further reading

  • Filipowicz W, Konarska M, Gross HJ, Shatkin AJ (1983). "RNA 3'-terminal phosphate cyclase activity and RNA ligation in HeLa cell extract". Nucleic Acids Res. 11 (5): 1405&ndash, 18. doi:10.1093/nar/11.5.1405. PMC 325805. PMID 6828385.
  • Reinberg D, Arenas J, Hurwitz J (1985). "The enzymatic conversion of 3'-phosphate terminated RNA chains to 2',3'-cyclic phosphate derivatives". J. Biol. Chem. 260 (10): 6088&ndash, 97. PMID 2581947.


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