RNA-3'-phosphate cyclase

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

RNA-3′-phosphate cyclase
Identifiers
EC no.6.5.1.4
CAS no.85638-41-1
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins
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

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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

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  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

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[1] [2]


  1. ^ Filipowicz, W. (2016). "RNA 3'-terminal phosphate cyclases and cyclase-like proteins". Postepy Biochemii. 62 (3): 327–334. doi:10.18388/pb.2016_32. PMID 28132487. S2CID 36153563.
  2. ^ Palm, Gottfried J.; Billy, Eric; Filipowicz, Witold; Wlodawer, Alexander (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.