EC |
3.1.13.5 |
Accepted name: |
ribonuclease D |
Reaction: |
Exonucleolytic cleavage that removes extra residues from the 3′-terminus of tRNA to produce 5′-mononucleotides |
Other name(s): |
RNase D |
Comments: |
Requires divalent cations for activity (Mg2+, Mn2+ or Co2+). Alteration of the 3′-terminal base has no effect on the rate of hydrolysis whereas modification of the 3′-terminal sugar has a major effect. tRNA terminating with a 3′-phosphate is completely inactive [3]. This enzyme can convert a tRNA precursor into a mature tRNA [2]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Ghosh, R.K. and Deutscher, M.P. Identification of an Escherichia coli nuclease acting on structurally altered transfer RNA molecules. J. Biol. Chem. 253 (1978) 997–1000. [PMID: 342522] |
2. |
Cudny, H., Zaniewski, R. and Deutscher, M.P. Escherichia coli RNase D. Purification and structural characterization of
a putative processing nuclease. J. Biol. Chem. 256 (1981) 5627–5632. [PMID: 6263885] |
3. |
Cudny, H., Zaniewski, R. and Deutscher, M.P. Escherichia coli RNase D. Catalytic properties and substrate specificity. J. Biol. Chem. 256 (1981) 5633–5637. [PMID: 6263886] |
4. |
Zhang, J.R. and Deutscher, M.P. Cloning, characterization, and effects of overexpression of the Escherichia coli rnd gene encoding RNase D. J. Bacteriol. 170 (1988) 522–527. [DOI] [PMID: 2828310] |
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[EC 3.1.13.5 created 2006] |
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