The Enzyme Database

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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. [PMID: 2828310]
[EC 3.1.13.5 created 2006]
 
 


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