| EC |
3.1.4.58 |
| Accepted name: |
RNA 2′,3′-cyclic 3′-phosphodiesterase |
| Reaction: |
(ribonucleotide)n-2′,3′-cyclic phosphate + H2O = (ribonucleotide)n-2′-phosphate |
| Other name(s): |
thpR (gene name); ligT (gene name) |
| Systematic name: |
(ribonucleotide)n-2′,3′-cyclic phosphate 3′-nucleotidohydrolase |
| Comments: |
The enzyme hydrolyses RNA 2′,3′-cyclic phosphodiester to an RNA 2′-phosphomonoester. In vitro the enzyme can also ligate tRNA molecules with 2′,3′-cyclic phosphate to tRNA with 5′-hydroxyl termini, forming a 2′-5′ phosphodiester linkage. However, the ligase activity is unlikely to be relevant in vivo. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
| References: |
| 1. |
Kanai, A., Sato, A., Fukuda, Y., Okada, K., Matsuda, T., Sakamoto, T., Muto, Y., Yokoyama, S., Kawai, G. and Tomita, M. Characterization of a heat-stable enzyme possessing GTP-dependent RNA ligase activity from a hyperthermophilic archaeon, Pyrococcus furiosus. RNA 15 (2009) 420–431. [DOI] [PMID: 19155324] |
| 2. |
Remus, B.S., Jacewicz, A. and Shuman, S. Structure and mechanism of E. coli RNA 2′,3′-cyclic phosphodiesterase. RNA 20 (2014) 1697–1705. [DOI] [PMID: 25239919] |
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| [EC 3.1.4.58 created 2017] |
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