3.1.13.5: ribonuclease D
This is an abbreviated version!
For detailed information about ribonuclease D, go to the full flat file.
Word Map on EC 3.1.13.5
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3.1.13.5
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rnase
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antiproliferative
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transposon
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trna
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deadenylases
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ccr4-associated
- 3.1.13.5
- rnase
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antiproliferative
- transposon
- trna
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deadenylases
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ccr4-associated
Reaction
exonucleolytic cleavage that removes extra residues from the 3'-terminus of tRNA to produce 5'-mononucleotides =
Synonyms
RNase D
ECTree
3.1.13.5 ribonuclease DAdvanced search results
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results (Substrates Products
Substrates Products on EC 3.1.13.5 - ribonuclease D
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
structurally altered tRNA
5'-mononucleotide + ?
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exonuclease activity. RNase D can recognize structurally altered tRNA molecules. The enzyme acts poorly on intact tRNA and is inactive with the synthetic polyribonucleotides, poly(A), poly(U), or double-stranded poly(A)*poly(U). The enzyme acts on diesterase-treated tRNA, but relatively poorly on intact tRNA. RNase D does not attack ribosomal RNA
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-
?
tRNA containing extra residues at the 3'-terminus
5'-mononucleotide + tRNA
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-
-
-
?
tRNA containing extra residues at the 3'-terminus
5'-mononucleotide + tRNA
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ribonuclease D is not essential for the normal growth of Escherichia coli or bacteriophage T4 or for the biosynthesis of a T4 suppressor tRNA
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-
?
tRNA containing extra residues at the 3'-terminus
5'-mononucleotide + tRNA
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the enzyme can act at the 3'-terminus of tRNA in vivo. RNase D participates in tRNA metabolism
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-
?
additional information
?
-
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enzyme is involved in structured RNA processing
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-
?
additional information
?
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the enzyme may represent an intracellular scavenging mechanism for denatured tRNAs and other inactive RNA molecules
-
-
?
additional information
?
-
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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 as a substrate. The rate of hydrolysis of intact tRNA is very slow compared to tRNAs containing extra residues or compared to tRNAs from which part of the -C-C-A sequence has been removed. Oxidation of the terminal sugar, reduction of the dialdehyde with borohydride, or removal of the terminal AMP from intact tRNA increase the activity of the substrate. Addition of a second -C-C-A sequence gives an active substrate indicating that the relative resistance of intact tRNA to RNase D hydrolysis is not due to the sequence per se but to the structural environment of the 3'-terminus. The enzyme is an exonuclease which initiates hydrolysis at the 3'-terminus and removes 5'-mononucleotides in a random fashion
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?
additional information
?
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in vitro, TbRND exhibits 3' to 5' exoribonuclease activity, with specificity toward uridine homopolymers, including the 3' oligo(U) tails of guide RNAs that provide the sequence information for RNA editing
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-
?
additional information
?
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in vitro, TbRND exhibits 3' to 5' exoribonuclease activity, with specificity toward uridine homopolymers, including the 3' oligo(U) tails of guide RNAs that provide the sequence information for RNA editing
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?
